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 01-MAY-2013, entry version 75.
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 (By similarity).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the ATCase/OTCase family.
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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; RLMDFTP; -.
DR ProtClustDB; PRK12562; -.
DR UniPathway; UPA00068; UER00112.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:HAMAP.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
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; Asp/Orn_carbamoyltranf; 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 (By similarity).
FT CHAIN 2 334 Ornithine carbamoyltransferase.
FT /FTId=PRO_0000112920.
FT REGION 56 60 Carbamoyl phosphate binding (By
FT similarity).
FT REGION 134 137 Carbamoyl phosphate binding (By
FT similarity).
FT REGION 236 237 Ornithine binding (By similarity).
FT REGION 273 276 Carbamoyl phosphate binding (By
FT similarity).
FT BINDING 10 10 Carbamoyl phosphate (By similarity).
FT BINDING 72 72 Carbamoyl phosphate (By similarity).
FT BINDING 83 83 Carbamoyl phosphate (By similarity).
FT BINDING 107 107 Carbamoyl phosphate (By similarity).
FT BINDING 168 168 Ornithine (By similarity).
FT BINDING 232 232 Ornithine (By similarity).
FT BINDING 302 302 Carbamoyl phosphate (By similarity).
FT BINDING 320 320 Carbamoyl phosphate (By similarity).
FT SITE 31 31 Important for structural integrity (By
FT similarity).
FT SITE 147 147 Important for structural integrity (By
FT similarity).
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
//
