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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
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

BioCyciSAMA326297:G1G7Q-2065-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:Sama_1963
OrganismiShewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Taxonomic identifieri326297 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000009175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000242641 – 636Biosynthetic arginine decarboxylaseAdd BLAST636

Amino acid modifications

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

Proteomic databases

PRIDEiA1S712

Interactioni

Protein-protein interaction databases

STRINGi326297.Sama_1963

Structurei

3D structure databases

ProteinModelPortaliA1S712
SMRiA1S712
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
SUPFAMiSSF51419 SSF51419, 1 hit
TIGRFAMsiTIGR01273 speA, 1 hit

Sequencei

Sequence statusi: Complete.

A1S712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEWSIDDAR AGYNVAHWSQ GFYGISDEGE VTVSPDPKNP TFKIGLNALA
60 70 80 90 100
KDMVKAGVSL PVLVRFPQIL HHRVDHLCQM FNQAIQKYEY QSDYLLVYPI
110 120 130 140 150
KVNQQQTVVE EILASQVSKT VPQLGLEAGS KPELMAVLAM AQKASSVIVC
160 170 180 190 200
NGYKDKEYIR LALIGEKLGH SVYIVLEKMS ELQMVLEESK KLGVTPRLGL
210 220 230 240 250
RARLAFQGKG KWQASGGEKS KFGLSAAQIL KVVERLKDED MLESLQLLHF
260 270 280 290 300
HLGSQIANIR DIRHGVGEAA RFYCELRKLG AKVNCFDVGG GLAVDYDGTR
310 320 330 340 350
SQSNNSMNYA LAEYANNIVS VLTDVCNQNE QPMPRIISES GRYLTAHHAV
360 370 380 390 400
LITDVIGTEA YSPEDIPAPE EEAPQLLHNM WRSWNEISSR LDQRALIEIF
410 420 430 440 450
HDTQSDLAEA QSLFALGQLS LEDRAWAEQC NLAVCHELQG LMNARNRYQR
460 470 480 490 500
PIIDELNEKL ADRFFVNFSL FQSLPDAWGI DQVFPVLPLS GLDKVPERRA
510 520 530 540 550
VMLDITCDSD GIVDQYVDGQ GIETTLPVPN WSAEDPYLIG FFLVGAYQEI
560 570 580 590 600
LGDLHNLFGD TNSAVVRIDE EGQTNIESVL AGDTVADVLR YVNLDAVSFM
610 620 630
RTYEELVNSH IAEDERAMIL EELQVGLKGY TYLEDF
Length:636
Mass (Da):71,125
Last modified:February 6, 2007 - v1
Checksum:i1922594751248BA0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000507 Genomic DNA Translation: ABM00169.1
RefSeqiWP_011760076.1, NC_008700.1

Genome annotation databases

EnsemblBacteriaiABM00169; ABM00169; Sama_1963
KEGGisaz:Sama_1963

Similar proteinsi

Entry informationi

Entry nameiSPEA_SHEAM
AccessioniPrimary (citable) accession number: A1S712
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 23, 2018
This is version 69 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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