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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella woodyi (strain ATCC 51908 / MS32)
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

Pathwayi

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine catabolic process Source: InterPro
  2. spermidine biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciSWOO392500:GI2C-2103-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:Swoo_2057
OrganismiShewanella woodyi (strain ATCC 51908 / MS32)
Taxonomic identifieri392500 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002168: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_1000145604Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi392500.Swoo_2057.

Structurei

3D structure databases

ProteinModelPortaliB1KRD4.
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]
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.

B1KRD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNWSINDAR TGYNVNYWSQ GLYGISDEGE ATVSPDPTRP ECSIGLNELA
60 70 80 90 100
KDMVKSGVNL PVLVRFPQIL HHRVNSLCQA FNQAIQKYQY QADYLLVYPI
110 120 130 140 150
KVNQQQTVVE EILASQVEKE VPQLGLEAGS KPELMAVLAM AQKASSVIIC
160 170 180 190 200
NGYKDIEYIR LALIGEKLGH KVYIVLEKLS ELKTVLEESK KLGVTPRLGL
210 220 230 240 250
RVRLAFQGKG KWQASGGEKS KFGLSASQVL TVIESLKSEE MLDSLQLLHF
260 270 280 290 300
HLGSQIANIR DIRQGVSEAG RFYCELQKLG ANVKCFDVGG GLAVDYDGTR
310 320 330 340 350
SQSSSSMNYG LTEYANNIVS VLTDICNEYE QPMPRIISES GCYLTAHHAV
360 370 380 390 400
LITDVIGTEA YKPEDIQPPA EDAPQLLHNM WHSWNEISGR ADQRALIEIY
410 420 430 440 450
HDCQSDLTEV HSLFALGQLS LTDRAWAEQV NLRVCHELQG VMSSKYRFHR
460 470 480 490 500
PIIDELTEKL ADKFFVNFSL FQSLPDAWGI DQVFPIMPLS GLDKAPERRA
510 520 530 540 550
VMLDITCDSD GTIDQYVDGQ GIETTLPVPA WSAESPYLIG FFLVGAYQEI
560 570 580 590 600
LGDMHNLFGD TNSAVIRLDD DGRTNIESVL AGDTVADVLR YVNLDAVSFM
610 620 630
RTYEELVNKH IQEDERANIL EELQLGLKGY TYLEDFS
Length:637
Mass (Da):71,154
Last modified:April 29, 2008 - v1
Checksum:i0609B1DA84469D62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000961 Genomic DNA. Translation: ACA86341.1.
RefSeqiWP_012324686.1. NC_010506.1.
YP_001760436.1. NC_010506.1.

Genome annotation databases

EnsemblBacteriaiACA86341; ACA86341; Swoo_2057.
GeneIDi6116320.
KEGGiswd:Swoo_2057.
PATRICi23606515. VBISheWoo126588_2125.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000961 Genomic DNA. Translation: ACA86341.1.
RefSeqiWP_012324686.1. NC_010506.1.
YP_001760436.1. NC_010506.1.

3D structure databases

ProteinModelPortaliB1KRD4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi392500.Swoo_2057.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA86341; ACA86341; Swoo_2057.
GeneIDi6116320.
KEGGiswd:Swoo_2057.
PATRICi23606515. VBISheWoo126588_2125.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciSWOO392500:GI2C-2103-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]
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 51908 / MS32.

Entry informationi

Entry nameiSPEA_SHEWM
AccessioniPrimary (citable) accession number: B1KRD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: March 4, 2015
This is version 51 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.