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Q0T0V3

- SPEA_SHIF8

UniProt

Q0T0V3 - SPEA_SHIF8

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Protein

Biosynthetic arginine decarboxylase

Gene
speA, SFV_2993
Organism
Shigella flexneri serotype 5b (strain 8401)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine By similarity.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation
Pyridoxal phosphate By similarity.UniRule 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. putrescine biosynthetic process Source: UniProtKB-HAMAP
  3. spermidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSFLE373384:GHZM-2989-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylase (EC:4.1.1.19)
Short name:
ADC
Gene namesi
Name:speA
Ordered Locus Names:SFV_2993
OrganismiShigella flexneri serotype 5b (strain 8401)
Taxonomic identifieri373384 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000000659: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Biosynthetic arginine decarboxylaseUniRule annotationPRO_1000024275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-(pyridoxal phosphate)lysine By similarity

Proteomic databases

PRIDEiQ0T0V3.

Interactioni

Protein-protein interaction databases

STRINGi373384.SFV_2993.

Structurei

3D structure databases

ProteinModelPortaliQ0T0V3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni281 – 29111Substrate-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

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.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
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.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0T0V3-1 [UniParc]FASTAAdd to Basket

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MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAQLV    50
KTREAQGQRL PALFCFPQIL QHRLRSINAA FKRARESYGY NGDYFLVYPI 100
KVNQHRRVIE SLIHSGEPLG LEAGSKAELM AVLAHAGMTR SVIVCNGYKD 150
REYIRLALIG EKMGHKVYLV IEKMSEIAIV LDEAERLNVV PRLGVRARLA 200
SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LREAGRLDSL QLLHFHLGSQ 250
MANIRDIATG VRESARFYVE LHKLGVNIQC FDVGGGLGVD YEGTRSQSDC 300
SVNYGLNEYA NNIIWAIGDA CEENGLPHPT VITESGRAVT AHHTVLVSNI 350
IGVERNEYTV PTAPVEDAPR ALQSMWETWQ EMHEPGTRRS LREWLHDSQM 400
DLHDIHIGYS SGTFSLQERA WAEQLYLSMC HEVQKQLDPQ NRAHRPIIDE 450
LQERMADKMY VNFSLFQSMP DAWGIDQLFP VLPLEGLDQV PERRAVLLDI 500
TCDSDGAIDH YIDGDGIATT MPMPEYDPEN PPMLGFFMVG AYQEILGNMH 550
NLFGDTEAVD VFVFPDGSVE VELSDEGDTV ADMLQYVQLD PKTLLTQFRD 600
QVKKTDLDAE LQQQFLEEFE AGLYGYTYLE DE 632
Length:632
Mass (Da):71,209
Last modified:September 5, 2006 - v1
Checksum:iC801CC5D55FA2563
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000266 Genomic DNA. Translation: ABF05062.1.
RefSeqiYP_690367.1. NC_008258.1.

Genome annotation databases

EnsemblBacteriaiABF05062; ABF05062; SFV_2993.
GeneIDi4210125.
KEGGisfv:SFV_2993.
PATRICi18729921. VBIShiFle33408_3428.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000266 Genomic DNA. Translation: ABF05062.1 .
RefSeqi YP_690367.1. NC_008258.1.

3D structure databases

ProteinModelPortali Q0T0V3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 373384.SFV_2993.

Proteomic databases

PRIDEi Q0T0V3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF05062 ; ABF05062 ; SFV_2993 .
GeneIDi 4210125.
KEGGi sfv:SFV_2993.
PATRICi 18729921. VBIShiFle33408_3428.

Phylogenomic databases

eggNOGi COG1166.
HOGENOMi HOG000029191.
KOi K01585.
OMAi IDHYVDG.
OrthoDBi EOG676Z0R.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SFLE373384:GHZM-2989-MONOMER.

Family and domain databases

Gene3Di 2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPi MF_01417. SpeA.
InterProi IPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view ]
Pfami PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view ]
PIRSFi PIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSi PR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMi SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsi TIGR01273. speA. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a."
    Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.
    BMC Genomics 7:173-173(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 8401.

Entry informationi

Entry nameiSPEA_SHIF8
AccessioniPrimary (citable) accession number: Q0T0V3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: June 11, 2014
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

Documents

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

External Data

Dasty 3

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