OTC_NEIMU
ID OTC_NEIMU Reviewed; 262 AA.
AC Q01326; O86399;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ornithine carbamoyltransferase;
DE Short=OTCase;
DE EC=2.1.3.3;
DE Flags: Fragment;
GN Name=argF;
OS Neisseria mucosa.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LNP 405;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-247.
RC STRAIN=Vedros M1801;
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; X64873; CAA46085.1; -; Genomic_DNA.
DR EMBL; AJ223896; CAA11627.1; -; Genomic_DNA.
DR PIR; S24727; S24727.
DR AlphaFoldDB; Q01326; -.
DR SMR; Q01326; -.
DR STRING; 435832.HMPREF0604_01626; -.
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_0000112967"
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 VARIANT 32
FT /note="R -> G (in strain: Vedros M1801)"
FT VARIANT 48
FT /note="Y -> F (in strain: Vedros M1801)"
FT VARIANT 97
FT /note="G -> D (in strain: Vedros M1801)"
FT VARIANT 103
FT /note="T -> V (in strain: Vedros M1801)"
FT VARIANT 123
FT /note="G -> A (in strain: Vedros M1801)"
FT VARIANT 137
FT /note="T -> S (in strain: Vedros M1801)"
FT VARIANT 145..149
FT /note="VARAR -> IETVQ (in strain: Vedros M1801)"
FT VARIANT 153
FT /note="E -> K (in strain: Vedros M1801)"
FT VARIANT 158
FT /note="K -> R (in strain: Vedros M1801)"
FT VARIANT 166
FT /note="E -> Q (in strain: Vedros M1801)"
FT VARIANT 209..211
FT /note="VSG -> AAE (in strain: Vedros M1801)"
FT NON_TER 1
FT NON_TER 262
SQ SEQUENCE 262 AA; 29063 MW; BDE7B8F8D1CC48B4 CRC64;
KTSTRTRCAF EVAARDQGAG VTYLEPSASQ IRHKESIKDT ARVLGRMYDG IEYRGFGQDV
VEELAKYAGV PVFNGLTNEF HPTQMLADAL TMREHSGKPL NQTAFAYVGD ARYNMANSLL
VLGAKLGMDV RIGAPKTLWP SENIVARARA VAEETGGKIL LTENAEEAVK GVDFIHTDVW
VSMGEPKEAW QERIDLLKDY RVTPELMAVS GNPQVKFMHC LPAFHNRETK VGEWIYETFG
LNGVEVTEEV FESSASIVFD QA
