Xanthomonas fuscans subsp. fuscans

S=1366 I=97 E=4.8574e-157

S-adenosyl methionine decarboxylase proenzyme ; Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff base Spermidine

Pubmed 17574998

prodomImg

Q7WZ08 sp|Q7WZ08|Q7WZ08_LYSEN

S=1283 I=89 E=6.59312e-147

S-adenosylmethionine decarboxylase SpeD ; Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff base Spermidine

Pubmed 15640196

prodomImg

Q540E1 sp|Q540E1|Q540E1_SALTY

263

S=925 I=65 E=1.39406e-103

S-adenosylmethionine decarboxylase proenzyme EC=4.1.1.50 ; Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff base Spermidine

Pubmed 11526206

prodomImg

P0A7F6 sp|P0A7F6|SPED_ECOLI

262

S=919 I=65 E=8.25521e-103

S-adenosylmethionine decarboxylase proenzyme EC=4.1.1.50 ; Allosteric Autocatalytic cleavage Lyase Magnesium Polyamine biosynthesis Pyruvate S-ad

Pubmed 3316212,8202364

prodomImg

B0TI92 sp|B0TI92|SPED_HELMI

262

S=877 I=62 E=1.00463e-97

S-adenosylmethionine decarboxylase proenzyme EC=4.1.1.50 ; Autocatalytic cleavage Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff b

Pubmed 18441057

prodomImg

sp|Q8PQ44|SPED_XANAC

S=1402 I=100 E=1.46823e-161

S-adenosylmethionine decarboxylase proenzyme EC=4.1.1.50 ; Autocatalytic cleavage Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff b

sp|Q3BYB2|SPED_XANC5

S=1399 I=100 E=3.69968e-161

S-adenosylmethionine decarboxylase proenzyme EC=4.1.1.50 ; Autocatalytic cleavage Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff b

sp|Q9X4I6|SPED_XANCP

S=1396 I=100 E=7.83076e-161

S-adenosylmethionine decarboxylase proenzyme EC=4.1.1.50 ; Autocatalytic cleavage Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff b

sp|B0RN02|SPED_XANCB

S=1396 I=100 E=7.83076e-161

S-adenosylmethionine decarboxylase proenzyme EC=4.1.1.50 ; Autocatalytic cleavage Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff b

sp|Q4UZF5|SPED_XANC8

S=1396 I=100 E=7.83076e-161

S-adenosylmethionine decarboxylase proenzyme EC=4.1.1.50 ; Autocatalytic cleavage Lyase Polyamine biosynthesis Pyruvate S-adenosyl-L-methionine Schiff b

IPR016067 [G3DSA:3.60.90.10]

187

S-adenosylmethionine decarboxylase, core

IPR009165 [PIRSF001356]

264

S-adenosylmethionine decarboxylase, bacterial

IPR003826 [PF02675]

170

S-adenosylmethionine decarboxylase, bacterial/archaeal

IPR009165 [TIGR03331]

262

S-adenosylmethionine decarboxylase, bacterial

PD123272

260

S=1061 I=76 E=4.73654e-121

IPR016067 [SSF56276]

175

S-adenosylmethionine decarboxylase, core

P0ADT5 sp|P0ADT5|YGIC_ECOLI

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Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one iKYk1Lgp)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	5 hits
	Swiss-Prot ncbi-blastp	102 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	1 hits
	IprScan	5 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr04830.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr04830.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr04830.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr04830.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

XFF4834R_chr17500382_1879548_f1_XFF4834R-XFF4834R_chr16250 XFF4834R_chr16250

ID	XFF4834R_chr17500382_1879548_f1_XFF4834R-XFF4834R_chr16250
AC	XFF4834R_chr16250
LT	XFF4834R_chr16250
OR	XFF4834R_chr from 1878382 to 1879548 on strand +
DE	putative glutathionylspermidine synthase
IP	Glutathionylspermidine synthase
CL	1.7.14.3 Spermidine biosynthesis
EC
GO	InterPro Curated
PM
AN
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by jacques (20110314)
MW	43600.7 Da
SQ	388 aa
	........10........20........30........40........50 \| \| \| \| \| MQRILIPERADWRTQAESLGFHFHTIDGEPYWDESAYYAFSLRQIEDDIE APTQELHDMAMQLVDEVVGSEALMTRLAIPPFYWDWIVNSWKERDPHLCG RMDLAYSGDGPAKLYELNYDTPTSLYESAYFQWLWLEQQIASGALPKGTD QYNLIQDLLCETLGALAVDGAIGAQMHFAAVRDSLEDRATVRYLRDCAHQ VGISTEEVAIEDIGLSAEGWFTDEQDRVIHTLFKLYPLEFMMEERFGPAL IADRVRLIEPAWKSVLSNKGILPLLWDRHQGHPNLLPARFAQAGEAPSAG WVRKPLLSREGANIALVTAQGEAAHTDGPYVDGPAILQAHHPLPVFDGRH ALVGSWVVADRPAGLGMRDDDGPITRDTSRFVPHVITD

NP_643311.1 lcl|XAC3002-XAC3002

388

S=2026 I=99 E=0

synthetase/amidase

YP_364883.1 lcl|XCV3152

388

S=2018 I=98 E=0

putative glutathionylspermidine synthase

NP_638181.1 lcl|XCC2833

388

S=1929 I=93 E=0

synthetase/amidase

S=987 I=48 E=6.87561e-111

Uncharacterized protein ygiC

Pubmed 1314093

prodomImg

Q9GT49 sp|Q9GT49|Q9GT49_TRYCR

Q9GT48 sp|Q9GT48|Q9GT48_TRYCR

S=336 I=29 E=5.69703e-32

Trypanothione synthetase Trypanothione synthetase, putative

Pubmed 12826302

prodomImg

382

S=333 I=28 E=1.35056e-31

Trypanothione synthetase Trypanothione synthetase, putative

Pubmed 12826302

prodomImg

Q95WL5 sp|Q95WL5|Q95WL5_TRYCR

O60993 sp|O60993|TRYS_CRIFA

S=320 I=28 E=4.65408e-30

Trypanothione synthetase

Pubmed 12121990

prodomImg

Q5DM89 sp|Q5DM89|Q5DM89_CRIFA

S=320 I=29 E=4.73594e-30

Trypanothione synthetase EC=6.3.1.9 ; ATP-binding Ligase Magnesium Nucleotide-binding

Pubmed 9677355,1304372

prodomImg

Q8IFU8 sp|Q8IFU8|Q8IFU8_LEIDO

S=316 I=28 E=1.37202e-29

Trypanothione synthetase

Pubmed 15537651

prodomImg

A5JV94 sp|A5JV94|A5JV94_LEIAM

S=308 I=28 E=1.5354e-28

Trypanothione synthetase EC=6.3.1.9 ; Ligase

Pubmed 15610825

prodomImg

Q8IEX1 sp|Q8IEX1|Q8IEX1_9TRYP

S=302 I=28 E=8.70436e-28

Trypanothione synthetase

Pubmed 18083246

prodomImg

383

S=300 I=26 E=1.46868e-27

Trypanothione synthetase EC=6.3.1.9 ; Ligase

Pubmed 12967709

prodomImg

Q711P7 sp|Q711P7|Q711P7_LEIMA

S=297 I=27 E=2.97601e-27

Trypanothione synthetase

Pubmed 15610825

prodomImg

sp|P0ADT5|YGIC_ECOLI

S=987 I=48 E=4.73336e-111

Uncharacterized protein ygiC

sp|P0ADT6|YGIC_ECOL6

S=987 I=48 E=4.73336e-111

Uncharacterized protein ygiC

sp|P0ADT7|YGIC_ECO57

S=987 I=48 E=4.73336e-111

Uncharacterized protein ygiC

sp|P33222|YJFC_ECOLI

386

S=983 I=51 E=1.67576e-110

Uncharacterized protein yjfC

sp|P44940|Y929_HAEIN

387

S=603 I=37 E=1.64098e-64

Uncharacterized protein HI0929

IPR005494 [PF03738]

387

Glutathionylspermidine synthase

PD597651

193

386

S=480 I=49 E=1.25207e-50

PD007794

169

S=414 I=50 E=1.32201e-42

P21170 sp|P21170|SPEA_ECOLI

Suggest an annotation
Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one 7cuLjiEc)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	13 hits
	Swiss-Prot ncbi-blastp	9 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	0 hits
	IprScan	1 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr16250.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr16250.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr16250.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr16250.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

speA XFF4834R_chr38130

ID	speA
AC	XFF4834R_chr38130
LT	XFF4834R_chr38130
OR	XFF4834R_chr from 4406364 to 4408301 on strand -
DE	Arginine decarboxylase
IP	Orn/DAP/Arg decarboxylase 2
CL	1.7.14.3 Spermidine biosynthesis
EC
GO	InterPro Biological Process: arginine catabolic process (GO:0006527) Biological Process: spermidine biosynthetic process (GO:0008295) Molecular Function: arginine decarboxylase activity (GO:0008792) Molecular Function: catalytic activity (GO:0003824) Curated
PM
AN	GenProtEC Metabolism --> Carbon compound utilization --> Amino acids --> Arginine degradation III (agmatinase pathway) Metabolism --> Central intermediary metabolism --> Polyamine biosynthesis --> Putrescine biosynthesis I Location of gene products --> Periplasmic space
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by darrasse (20120410)
MW	70918.3 Da
SQ	645 aa
	........10........20........30........40........50 \| \| \| \| \| MPGVTLHALFNSSRDSEMSDWSLDQARKTYSIPHWADGYFDVNAAGHVVV TPTADGPAVSLPEVVDAARAAGAKLPLLVRFPDILGQRLGKLQAAFAQAQ SEWDYAGGYTAVYPIKVNQHRGVAGTLASHHGEGFGLEAGSKPELMAVLA LSRPGGLIVCNGYKDREYIRLALIGRKLGLQTFIVIEKPSELTLVLEEAR ALDVKPGLGVRMRLASLGAGKWQNSGGDKAKFGLSPRQVLDLWKTLRDTE YADSLNLLHFHMGSQISNVRDIANGMREATRYFVELSRLGAKISHVDVGG GLGIDYEGTRSRSYCSINYGLHSYASNIVQPLASACEEHGLTPPRIVTEC GRAMTAHHAVLIANVSEVEQAPEGRVPDAHDDEPAAIRHLREIHDELDVR PAVELFQEAQHFHAEGLSAYALGQIDLTHRARIDDLFYAIAHGVRARLSF DEKSHRPVLDELNERLVDKYFVNFSVFESIPDVWAIDQVFPIVPIERLNE APLRRGIIADMTCDSDGMVKTYVENESLDSSLPLHRLNAGESYRIGFFLV GAYQEILGDIHNLFGDTDAVEVVVDRDGYRIAQQRRGDTTDVMLDYVGYQ LDTLRATYAERIAAAHLSPERAQELSAALEAGLTGYTYLSDEPLG

642

S=1540 I=48 E=1.34394e-177

Biosynthetic arginine decarboxylase EC=4.1.1.19 ; Lyase Magnesium Metal-binding Periplasm Polyamine biosynthesis Putrescine Pyridoxal phosphate

Pubmed 2198270

prodomImg

Q2PEQ1 sp|Q2PEQ1|Q2PEQ1_TRIPR

S=951 I=40 E=3.24768e-106

Arginine decarboxylase EC=4.1.1.19 ; Lyase Spermidine biosynthesis

Pubmed 16769692,13679984

prodomImg

Q2PEV1 sp|Q2PEV1|Q2PEV1_TRIPR

S=950 I=40 E=4.44516e-106

Arginine decarboxylase EC=4.1.1.19 ; Lyase Spermidine biosynthesis

Pubmed 16769692,13679984

prodomImg

Q43075 sp|Q43075|SPE1_PEA

S=934 I=39 E=3.92782e-104

Arginine decarboxylase EC=4.1.1.19 ; Lyase Magnesium Putrescine biosynthesis Pyridoxal phosphate Spermidine

Pubmed 7548836

prodomImg

Q5R1Y5 sp|Q5R1Y5|Q5R1Y5_MALDO

572

S=918 I=40 E=2.91531e-102

Arginine decarboxylase EC=4.1.1.19 ; Lyase Spermidine biosynthesis

Pubmed 15723827

prodomImg

Q9M618 sp|Q9M618|Q9M618_BRAJU

572

S=917 I=39 E=4.91898e-102

Arginine decarboxylase EC=4.1.1.19 ; Lyase Spermidine biosynthesis

Pubmed 12060267

prodomImg

Q9SI64 sp|Q9SI64|SPE1_ARATH

S=915 I=39 E=7.87674e-102

Arginine decarboxylase 1 EC=4.1.1.19 ; Lyase Magnesium Putrescine biosynthesis Pyridoxal phosphate Spermidine

Pubmed 8756495

prodomImg

Q6VMQ5 sp|Q6VMQ5|Q6VMQ5_PRIAN

632

S=903 I=37 E=2.44472e-100

Arginine decarboxylase EC=4.1.1.19 ; Lyase Spermidine biosynthesis

Pubmed 15527979

prodomImg

Q30JE3 sp|Q30JE3|Q30JE3_VIBCH

359

S=896 I=53 E=1.66441e-99

Arginine decarboxylase EC=4.1.1.19 ; Lyase Spermidine biosynthesis

Pubmed 16318732

prodomImg

Q30JE7 sp|Q30JE7|Q30JE7_VIBCH

359

S=894 I=53 E=2.31818e-99

Arginine decarboxylase EC=4.1.1.19 ; Lyase Spermidine biosynthesis

Pubmed 16318732

prodomImg

sp|Q8PFQ5|SPEA_XANAC

645

S=3318 I=100 E=0

Biosynthetic arginine decarboxylase EC=4.1.1.19 ; Lyase Magnesium Metal-binding Polyamine biosynthesis Pyridoxal phosphate Spermidine

sp|Q8P448|SPEA_XANCP

645

S=3172 I=97 E=0

Biosynthetic arginine decarboxylase EC=4.1.1.19 ; Lyase Magnesium Metal-binding Polyamine biosynthesis Pyridoxal phosphate Spermidine

sp|Q87F25|SPEA_XYLFT

644

S=2781 I=84 E=0

Biosynthetic arginine decarboxylase EC=4.1.1.19 ; Lyase Magnesium Metal-binding Polyamine biosynthesis Pyridoxal phosphate Spermidine

sp|B2I6M1|SPEA_XYLF2

644

S=2781 I=84 E=0

Biosynthetic arginine decarboxylase EC=4.1.1.19 ; Lyase Magnesium Metal-binding Polyamine biosynthesis Pyridoxal phosphate Spermidine

sp|Q9PH02|SPEA_XYLFA

644

S=2770 I=84 E=0

Biosynthetic arginine decarboxylase EC=4.1.1.19 ; Lyase Magnesium Metal-binding Polyamine biosynthesis Pyridoxal phosphate Spermidine

Arginine decarboxylase

105

119

Arginine decarboxylase

159

174

Arginine decarboxylase

185

206

Arginine decarboxylase

209

231

Arginine decarboxylase

336

353

Arginine decarboxylase

473

494

Arginine decarboxylase

498

523

Arginine decarboxylase

551

572

Arginine decarboxylase

113

131

Orn/DAP/Arg decarboxylase 2

136

148

Orn/DAP/Arg decarboxylase 2

252

265

Orn/DAP/Arg decarboxylase 2

346

365

Orn/DAP/Arg decarboxylase 2

IPR002985 [PTHR11482:SF3]

551

564

Orn/DAP/Arg decarboxylase 2

[G3DSA:3.20.20.10]

351

IPR002985 [PIRSF001336]

642

Arginine decarboxylase

565

Arginine decarboxylase

[PTHR11482]

565

IPR000183 [PF02784]

357

Orn/DAP/Arg decarboxylase 2

IPR000183 [PF00278]

360

572

Orn/DAP/Arg decarboxylase 2

IPR002985 [TIGR01273]

640

Arginine decarboxylase

PD005416

467

582

S=404 I=59 E=2.22253e-41

PD862121

140

S=304 I=50 E=2.98554e-29

PDA1E4D8

308

453

S=239 I=39 E=2.12929e-21

PDA1F8M5

141

202

S=234 I=77 E=8.51703e-21

PDA1K8H5

204

230

S=143 I=100 E=1.08669e-09

PD706117

587

642

S=128 I=52 E=5.99652e-08

PDA52017

201

229

S=115 I=69 E=2.80381e-06

PDA52015

202

229

S=106 I=64 E=2.80147e-05

PDA2P3E5

202

230

S=106 I=55 E=3.03015e-05

PDA2P3E4

197

229

S=105 I=64 E=4.29462e-05

[SSF51419]

359

B6YXJ9 sp|B6YXJ9|SPEE_THEON

Suggest an annotation
Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one i5tl9Qsv)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	92 hits
	Swiss-Prot ncbi-blastp	110 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	0 hits
	IprScan	22 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr38130.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr38130.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr38130.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WB6i6Q9T/XFF4834R_chr38130.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

speE XFF4834R_chr38140

ID	speE
AC	XFF4834R_chr38140
LT	XFF4834R_chr38140
OR	XFF4834R_chr from 4408483 to 4409340 on strand +
DE	Spermidine synthase
IP	Spermine synthase
CL	1.7.14.3 Spermidine biosynthesis
EC
GO	InterPro Molecular Function: catalytic activity (GO:0003824) Curated
PM
AN
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by darrasse (20120410)
MW	31522.4 Da
SQ	285 aa
	........10........20........30........40........50 \| \| \| \| \| MSANDNWYIEHFQPTGSAIGFRISGKLDEVQSPFQKIEIYQTTDWGKLML IDGAVMLTSRDNFFYHEMISHPALFTHPAPKRVVIIGGGDCGTLREVLKH PGVESATQCDIDEQVTRMSEKYFPELCDSNHDARAELLFNDGVAYMANCP AGSVDIVIVDSTDPVGPAEGLFNKAFYESCFKALKDDGILVQQSESPLAL LDLINEMRTEMGKAGFQSFKTLPFPQPCYPTGWWSVTMASKQADADFAFR QDAAQAKGFDTLYYTAHQHTGVLVAPPFVAKALGE

Domain decomposition

283

S=482 I=36 E=8.86678e-50

Probable spermidine synthase EC=2.5.1.16 ; Polyamine biosynthesis Transferase

Pubmed 18790866

prodomImg

Q64674 sp|Q64674|SPEE_MOUSE

P70998 sp|P70998|SPEE_BACSU

S=456 I=36 E=1.21058e-46

Spermidine synthase EC=2.5.1.16 ; biosynthesis Transferase

Pubmed 7803821

prodomImg

280

S=454 I=38 E=1.77664e-46

Spermidine synthase EC=2.5.1.16 ; Polyamine biosynthesis Transferase

Pubmed 9353933

prodomImg

Q9WZC2 sp|Q9WZC2|SPEE_THEMA

284

S=452 I=35 E=3.32833e-46

Spermidine synthase EC=2.5.1.16 ; Polyamine biosynthesis Transferase

Pubmed 11731804

prodomImg

P19623 sp|P19623|SPEE_HUMAN

Q93X16 sp|Q93X16|Q93X16_SOLTU

S=451 I=35 E=4.80021e-46

Spermidine synthase EC=2.5.1.16 ; Polymorphism biosynthesis Transferase

Pubmed 2344393,2069720

prodomImg

240

S=437 I=38 E=2.24444e-44

Spermidine synthase EC=2.5.1.16 ; Transferase

Pubmed 16088399

prodomImg

Q96UK1 sp|Q96UK1|Q96UK1_EMENI

284

S=436 I=33 E=2.76685e-44

SPEE_NEUCR Spermidine synthase (Putrescine aminopropyltransferase) (SPDSY) Spermidine synthase

Pubmed 12410837

prodomImg

Q9ZTR0 sp|Q9ZTR0|SPD2_PEA

240

S=435 I=38 E=3.78703e-44

Spermidine synthase 2 EC=2.5.1.16 ; biosynthesis Transferase

Pubmed 10344199

prodomImg

O48658 sp|O48658|SPD1_HYONI

240

S=434 I=38 E=5.46176e-44

Spermidine synthase 1 EC=2.5.1.16 ; biosynthesis Transferase

Pubmed 9517003

prodomImg

B2LGI4 sp|B2LGI4|B2LGI4_SILDC

232

S=431 I=42 E=1.26135e-43

Putative spermidine synthase ; Transferase

Pubmed 18394889

prodomImg

sp|Q8PFQ4|SPEE_XANAC

S=1434 I=94 E=2.22406e-165

Spermidine synthase EC=2.5.1.16 ; Polyamine biosynthesis Transferase

sp|Q3BN93|SPEE_XANC5

S=1430 I=93 E=6.78921e-165

Spermidine synthase EC=2.5.1.16 ; Polyamine biosynthesis Transferase

sp|Q5H6E7|SPEE_XANOR

S=1412 I=92 E=1.08534e-162

Spermidine synthase EC=2.5.1.16 ; Polyamine biosynthesis Transferase

sp|B2SHF6|SPEE_XANOP

S=1412 I=92 E=1.08534e-162

Spermidine synthase EC=2.5.1.16 ; Polyamine biosynthesis Transferase

sp|Q2P928|SPEE_XANOM

S=1412 I=92 E=1.08534e-162

Spermidine synthase EC=2.5.1.16 ; Polyamine biosynthesis Transferase

[G3DSA:2.30.140.10]

[G3DSA:3.40.50.150]

283

IPR001045 [PTHR11558]

285

Spermine synthase

IPR001045 [PF01564]

243

Spermine synthase

IPR001045 [TIGR00417]

278

Spermine synthase

[seg]

242

256

PD002785

283

S=484 I=40 E=3.56181e-51

PDA1U0A5

233

285

S=146 I=55 E=3.10001e-10

[SSF53335]

283