Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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

Pathway:iagmatine 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

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSAMA326297:GH0T-2040-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
ProteomesiUP000009175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636Biosynthetic arginine decarboxylasePRO_1000024264Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi326297.Sama_1963.

Structurei

3D structure databases

ProteinModelPortaliA1S712.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 29611Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 1 hit.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
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.
PATRICi23452671. VBISheAma74963_2024.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliA1S712.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326297.Sama_1963.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM00169; ABM00169; Sama_1963.
KEGGisaz:Sama_1963.
PATRICi23452671. VBISheAma74963_2024.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciSAMA326297:GH0T-2040-MONOMER.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 1 hit.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-1098 / SB2B.

Entry informationi

Entry nameiSPEA_SHEAM
AccessioniPrimary (citable) accession number: A1S712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: July 22, 2015
This is version 60 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.