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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella sp. (strain MR-4)
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: 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

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

BioCyciSSP60480:GI2N-1641-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:Shewmr4_1557
OrganismiShewanella sp. (strain MR-4)
Taxonomic identifieri60480 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_1000024272Add
BLAST

Amino acid modifications

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

Structurei

3D structure databases

ProteinModelPortaliQ0HJY2.
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.

Q0HJY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDWSIDAAR AGYNVTHWSQ GFYGISDQGE VTVSPDPKNP DHKIGLNELA
60 70 80 90 100
KDMVKAGVAL PVLVRFPQIL HHRVNSLCQA FDQAIQKYEY QADYLLVYPI
110 120 130 140 150
KVNQQKTVVE EILASQASKE VPQLGLEAGS KPELMAVLAM AQKASSVIVC
160 170 180 190 200
NGYKDNEYIR LALIGEKLGH KVYIVLEKLS ELKMVLAESK RLGVKPRLGL
210 220 230 240 250
RARLAFQGKG KWQASGGEKS KFGLSAAQIL TVVDQLKEND MLDSLQLLHF
260 270 280 290 300
HLGSQIANIR DIRQGVSEAA RFYCELRELG ASINCFDVGG GLAVDYDGTR
310 320 330 340 350
SQSNNSMNYG LSEYANNIVN VLTDICNEYE QPMPRIISES GRHLTAHHAV
360 370 380 390 400
LITDVIGTEA YQVEDIQPPA EESPQLLHNM WQSWTELSGR ADQRALIEIY
410 420 430 440 450
HDSQSDLQEA QSLFALGQLS LAERAWAEQA NLRVCHEVQG LLSTKNRYHR
460 470 480 490 500
PIIDELNEKL ADKFFVNFSL FQSLPDAWGI DQVFPVLPLS GLDKAPERRA
510 520 530 540 550
VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSAESPYLMG FFMVGAYQEI
560 570 580 590 600
LGDMHNLFGD TNSAVVSIEE NGMTNIESVL AGDTVADVLR YVNLDAVDFM
610 620 630
RTYEELVNQH IVEEERAQIL EELQVGLKGY TYLEDFS
Length:637
Mass (Da):71,019
Last modified:October 3, 2006 - v1
Checksum:i1E26995E7BB168BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000446 Genomic DNA. Translation: ABI38635.1.
RefSeqiWP_011622338.1. NC_008321.1.
YP_733692.1. NC_008321.1.

Genome annotation databases

EnsemblBacteriaiABI38635; ABI38635; Shewmr4_1557.
KEGGishe:Shewmr4_1557.
PATRICi23579758. VBISheSp133532_1622.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000446 Genomic DNA. Translation: ABI38635.1.
RefSeqiWP_011622338.1. NC_008321.1.
YP_733692.1. NC_008321.1.

3D structure databases

ProteinModelPortaliQ0HJY2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI38635; ABI38635; Shewmr4_1557.
KEGGishe:Shewmr4_1557.
PATRICi23579758. VBISheSp133532_1622.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciSSP60480:GI2N-1641-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: MR-4.

Entry informationi

Entry nameiSPEA_SHESM
AccessioniPrimary (citable) accession number: Q0HJY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: June 24, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.