ID   OTC_NEIFV               Reviewed;         232 AA.
AC   O86385;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
DE   Flags: Fragment;
GN   Name=argF;
OS   Neisseria flava.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=34026;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangor 9;
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, recA,
RT   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 from
CC       carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC       produce L-citrulline. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC         phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:58228; EC=2.1.3.3;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
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DR   EMBL; AJ223894; CAA11625.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86385; -.
DR   SMR; O86385; -.
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; IPR036901; Asp/Orn_carbamoylTrfase_sf.
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; 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; Transferase.
FT   CHAIN           <1..>232
FT                   /note="Ornithine carbamoyltransferase"
FT                   /id="PRO_0000112961"
FT   BINDING         15
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..69
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..207
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="Important for structural integrity"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         232
SQ   SEQUENCE   232 AA;  25623 MW;  FE5CD32F644FC490 CRC64;
     DQGAGVTYLE PSASQIGHKE SIKDTARVLG RMYDGIEYRG FGQDVVEELA KYAGVPVFNG
     LTNEFHPTQM FADALTMREH SGKPLNQTAF AYVGDARYNM ANSLLVLGAK LGMDVRIGAP
     KTLWPSENIV ARARAVAEET GGKILLTENA EEAVKGADFI HTDVWVSMGE PKEAWQERID
     LLKDYRVTPE LMAASGNPQV KFMHCLPAFH NRETKVGEWI YETFGLNGVE VT