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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella sediminis (strain HAW-EB3)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation
  • pyridoxal 5'-phosphateUniRule annotation

Pathwayi: agmatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Biosynthetic arginine decarboxylase (speA)
This subpathway is part of the pathway agmatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes agmatine from L-arginine, the pathway agmatine biosynthesis and in Amine and polyamine biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPolyamine biosynthesis, Spermidine biosynthesis
LigandMagnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSSED425104:G1G9Y-2790-MONOMER
UniPathwayiUPA00186; UER00284

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation)
Short name:
ADCUniRule annotation
Gene namesi
Name:speAUniRule annotation
Ordered Locus Names:Ssed_2609
OrganismiShewanella sediminis (strain HAW-EB3)
Taxonomic identifieri425104 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000002015 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000874091 – 637Biosynthetic arginine decarboxylaseAdd BLAST637

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiA8FWJ3

Interactioni

Protein-protein interaction databases

STRINGi425104.Ssed_2609

Structurei

3D structure databases

ProteinModelPortaliA8FWJ3
SMRiA8FWJ3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni286 – 296Substrate-bindingUniRule annotationAdd BLAST11

Sequence similaritiesi

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DP5 Bacteria
COG1166 LUCA
HOGENOMiHOG000029191
KOiK01585
OMAiLFPIMPI
OrthoDBiPOG091H04NG

Family and domain databases

CDDicd06830 PLPDE_III_ADC, 1 hit
Gene3Di2.40.37.10, 3 hits
3.20.20.10, 1 hit
HAMAPiMF_01417 SpeA, 1 hit
InterProiView protein in InterPro
IPR009006 Ala_racemase/Decarboxylase_C
IPR002985 Arg_decrbxlase
IPR022644 De-COase2_N
IPR000183 Orn/DAP/Arg_de-COase
IPR029066 PLP-binding_barrel
PANTHERiPTHR43295 PTHR43295, 1 hit
PfamiView protein in Pfam
PF02784 Orn_Arg_deC_N, 1 hit
PIRSFiPIRSF001336 Arg_decrbxlase, 1 hit
PRINTSiPR01180 ARGDCRBXLASE
PR01179 ODADCRBXLASE
SUPFAMiSSF50621 SSF50621, 1 hit
SSF51419 SSF51419, 1 hit
TIGRFAMsiTIGR01273 speA, 1 hit

Sequencei

Sequence statusi: Complete.

A8FWJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDWSINDAR TGYNVNYWSQ GLYGISDTGE VTVSPDPSHP EYSIGLNELA
60 70 80 90 100
KDMVKSGVAL PVLIRFPQIL HHRVNSVCQA FNQAIQKYEY QSDYLLVYPI
110 120 130 140 150
KVNQQQTVVE EILASQVSKE VPQLGLEAGS KPELMAVLAM AQKASSVIIC
160 170 180 190 200
NGYKDVEYIR LALIGEKLGH KVYIVLEKLS ELKIILEEAE KLGVTPRLGC
210 220 230 240 250
RVRLAFQGKG KWQASGGEKS KFGLSASQVL TVIDSLKQSQ MLDSLQLLHF
260 270 280 290 300
HLGSQIANIR DIRQGVSEAG RFYCELQKLG ANVKCFDVGG GLAVDYDGTR
310 320 330 340 350
SQSSSSMNYG LTEYANNIVS VLTDLCNEYK EPMPRIISES GRFLTAHHAV
360 370 380 390 400
LITDVIGTEA YKPEVIEEPE TEAPQLLHNM WQSWSEVSGR ADQRALIEIY
410 420 430 440 450
HDCQSDLSEV HSLFALGQLS LSERAWAEQV NLRVCHELRD VMSPKYRFHR
460 470 480 490 500
PIIDELNEKL ADKFFVNFSL FQSLPDAWGI DQVFPIMPLS GLDKAPERRA
510 520 530 540 550
VMLDITCDSD GTIDQYVDGQ GIETTIPVPT WSAESPYLIG FFLVGAYQEI
560 570 580 590 600
LGDMHNLFGD TNSAVVRLDD DGRTNIESVL AGDTVADVLR YVNLDAVSFM
610 620 630
RTYEELVNKH IQEAERANIL EELQLGLKGY TYLEDFS
Length:637
Mass (Da):71,200
Last modified:November 13, 2007 - v1
Checksum:iC7C03577B46A88ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA Translation: ABV37216.1
RefSeqiWP_012142948.1, NC_009831.1

Genome annotation databases

EnsemblBacteriaiABV37216; ABV37216; Ssed_2609
KEGGisse:Ssed_2609

Similar proteinsi

Entry informationi

Entry nameiSPEA_SHESH
AccessioniPrimary (citable) accession number: A8FWJ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: May 23, 2018
This is version 67 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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