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Q740I5 (OTC_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. 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
Short name=OTCase
EC=2.1.3.3
Gene names
Name:argF
Ordered Locus Names:MAP_1365
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC) ›

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline By similarity. HAMAP-Rule MF_01109

Catalytic activity

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

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3. HAMAP-Rule MF_01109

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the ATCase/OTCase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionamino acid binding

Inferred from electronic annotation. Source: InterPro

ornithine carbamoyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Ornithine carbamoyltransferase HAMAP-Rule MF_01109
PRO_0000112952

Regions

Region51 – 555Carbamoyl phosphate binding By similarity
Region129 – 1324Carbamoyl phosphate binding By similarity
Region229 – 2302Ornithine binding By similarity
Region264 – 2674Carbamoyl phosphate binding By similarity

Sites

Binding site71Carbamoyl phosphate By similarity
Binding site781Carbamoyl phosphate By similarity
Binding site1021Carbamoyl phosphate By similarity
Binding site1611Ornithine By similarity
Binding site2251Ornithine By similarity
Binding site2751Carbamoyl phosphate By similarity
Binding site2931Carbamoyl phosphate By similarity
Site281Important for structural integrity By similarity
Site1421Important for structural integrity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q740I5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 7500E6BE03398101

FASTA30933,595
        10         20         30         40         50         60 
MTPRHFLRDD DLSPAEQAEV LALAAELKKD PFSARPLEGP RGVAVLFDKN STRTRFSFEV 

        70         80         90        100        110        120 
GIAQLGGHAV VVDARSTQLG RDETLEDTAR VLSRYVEAIV WRTFEQQRLE AMAGAATVPV 

       130        140        150        160        170        180 
INALSDEFHP CQMLADLQAI AEHKGSLSGL RMCYLGDGAN NMAHSLMLGG VTAGIHVTIA 

       190        200        210        220        230        240 
APDGFTPAPE FVAAARRRAE STGATVTLTT DARAAARGVD VLVTDTWTSM GQEDDGLDRR 

       250        260        270        280        290        300 
TPFWPYQLNA DLVSLADPEA IVLHCLPAHR GEEITDEVMD GPSSVVWDEA ENRLHAQKAL 


LTWLLERQS

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016958 Genomic DNA. Translation: AAS03682.1.
RefSeqNP_960299.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ740I5.
SMRQ740I5. Positions 4-307.
ModBaseSearch...

Protein-protein interaction databases

STRING262316.MAP1365.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS03682; AAS03682; MAP_1365.
GeneID2720213.
KEGGmpa:MAP1365.
PATRIC17995219. VBIMycAvi108102_1439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0078.
KOK00611.
OMAKHLLSIK.
ProtClustDBPRK00779.

Enzyme and pathway databases

UniPathwayUPA00068; UER00112.

Family and domain databases

HAMAPMF_01109. OTCase.
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]
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 nameOTC_MYCPA
AccessionPrimary (citable) accession number: Q740I5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 72 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

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