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Q7NRK0 (OTCC_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ornithine carbamoyltransferase, catabolic

Short name=OTCase
EC=2.1.3.3
Gene names
Name:arcB
Ordered Locus Names:CV_3781
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline. HAMAP MF_01109

Pathway

Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2. HAMAP MF_01109

Subcellular location

Cytoplasm Probable HAMAP MF_01109.

Sequence similarities

Belongs to the ATCase/OTCase family.

Ontologies

Keywords
   Biological processArginine metabolism
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentornithine carbamoyltransferase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionamino acid binding

Inferred from electronic annotation. Source: InterPro

ornithine carbamoyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336Ornithine carbamoyltransferase, catabolic HAMAP MF_01109
PRO_0000112909

Regions

Region57 – 615Carbamoyl phosphate binding By similarity
Region274 – 2774Ornithine binding By similarity

Sites

Binding site1081Carbamoyl phosphate By similarity
Binding site1361Carbamoyl phosphate By similarity
Site321Important for structural integrity By similarity
Site1491Important for structural integrity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NRK0 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: E35A95E2046A82B3

FASTA33637,764
        10         20         30         40         50         60 
MAFNLRNRNF LKMLDFTPRE IRYLLDLSRD LKRAKYSGTE QQHLKGKNVA LIFEKTSTRT 

        70         80         90        100        110        120 
RCAFEVACFD QGANVSYIGP SGSQIGHKES MKDTARVLGR MYDAIEYRGY SQDMVEHELA 

       130        140        150        160        170        180 
AYAGVPVYNG LTDEYHPTQM LADVLTMWEH SDKPISQISY TYLGDARNNM GNSLLVIGSK 

       190        200        210        220        230        240 
LGMDVRIGAP KHLWPTDELV AECREIAKRT GARITLTEDP KEAVKGTDFI HTDVWVSMGE 

       250        260        270        280        290        300 
PAEVWAERIR LLKPYQVNSA LMAASGNPQV KFMHCLPAFH NSETKVGKEI SAQYPELANG 

       310        320        330 
IEVTEDVFES EACIAFEQAE NRMHTIKAIL VSTLGD 

« 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: 14500782] [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: AAQ61443.1.
RefSeqNP_903451.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NRK0.
SMRQ7NRK0. Positions 2-336.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2548111.
GenomeReviewsGene locus CV_3781 in contig AE016825_GR.
KEGGcvi:CV_3781.
NMPDRfig|243365.1.peg.3781.
PATRIC21442387. VBIChrVio67196_3708.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG579429.
OMAMTPYQIN.
PhylomeDBQ7NRK0.

Enzyme and pathway databases

BioCycCVIO243365:CV_3781-MONOMER.

Family and domain databases

HAMAPMF_01109. OTCase.
[Tree]
InterProIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
IPR024904. Orn_carbamltrans.
[Graphical view]
KOK00611.
PfamPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMSSF53671. Asp/Orn_carbamoyltranf. 1 hit.
TIGRFAMsTIGR00658. Orni_carb_tr. 1 hit.
PROSITEPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOTCC_CHRVO
AccessionPrimary (citable) accession number: Q7NRK0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families