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Q7NU27

- SPEA_CHRVO

UniProt

Q7NU27 - SPEA_CHRVO

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Protein
Biosynthetic arginine decarboxylase
Gene
speA, CV_2876
Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
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

BioCyciCVIO243365:GHUD-2935-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:CV_2876
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
ProteomesiUP000001424: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 626626Biosynthetic arginine decarboxylaseUniRule annotation
PRO_0000149958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Protein-protein interaction databases

STRINGi243365.CV_2876.

Structurei

3D structure databases

ProteinModelPortaliQ7NU27.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni279 – 28911Substrate-binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiDSEDMVE.
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.
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.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7NU27-1 [UniParc]FASTAAdd to Basket

« Hide

MAWSVADSRS LYGIRHWGAG YFDVGDSGNI VVRPNVRQRK EIDLYRLVRD    50
LGGKGLDLPL LVRFPDILQD RVTRLCGAFD KAIAEQGYGN RYTAIYPIKV 100
NQQEAVVKSI IATQDVSIGL EAGSKPELMA VLALAPKGCT IVCNGYKDRE 150
FIRLALIGER LGHQVFIVIE KESEVDLVIE ESRKLEVRPN IGLRVRLSSL 200
ASSKWSDTGG EKGKFGLSAG QLISATDKLI AAGLGDCVRL MHFHMGSQIA 250
NIADYRLGFR EAIRYFAELR ALGLPVDHVD VGGGLGVDYD GTHSRNDSSI 300
NYDMAEYAHV IVSMLSEFCA ENGIPHPRIL SESGRAMTAH HAVLLMNVTD 350
VERLPDTVAP IDKAEELSLP LRKLVELANL NDEELVTEIY YRASHCVSEV 400
SEMYAEGRLS LQEKALAEDL HATLCRRLHN QLQASQRSQR QVYDELTDRL 450
ADKYFCNFSV FQSLPDTWAI DQVLPIMPVH RLAEQPTRRA VLQDLTCDSD 500
GKLKQYVDQQ SIESSMSVHE VKQGDEYLIA VFLVGAYQEI LGDMHNLFGD 550
TDSVNVYVRE GGELEISGIE EHDTIEDMLR YVHLSPEDLL NRYEAKTREC 600
DLNPEERSLY FAEFCRGLKQ SSYLAV 626
Length:626
Mass (Da):70,119
Last modified:December 15, 2003 - v1
Checksum:i98A2CC60BACFB3F3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016825 Genomic DNA. Translation: AAQ60544.1.
RefSeqiNP_902546.1. NC_005085.1.
WP_011136423.1. NC_005085.1.

Genome annotation databases

EnsemblBacteriaiAAQ60544; AAQ60544; CV_2876.
GeneIDi2548774.
KEGGicvi:CV_2876.
PATRICi21440494. VBIChrVio67196_2799.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016825 Genomic DNA. Translation: AAQ60544.1 .
RefSeqi NP_902546.1. NC_005085.1.
WP_011136423.1. NC_005085.1.

3D structure databases

ProteinModelPortali Q7NU27.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243365.CV_2876.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAQ60544 ; AAQ60544 ; CV_2876 .
GeneIDi 2548774.
KEGGi cvi:CV_2876.
PATRICi 21440494. VBIChrVio67196_2799.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci CVIO243365:GHUD-2935-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.
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 PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
    Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
    , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
    Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Entry informationi

Entry nameiSPEA_CHRVO
AccessioniPrimary (citable) accession number: Q7NU27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: December 15, 2003
Last modified: September 3, 2014
This is version 80 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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