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Q7NU27 (SPEA_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase

Short name=ADC
EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:CV_2876
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP-Rule MF_01417

Catalytic activity

L-arginine = agmatine + CO2. HAMAP-Rule MF_01417

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01417

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01417

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP-Rule MF_01417

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149958

Regions

Region279 – 28911Substrate-binding Potential

Amino acid modifications

Modified residue991N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NU27 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 98A2CC60BACFB3F3

FASTA62670,119
        10         20         30         40         50         60 
MAWSVADSRS LYGIRHWGAG YFDVGDSGNI VVRPNVRQRK EIDLYRLVRD LGGKGLDLPL 

        70         80         90        100        110        120 
LVRFPDILQD RVTRLCGAFD KAIAEQGYGN RYTAIYPIKV NQQEAVVKSI IATQDVSIGL 

       130        140        150        160        170        180 
EAGSKPELMA VLALAPKGCT IVCNGYKDRE FIRLALIGER LGHQVFIVIE KESEVDLVIE 

       190        200        210        220        230        240 
ESRKLEVRPN IGLRVRLSSL ASSKWSDTGG EKGKFGLSAG QLISATDKLI AAGLGDCVRL 

       250        260        270        280        290        300 
MHFHMGSQIA NIADYRLGFR EAIRYFAELR ALGLPVDHVD VGGGLGVDYD GTHSRNDSSI 

       310        320        330        340        350        360 
NYDMAEYAHV IVSMLSEFCA ENGIPHPRIL SESGRAMTAH HAVLLMNVTD VERLPDTVAP 

       370        380        390        400        410        420 
IDKAEELSLP LRKLVELANL NDEELVTEIY YRASHCVSEV SEMYAEGRLS LQEKALAEDL 

       430        440        450        460        470        480 
HATLCRRLHN QLQASQRSQR QVYDELTDRL ADKYFCNFSV FQSLPDTWAI DQVLPIMPVH 

       490        500        510        520        530        540 
RLAEQPTRRA VLQDLTCDSD GKLKQYVDQQ SIESSMSVHE VKQGDEYLIA VFLVGAYQEI 

       550        560        570        580        590        600 
LGDMHNLFGD TDSVNVYVRE GGELEISGIE EHDTIEDMLR YVHLSPEDLL NRYEAKTREC 

       610        620 
DLNPEERSLY FAEFCRGLKQ SSYLAV 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ60544.1.
RefSeqNP_902546.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NU27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_2876.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ60544; AAQ60544; CV_2876.
GeneID2548774.
KEGGcvi:CV_2876.
PATRIC21440494. VBIChrVio67196_2799.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMADSEDMVE.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-2935-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPMF_01417. SpeA.
InterProIPR009006. 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]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsTIGR01273. speA. 1 hit.
PROSITEPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEA_CHRVO
AccessionPrimary (citable) accession number: Q7NU27
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways