ID   OTC_NEIFL               Reviewed;         262 AA.
AC   Q01323;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
DE   Flags: Fragment;
GN   Name=argF;
OS   Neisseria flavescens.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LNP 444;
RX   PubMed=1406254; DOI=10.1111/j.1365-2958.1992.tb01387.x;
RA   Zhou J., Spratt B.G.;
RT   "Sequence diversity within the argF, fbp and recA genes of natural isolates
RT   of Neisseria meningitidis: interspecies recombination within the argF
RT   gene.";
RL   Mol. Microbiol. 6:2135-2146(1992).
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; X64872; CAA46084.1; -; Genomic_DNA.
DR   PIR; S24719; S24719.
DR   AlphaFoldDB; Q01323; -.
DR   SMR; Q01323; -.
DR   STRING; 596320.NEIFL0001_1802; -.
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; 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; 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; Transferase.
FT   CHAIN           <1..>262
FT                   /note="Ornithine carbamoyltransferase"
FT                   /id="PRO_0000112960"
FT   BINDING         3..7
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..84
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         182..183
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..222
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   SITE            94
FT                   /note="Important for structural integrity"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         262
SQ   SEQUENCE   262 AA;  29205 MW;  1446FF7DA474BF70 CRC64;
     KTSTRTRCAF EVAARDQGAG VTYLEPSASQ IGHKESIKDT ARVLGRMFDG IEYRGFGQDV
     VEELAKYAGV PVFNGLTNEF HPTQMLADGL TMREHSDKPL NQIAFAYVGD ARYNMANSLL
     VLAAKLGMDV RISAPKSLWP SENIIEMVQA VAKETGGRIL LTENVQEAVK GVDFIHTDVW
     VSMGEPKEAW QERIDLLKDY RVTPELMAAA ENPQVKFMHC LPAFHNRETK VGEWIYETFG
     LNGVEVTEEV FESEASIVFD QA