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Database: UniProt
Entry: O86408
LinkDB: O86408
Original site: O86408 
ID   OTC_NEIPH               Reviewed;         232 AA.
AC   O86408;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   01-OCT-2014, entry version 69.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
DE   Flags: Fragment;
GN   Name=argF;
OS   Neisseria pharyngis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=29434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCTC 4590 / Flava;
RX   PubMed=10368955; DOI=10.1093/oxfordjournals.molbev.a026162;
RA   Smith N.H., Holmes E.C., Donovan G.M., Carpenter G.A., Spratt B.G.;
RT   "Networks and groups within the genus Neisseria: analysis of argF,
RT   recA, rho, and 16S rRNA sequences from human Neisseria species.";
RL   Mol. Biol. Evol. 16:773-783(1999).
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; AJ223905; CAA11636.1; -; Genomic_DNA.
DR   ProteinModelPortal; O86408; -.
DR   SMR; O86408; 1-232.
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:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1370; -; 2.
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   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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Transferase.
FT   CHAIN        <1   >232       Ornithine carbamoyltransferase.
FT                                /FTId=PRO_0000112969.
FT   REGION       66     69       Carbamoyl phosphate binding.
FT                                {ECO:0000250}.
FT   REGION      167    168       Ornithine binding. {ECO:0000250}.
FT   REGION      204    207       Carbamoyl phosphate binding.
FT                                {ECO:0000250}.
FT   BINDING       4      4       Carbamoyl phosphate. {ECO:0000250}.
FT   BINDING      15     15       Carbamoyl phosphate. {ECO:0000250}.
FT   BINDING      39     39       Carbamoyl phosphate. {ECO:0000250}.
FT   BINDING      99     99       Ornithine. {ECO:0000250}.
FT   BINDING     163    163       Ornithine. {ECO:0000250}.
FT   BINDING     232    232       Carbamoyl phosphate. {ECO:0000250}.
FT   SITE         79     79       Important for structural integrity.
FT                                {ECO:0000250}.
FT   NON_TER       1      1
FT   NON_TER     232    232
SQ   SEQUENCE   232 AA;  25640 MW;  3223C9ADDC2EF01E CRC64;
     DQGAGVTYLE PSASQIGHKE SIKDTARVLG RMYDGIEYRG FGQDVVEELA KYAGVPVFNG
     LTNEFHPTQM LADALTMREH SGKPLSQTAF AYVGDARYNM ANSLLVLGAK LGMDVRIGAP
     KTLWPSEHIV ARARAVAKET GGRILLTENA EEAVKGVDFI HTDVWVSMGE PKEAWQERID
     LLKDYRVTPE LMAASGNPQV KFMHCLPAFH NRETKVGEWI YETFGLNGVE VT
//
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