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Database: UniProt/SWISS-PROT
Entry: OTC_ECOL6
LinkDB: OTC_ECOL6
Original site: OTC_ECOL6 
ID   OTC_ECOL6               Reviewed;         334 AA.
AC   Q8FAD6;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   29-OCT-2014, entry version 83.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=argI; OrderedLocusNames=c5353;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group
CC       from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine
CC       (ORN) to produce L-citrulline. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate
CC       + L-citrulline.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN83775.1; -; Genomic_DNA.
DR   RefSeq; NP_757201.1; NC_004431.1.
DR   ProteinModelPortal; Q8FAD6; -.
DR   SMR; Q8FAD6; 2-334.
DR   STRING; 199310.c5353; -.
DR   EnsemblBacteria; AAN83775; AAN83775; c5353.
DR   GeneID; 1037355; -.
DR   KEGG; ecc:c5353; -.
DR   PATRIC; 18288350; VBIEscCol75197_5016.
DR   HOGENOM; HOG000022686; -.
DR   KO; K00611; -.
DR   OMA; YQRHFLR; -.
DR   OrthoDB; EOG690MGV; -.
DR   BioCyc; ECOL199310:C5353-MONOMER; -.
DR   UniPathway; UPA00068; UER00112.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   HAMAP; MF_01109; OTCase; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   InterPro; IPR024904; Orn_carbamltrans.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    334       Ornithine carbamoyltransferase.
FT                                /FTId=PRO_0000112920.
FT   REGION       56     60       Carbamoyl phosphate binding.
FT                                {ECO:0000250}.
FT   REGION      134    137       Carbamoyl phosphate binding.
FT                                {ECO:0000250}.
FT   REGION      236    237       Ornithine binding. {ECO:0000250}.
FT   REGION      273    276       Carbamoyl phosphate binding.
FT                                {ECO:0000250}.
FT   BINDING      10     10       Carbamoyl phosphate. {ECO:0000250}.
FT   BINDING      72     72       Carbamoyl phosphate. {ECO:0000250}.
FT   BINDING      83     83       Carbamoyl phosphate. {ECO:0000250}.
FT   BINDING     107    107       Carbamoyl phosphate. {ECO:0000250}.
FT   BINDING     168    168       Ornithine. {ECO:0000250}.
FT   BINDING     232    232       Ornithine. {ECO:0000250}.
FT   BINDING     302    302       Carbamoyl phosphate. {ECO:0000250}.
FT   BINDING     320    320       Carbamoyl phosphate. {ECO:0000250}.
FT   SITE         31     31       Important for structural integrity.
FT                                {ECO:0000250}.
FT   SITE        147    147       Important for structural integrity.
FT                                {ECO:0000250}.
SQ   SEQUENCE   334 AA;  36751 MW;  275AB9C6DC88331B CRC64;
     MSGFYHKHFL KLLDFTPAEL NSLLQLAAKL KADKKSGKEE ARLTGKNIAL IFEKDSTRTR
     CSFEVAAYDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGYG QEIVETLAEY
     AGVPVWNGLT NEFHPTQLLA DLLTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT
     GLDLRLVAPQ ACWPEAALVA ECSALAQKHG GKITLTEDIA SGVKGADFIY TDVWVSMGEP
     KEKWAERIAL LRDYQVNSKM MALTGNSQVK FLHCLPAFHD EQTTLGKKMA AEFGLYGGME
     VTDEVFESPA SIVFDQAENR MHTIKAVMVA TLAK
//
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