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A7ZVD3 (OTC_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 48. 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:argI
Ordered Locus Names:EcE24377A_4825
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length337 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 HAMAP-Rule MF_01109.

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 – 337337Ornithine carbamoyltransferase HAMAP-Rule MF_01109
PRO_1000084843

Regions

Region56 – 605Carbamoyl phosphate binding By similarity
Region134 – 1374Carbamoyl phosphate binding By similarity
Region236 – 2372Ornithine binding By similarity
Region273 – 2764Carbamoyl phosphate binding By similarity

Sites

Binding site101Carbamoyl phosphate By similarity
Binding site721Carbamoyl phosphate By similarity
Binding site831Carbamoyl phosphate By similarity
Binding site1071Carbamoyl phosphate By similarity
Binding site1681Ornithine By similarity
Binding site2321Ornithine By similarity
Binding site3021Carbamoyl phosphate By similarity
Binding site3201Carbamoyl phosphate By similarity
Site311Important for structural integrity By similarity
Site1471Important for structural integrity By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZVD3 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 518D76277D1BF6DC

FASTA33737,235
        10         20         30         40         50         60 
MSGFYHKHFL KLLDFTPAEL NSLLQLAAKL KADKKSGKEE AKLTGKNIAL IFEKDSTRTR 

        70         80         90        100        110        120 
CSFEVAAYDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGYG QEIVETLAEY 

       130        140        150        160        170        180 
AGVPVWNGLT NEFHPTQLLA DLLTMQEHLP GKTFNEMTLV YAGDARNNMG NSMLEAAALT 

       190        200        210        220        230        240 
GLDLRLVAPK ACWPEAALVT ECRALAQQNG GDITLTEDVA KGVEGADFIY TDVWVSMGEA 

       250        260        270        280        290        300 
KEKWAERIAL LRDYQVNSKM MQLTGNPEVK FLHCLPAFHD DQTTLGKKMA EEFGLHGGME 

       310        320        330 
VTDEVFESAA SIVFDQAENR MHTIKAVMVA TLSKLNN

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000800 Genomic DNA. Translation: ABV17681.1.
RefSeqYP_001465762.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZVD3.
SMRA7ZVD3. Positions 2-334.
ModBaseSearch...

Protein-protein interaction databases

STRING331111.EcE24377A_4825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV17681; ABV17681; EcE24377A_4825.
GeneID5586475.
KEGGecw:EcE24377A_4825.
PATRIC18298906. VBIEscCol31211_5024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0078.
HOGENOMHOG000022686.
KOK00611.
OMARLMDFTP.
ProtClustDBPRK03515.

Enzyme and pathway databases

BioCycECOL331111:GH7P-4806-MONOMER.
UniPathwayUPA00068; UER00112.

Family and domain databases

Gene3D3.40.50.1370. 2 hits.
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_ECO24
AccessionPrimary (citable) accession number: A7ZVD3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: May 29, 2013
This is version 48 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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