5 hits
XFF4834R_chr04400 | XFF4834R_chr_0507356_0508495_f2_XFF4834R-XFF4834R_chr04400 | XFF4834R_chr04400 | putative tryptophan 2,3-dioxygenase |
XFF4834R_chr16360 | XFF4834R_chr17640403_1893920_f3_XFF4834R-XFF4834R_chr16360 | XFF4834R_chr16360 | probable tryptophan halogenase |
XFF4834R_chr29100 | XFF4834R_chr31610984_3344514_f1_XFF4834R-XFF4834R_chr29100 | XFF4834R_chr29100 | putative 3-hydroxyanthranilate 3,4-dioxygenase |
XFF4834R_chr29120 | XFF4834R_chr31640741_3348012_f1_XFF4834R-XFF4834R_chr29120 | XFF4834R_chr29120 | Putative kynureninase |
XFF4834R_chr29130 | XFF4834R_chr31660184_3349551_f1_XFF4834R-XFF4834R_chr29130 | XFF4834R_chr29130 | probable kynurenine 3-monooxygenase |
![]() XFF4834R_chr_0485 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr04410 |
ID | XFF4834R_chr_0507356_0508495_f2_XFF4834R-XFF4834R_chr04400 |
AC | XFF4834R_chr04400 |
LT | XFF4834R_chr04400 |
OR | XFF4834R_chr from 507599 to 508495 on strand + |
DE | putative tryptophan 2,3-dioxygenase |
IP | Tryptophan 2,3-dioxygenase |
CL | 1.1.3.8 Tryptophan utilization GO:0006569 |
EC | |
GO |
InterPro 3-dioxygenase activity (GO:0004833) Biological Process: oxidation reduction (GO:0055114) Biological Process: tryptophan catabolic process to kynurenine (GO:0019441) Molecular Function: oxidoreductase activity (GO:0016491) Molecular Function: iron ion binding (GO:0005506) Curated
|
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by darrasse (20120319) |
MW | 34430.8 Da |
SQ | 298 aa |
........10........20........30........40........50 |
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YP_362209.1 XCV0478 |
1 |
298 |
S=1567 I=99 E=0 |
tryptophan 2,3-dioxygenase |
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NP_635826.1 XCC0432 |
1 |
297 |
S=1516 I=96 E=1.05237e-176 |
tryptophan 2,3-dioxygenase |
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NP_640803.1 XAC0448-XAC0448 |
1 |
296 |
S=1500 I=96 E=1.14632e-174 |
tryptophan 2,3-dioxygenase |
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XALc_2742 XALc_2742 |
1 |
285 |
S=1294 I=86 E=1.03791e-149 |
probable tryptophan 2,3-dioxygenase protein |
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NP_636584.1 XCC1210 |
220 |
298 |
S=135 I=41 E=2.22753e-09 |
tryptophan 2,3-dioxygenase |
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1 |
297 |
S=1516 I=96 E=4.34273e-175 |
Tryptophan 2,3-dioxygenase EC=1.13.11.11 ; Heme Iron Metal-binding Oxidoreductase catabolism |
Pubmed 17197414 |
|
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13 |
282 |
S=644 I=48 E=2.14031e-69 |
Tryptophan 2,3-dioxygenase EC=1.13.11.11 ; Heme Iron Metal-binding Oxidoreductase catabolism |
||
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17 |
282 |
S=567 I=44 E=4.26711e-60 |
Tryptophan 2,3-dioxygenase EC=1.13.11.11 ; Heme Iron Metal-binding Oxidoreductase catabolism |
Pubmed 15066027 |
|
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17 |
191 |
S=407 I=51 E=1.08636e-40 |
ORF1 ; Plasmid |
||
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24 |
282 |
S=396 I=36 E=2.52872e-39 |
SibP |
Pubmed 19270142 |
|
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1 |
298 |
S=1567 I=99 E=0 |
Tryptophan 2,3-dioxygenase EC=1.13.11.11 ; Heme Iron Metal-binding Oxidoreductase catabolism |
||
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1 |
297 |
S=1516 I=96 E=2.95651e-175 |
Tryptophan 2,3-dioxygenase EC=1.13.11.11 ; Heme Iron Metal-binding Oxidoreductase catabolism |
||
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1 |
297 |
S=1516 I=96 E=2.95651e-175 |
Tryptophan 2,3-dioxygenase EC=1.13.11.11 ; Heme Iron Metal-binding Oxidoreductase catabolism |
||
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1 |
297 |
S=1516 I=96 E=2.95651e-175 |
Tryptophan 2,3-dioxygenase EC=1.13.11.11 ; Heme Iron Metal-binding Oxidoreductase catabolism |
||
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1 |
296 |
S=1500 I=96 E=3.22047e-173 |
Tryptophan 2,3-dioxygenase EC=1.13.11.11 ; Heme Iron Metal-binding Oxidoreductase catabolism |
||
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IPR004981 [PTHR10138] | 12 |
291 |
Tryptophan 2,3-dioxygenase |
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IPR004981 [PF03301] | 18 |
144 |
Tryptophan 2,3-dioxygenase |
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IPR004981 [PF03301] | 208 |
281 |
Tryptophan 2,3-dioxygenase |
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86 |
178 |
S=249 I=54 E=1.08965e-22 |
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22 |
83 |
S=191 I=66 E=1.10235e-15 |
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209 |
276 |
S=181 I=51 E=1.94124e-14 |
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192 |
219 |
S=150 I=96 E=9.71618e-11 |
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274 |
298 |
S=126 I=96 E=7.20554e-08 |
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140 |
191 |
S=116 I=52 E=1.16295e-06 |
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1 |
21 |
S=111 I=100 E=4.85902e-06 |
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136 |
282 |
S=102 I=35 E=6.47352e-05 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr16350 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr16370 |
ID | XFF4834R_chr17640403_1893920_f3_XFF4834R-XFF4834R_chr16360 |
AC | XFF4834R_chr16360 |
LT | XFF4834R_chr16360 |
OR | XFF4834R_chr from 1892403 to 1893920 on strand + |
DE | probable tryptophan halogenase |
IP | Tryptophan halogenase |
CL | 1.1.3.8 Tryptophan utilization GO:0006569 |
EC | |
GO |
InterPro Curated |
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by jacques (20110310) |
MW | 56889.4 Da |
SQ | 505 aa |
........10........20........30........40........50 |
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XFF4834R_chr39170 lcl|XFF4834R_chr42380214_4513779_f1_XFF4834R-XFF4834R_chr39170 |
3 |
490 |
S=1211 I=48 E=5.13973e-140 |
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XFF4834R_chr41410 lcl|XFF4834R_chr_4816198_4817718_f1_XFF4834R-XFF4834R_chr41410 |
1 |
492 |
S=1192 I=48 E=1.08606e-137 |
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NP_643304.1 lcl|prnA-XAC2995 |
1 |
505 |
S=2480 I=93 E=0 |
tryptophan halogenase |
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YP_364875.1 lcl|XCV3144 |
1 |
505 |
S=2473 I=93 E=0 |
tryptophan halogenase |
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NP_638173.1 lcl|prnA-XCC2825 |
1 |
498 |
S=1862 I=71 E=0 |
tryptophan halogenase |
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5 |
505 |
S=1783 I=68 E=0 |
putative tryptophan halogenase protein |
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NP_644350.1 lcl|prnA-XAC4051 |
3 |
492 |
S=1223 I=48 E=6.88233e-141 |
tryptophan halogenase |
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NP_639305.1 lcl|prnA-XCC3966 |
2 |
490 |
S=1219 I=48 E=1.84336e-140 |
tryptophan halogenase |
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YP_365872.1 lcl|XCV4141 |
3 |
490 |
S=1215 I=48 E=6.6409e-140 |
tryptophan halogenase |
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35 |
492 |
S=1207 I=51 E=5.38255e-139 |
putative tryptophan halogenase protein |
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NP_639472.1 lcl|prnA-XCC4133 |
1 |
492 |
S=1202 I=47 E=2.51883e-138 |
tryptophan halogenase |
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YP_366108.1 lcl|XCV4377 |
1 |
492 |
S=1194 I=48 E=2.09566e-137 |
putative tryptophan halogenase |
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6 |
401 |
S=609 I=38 E=6.45578e-65 |
Tryptophan halogenase |
Pubmed 10547442 |
|
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6 |
401 |
S=587 I=35 E=3.15041e-62 |
PrnA Tryptophan halogenase |
||
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6 |
401 |
S=587 I=36 E=3.46752e-62 |
Tryptophan halogenase |
Pubmed 10547442 |
|
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5 |
486 |
S=584 I=32 E=7.73352e-62 |
Tryptophan halogenase |
Pubmed 10547442 |
|
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6 |
451 |
S=575 I=34 E=9.44287e-61 |
Tryptophan 5-halogenase |
Pubmed 15850981 |
|
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3 |
405 |
S=568 I=34 E=6.48517e-60 |
Putative tryptophan halogenase |
Pubmed 16873021 |
|
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6 |
401 |
S=560 I=36 E=6.20335e-59 |
Tryptophan halogenase |
Pubmed 10547442 |
|
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3 |
407 |
S=558 I=33 E=8.86897e-59 |
Halogenase Putative halogenase of tryptophan Putative tryptophan halogenase Tryptophan halogenase |
||
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6 |
401 |
S=547 I=35 E=2.08251e-57 |
Tryptophan halogenase PrnA |
Pubmed 9172332 |
|
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25 |
408 |
S=534 I=35 E=8.84678e-56 |
KtzR |
Pubmed 17940045 |
|
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IPR006905 [PF04820] | 8 |
458 |
Tryptophan halogenase |
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[PS51257] | 1 |
23 |
- |
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[seg] | 12 |
24 |
- |
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[seg] | 409 |
422 |
- |
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276 |
480 |
S=437 I=44 E=2.64799e-45 |
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200 |
281 |
S=330 I=73 E=2.06998e-32 |
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89 |
191 |
S=264 I=50 E=2.14782e-24 |
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31 |
85 |
S=205 I=65 E=2.89725e-17 |
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481 |
505 |
S=138 I=100 E=4.22368e-09 |
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282 |
308 |
S=134 I=96 E=1.08301e-08 |
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151 |
398 |
S=116 I=21 E=1.9561e-06 |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
12 hits |
![]() |
Swiss-Prot ncbi-blastp |
1 hits |
![]() |
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
2 hits |
![]() |
HAMAP scan |
0 hits |
![]() |
IprScan |
4 hits |
Miscellaneous analyses
![]() XFF4834R_chr29090 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr29110 |
ID | XFF4834R_chr31610984_3344514_f1_XFF4834R-XFF4834R_chr29100 |
AC | XFF4834R_chr29100 |
LT | XFF4834R_chr29100 |
OR | XFF4834R_chr from 3343984 to 3344514 on strand + |
DE | putative 3-hydroxyanthranilate 3,4-dioxygenase |
IP | 3-hydroxyanthranilic acid dioxygenase |
CL | 1.1.3.8 Tryptophan utilization GO:0006569 |
EC | |
GO |
InterPro 4-dioxygenase activity (GO:0000334) Biological Process: oxidation reduction (GO:0055114) Biological Process: metabolic process (GO:0008152) Molecular Function: iron ion binding (GO:0005506) Curated |
PM | |
AN | |
CC | COG: [G] Carbohydrate transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by elauber (20100716) |
MW | 20187 Da |
SQ | 176 aa |
........10........20........30........40........50 |
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YP_363376.1 lcl|XCV1645 |
1 |
176 |
S=931 I=99 E=3.66263e-106 |
3-hydroxyanthranilate 3,4-dioxygenase |
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NP_641935.1 lcl|haaO-XAC1603 |
1 |
175 |
S=911 I=98 E=1.07794e-103 |
3-hydroxyanthranilate 3,4-dioxygenase |
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NP_636926.1 lcl|haaO-XCC1555 |
1 |
175 |
S=889 I=92 E=5.68973e-101 |
3-hydroxyanthranilate 3,4-dioxygenase |
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1 |
165 |
S=676 I=73 E=3.7607e-75 |
putative 3-hydroxyanthranilate 3,4-dioxygenase protein |
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1 |
164 |
S=428 I=46 E=1.34939e-43 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Cytoplasm Iron Metal-binding Oxidoreductase Pyridine nucleotide biosynthesis |
Pubmed 18460219 |
|
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5 |
167 |
S=421 I=48 E=1.06547e-42 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Iron Metal-binding Oxidoreductase |
Pubmed 12620844 |
|
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5 |
167 |
S=414 I=50 E=7.00528e-42 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Iron Metal-binding Oxidoreductase Plasmid |
||
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6 |
157 |
S=409 I=49 E=2.70604e-41 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Cytoplasm Iron Metal-binding Oxidoreductase Phosphoprotein Pyridine nucleotide biosynthesis |
Pubmed 18630941 |
|
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6 |
157 |
S=402 I=49 E=1.77918e-40 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Alternative splicing Cytoplasm Iron Metal-binding Oxidoreductase Polymorphism Pyridine nucle |
Pubmed 7514594 |
|
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1 |
176 |
S=931 I=99 E=9.26316e-105 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Iron Metal-binding Oxidoreductase |
||
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1 |
175 |
S=911 I=98 E=2.72622e-102 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Iron Metal-binding Oxidoreductase |
||
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1 |
176 |
S=899 I=94 E=7.35969e-101 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Iron Metal-binding Oxidoreductase |
||
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1 |
176 |
S=899 I=94 E=7.35969e-101 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Iron Metal-binding Oxidoreductase |
||
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1 |
175 |
S=889 I=92 E=1.43899e-99 |
3-hydroxyanthranilate 3,4-dioxygenase EC=1.13.11.6 ; Iron Metal-binding Oxidoreductase |
||
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[MF_00825] | 1 |
170 |
- |
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IPR010329 [PF06052] | 3 |
150 |
3-hydroxyanthranilic acid dioxygenase |
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IPR010329 [TIGR03037] | 6 |
163 |
3-hydroxyanthranilic acid dioxygenase |
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1 |
167 |
S=538 I=61 E=1.1475e-57 |
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IPR011051 [SSF51182] | 3 |
139 |
Cupin, RmlC-type |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
9 hits |
![]() |
Swiss-Prot ncbi-blastp |
56 hits |
![]() |
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
![]() |
HAMAP scan |
0 hits |
![]() |
IprScan |
4 hits |
Miscellaneous analyses
![]() XFF4834R_chr29110 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr29130 |
ID | XFF4834R_chr31640741_3348012_f1_XFF4834R-XFF4834R_chr29120 |
AC | XFF4834R_chr29120 |
LT | XFF4834R_chr29120 |
OR | XFF4834R_chr from 3346741 to 3348012 on strand + |
DE | Putative kynureninase |
IP | Aminotransferase, class V/Cysteine desulfurase; Kynureninase; Pyridoxal phosphate-dependent transferase, major region, subdomain 1 |
CL | 1.1.3.8 Tryptophan utilization GO:0006569 |
EC | |
GO |
InterPro Biological Process: tryptophan catabolic process (GO:0006569) Biological Process: metabolic process (GO:0008152) Biological Process: NAD biosynthetic process (GO:0009435) Cellular Component: cytoplasm (GO:0005737) Molecular Function: pyridoxal phosphate binding (GO:0030170) Molecular Function: catalytic activity (GO:0003824) Molecular Function: kynureninase activity (GO:0030429) Curated |
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by darrasse (20120404) |
MW | 45862.8 Da |
SQ | 423 aa |
........10........20........30........40........50 |
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XFF4834R_chr00700 lcl|XFF4834R_chr00700474_0083655_f1_XFF4834R-XFF4834R_chr00700 |
77 |
290 |
S=99 I=26 E=2.10729e-05 |
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XFF4834R_chr00700 lcl|XFF4834R_chr00700474_0083655_f1_XFF4834R-XFF4834R_chr00700 |
77 |
290 |
S=99 I=26 E=2.10729e-05 |
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26 |
413 |
S=1019 I=47 E=1.03989e-114 |
Kynureninase EC=3.7.1.3 ; Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
Pubmed 17592475 |
|
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26 |
413 |
S=979 I=45 E=9.16566e-110 |
Kynureninase EC=3.7.1.3 ; Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
Pubmed 17107561 |
|
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32 |
419 |
S=880 I=43 E=7.89274e-98 |
Kynureninase EC=3.7.1.3 ; Cytoplasm Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
Pubmed 17615350 |
|
![]() |
32 |
418 |
S=871 I=46 E=9.47069e-97 |
Kynureninase EC=3.7.1.3 ; Cytoplasm Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
Pubmed 18273011 |
|
![]() |
31 |
414 |
S=854 I=45 E=1.03162e-94 |
Kynureninase 1 EC=3.7.1.3 ; Cytoplasm Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
Pubmed 18024570 |
|
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31 |
413 |
S=835 I=43 E=2.25726e-92 |
Kynureninase EC=3.7.1.3 ; Acetylation Cytoplasm Disease mutation Hydrolase Polymorphism Pyridine nucleotide biosynthesis Pyridoxal phosphate |
||
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33 |
419 |
S=827 I=42 E=2.17807e-91 |
Kynureninase EC=3.7.1.3 ; Acetylation Cytoplasm Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
||
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38 |
415 |
S=785 I=44 E=2.4937e-86 |
Kynureninase 2 EC=3.7.1.3 ; Cytoplasm Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
Pubmed 17259976 |
|
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32 |
414 |
S=770 I=42 E=1.48838e-84 |
Kynureninase 2 EC=3.7.1.3 ; Cytoplasm Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
Pubmed 18024570 |
|
![]() |
33 |
418 |
S=760 I=40 E=2.59829e-83 |
Kynureninase EC=3.7.1.3 ; Cytoplasm Hydrolase Nucleus Pyridine nucleotide biosynthesis Pyridoxal phosphate |
Pubmed 12062417 |
|
![]() |
1 |
423 |
S=1963 I=90 E=0 |
Kynureninase EC=3.7.1.3 ; Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
||
![]() |
1 |
423 |
S=1948 I=89 E=0 |
Kynureninase EC=3.7.1.3 ; Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
||
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1 |
423 |
S=1882 I=86 E=0 |
Kynureninase EC=3.7.1.3 ; Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
||
![]() |
1 |
423 |
S=1874 I=86 E=0 |
Kynureninase EC=3.7.1.3 ; Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
||
![]() |
1 |
423 |
S=1873 I=86 E=0 |
Kynureninase EC=3.7.1.3 ; Hydrolase Pyridine nucleotide biosynthesis Pyridoxal phosphate |
||
![]() |
IPR015421 [G3DSA:3.40.640.10] | 48 |
320 |
Pyridoxal phosphate-dependent transferase, major region, subdomain 1 |
![]() |
IPR010111 [PTHR14084] | 3 |
423 |
Kynureninase |
![]() |
IPR000192 [PF00266] | 75 |
371 |
Aminotransferase, class V/Cysteine desulfurase |
![]() |
IPR010111 [TIGR01814] | 10 |
422 |
Kynureninase |
![]() |
[seg] | 7 |
25 |
- |
![]() |
[seg] | 302 |
316 |
- |
![]() |
38 |
139 |
S=232 I=47 E=1.43696e-20 |
![]() |
204 |
273 |
S=192 I=54 E=1.02741e-15 |
![]() |
350 |
418 |
S=160 I=51 E=7.35201e-12 |
![]() |
141 |
201 |
S=158 I=52 E=1.31857e-11 |
![]() |
278 |
343 |
S=110 I=37 E=7.9124e-06 |
![]() |
IPR015424 [SSF53383] | 5 |
420 |
Pyridoxal phosphate-dependent transferase, major domain |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
19 hits |
![]() |
Swiss-Prot ncbi-blastp |
85 hits |
![]() |
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
1 hits |
![]() |
HAMAP scan |
0 hits |
![]() |
IprScan |
7 hits |
Miscellaneous analyses
![]() XFF4834R_chr29120 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr29140 |
ID | XFF4834R_chr31660184_3349551_f1_XFF4834R-XFF4834R_chr29130 |
AC | XFF4834R_chr29130 |
LT | XFF4834R_chr29130 |
OR | XFF4834R_chr from 3348184 to 3349551 on strand + |
DE | probable kynurenine 3-monooxygenase |
IP | FAD dependent oxidoreductase |
CL | 1.1.3.8 Tryptophan utilization GO:0006569 |
EC | |
GO |
InterPro Molecular Function: oxidoreductase activity (GO:0016491) Curated |
PM | |
AN | pubmed : Kynurenine 3-monooxygenase (KMO) is an NADPH-dependent flavoprotein hydroxylase that catalyzes the conversion of l-Kynurenine (L-Kyn) to 3-hydroxykynurenine (3OHKyn). The reaction is central to the tryptophan degradative pathway and takes place within microglial cells defining cellular concentrations of the N-methyl-d-aspatate (NMDA) receptor agonist quinolinate and antagonist kynurenate. The Pseudomonas siderophore quinolobactin is synthesized from xanthurenic acid, an intermediate of the kynurenine pathway. pyridine nucleotide biosynthetic process Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. Siderophore biosynthesis; quinolobactin biosynthesis. |
CC | COG: [CH] Energy production and conversion;Coenzyme transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by darrasse (20120404) |
MW | 50810.1 Da |
SQ | 455 aa |
........10........20........30........40........50 |
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NP_641932.1 lcl|XAC1600-XAC1600 |
1 |
455 |
S=2046 I=87 E=0 |
kynurenine 3-monooxygenase |
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YP_363372.1 lcl|XCV1641 |
1 |
455 |
S=2019 I=85 E=0 |
putative kynurenine 3-monooxygenase |
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NP_636923.1 lcl|XCC1552 |
2 |
455 |
S=1878 I=79 E=0 |
kynurenine 3-monooxygenase |
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5 |
454 |
S=1654 I=70 E=0 |
putative kynurenine 3-monooxygenase oxidoreductase protein |
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26 |
452 |
S=969 I=49 E=1.50384e-108 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
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27 |
427 |
S=646 I=36 E=2.11776e-69 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
Pubmed 17592475 |
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27 |
427 |
S=633 I=36 E=7.49129e-68 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
Pubmed 17107561 |
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26 |
422 |
S=628 I=35 E=2.58369e-67 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; Alternative splicing FAD Flavoprotein Membrane Mitochondrion outer NADP Oxidoreductase Phosphoprotein P |
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27 |
425 |
S=621 I=35 E=2.16844e-66 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; Alternative splicing FAD Flavoprotein Membrane Mitochondrion NADP Oxidoreductase Pyridine nucleotide bi |
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27 |
422 |
S=617 I=37 E=6.33706e-66 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
Pubmed 14700627 |
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26 |
422 |
S=614 I=36 E=1.48924e-65 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein Membrane Mitochondrion outer NADP Oxidoreductase Phosphoprotein Pyridine nucleotide biosyn |
Pubmed 1332540 |
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26 |
425 |
S=614 I=36 E=1.54209e-65 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein Membrane Mitochondrion outer NADP Oxidoreductase Phosphoprotein Pyridine nucleotide biosynthesis |
Pubmed 10721109 |
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27 |
430 |
S=591 I=35 E=9.19643e-63 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein Membrane Mitochondrion NADP Oxidoreductase Pyridine nucleotide biosynthesis Transmembrane |
Pubmed 12364791 |
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27 |
454 |
S=588 I=34 E=1.86349e-62 |
Kynurenine 3-monooxygenase |
Pubmed 12230548 |
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1 |
455 |
S=2046 I=87 E=0 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
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1 |
455 |
S=2019 I=85 E=0 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
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1 |
455 |
S=1989 I=84 E=0 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
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1 |
455 |
S=1987 I=84 E=0 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
||
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1 |
455 |
S=1987 I=84 E=0 |
Kynurenine 3-monooxygenase EC=1.14.13.9 ; FAD Flavoprotein NADP Oxidoreductase Pyridine nucleotide biosynthesis |
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44 |
104 |
S=307 I=98 E=1.12717e-29 |
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364 |
446 |
S=239 I=58 E=2.06131e-21 |
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227 |
285 |
S=186 I=62 E=4.61437e-15 |
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172 |
226 |
S=135 I=48 E=8.16292e-09 |
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30 |
80 |
S=132 I=55 E=2.0038e-08 |
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206 |
240 |
S=119 I=60 E=7.15027e-07 |
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26 |
74 |
S=108 I=51 E=1.33841e-05 |
Access unfiltered results
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Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
66 hits |
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Swiss-Prot ncbi-blastp |
54 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
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HAMAP scan |
0 hits |
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IprScan |
0 hits |
Miscellaneous analyses