OTC_NEICI
ID OTC_NEICI Reviewed; 262 AA.
AC Q01322; O86378; O88141;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ornithine carbamoyltransferase;
DE Short=OTCase;
DE EC=2.1.3.3;
DE Flags: Fragment;
GN Name=argF;
OS Neisseria cinerea.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LNP 1646;
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=ATCC 14685 / DSM 4630 / CIP 73.16 / NCTC 10294 / NRL 30003,
RC LCDC 81-176, and Vedros M601;
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X64869; CAA46081.1; -; Genomic_DNA.
DR EMBL; AJ223890; CAA11621.1; -; Genomic_DNA.
DR EMBL; AJ223891; CAA11622.1; -; Genomic_DNA.
DR EMBL; AJ223892; CAA11623.1; -; Genomic_DNA.
DR PIR; S24718; S24718.
DR AlphaFoldDB; Q01322; -.
DR SMR; Q01322; -.
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_0000112958"
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 50
FT /note="G -> A (in strain: NCTC 10294)"
FT VARIANT 57..60
FT /note="AQET -> GQDV (in strain: Vedros M601 and LCDC 81-
FT 176)"
FT VARIANT 57
FT /note="A -> G (in strain: NCTC 10294)"
FT VARIANT 60
FT /note="T -> V (in strain: NCTC 10294)"
FT VARIANT 108
FT /note="I -> V (in strain: Vedros M601, LCDC 81-176 and NCTC
FT 10294)"
FT VARIANT 116
FT /note="A -> G (in strain: NCTC 10294)"
FT VARIANT 121
FT /note="V -> I (in strain: NCTC 10294)"
FT VARIANT 136..137
FT /note="KT -> QS (in strain: NCTC 10294)"
FT VARIANT 143..153
FT /note="NIVARARAVAE -> GIIAAAHAAAK (in strain: NCTC 10294)"
FT VARIANT 157
FT /note="G -> A (in strain: NCTC 10294)"
FT VARIANT 160
FT /note="L -> T (in strain: NCTC 10294)"
FT VARIANT 165..166
FT /note="TK -> AH (in strain: NCTC 10294)"
FT VARIANT 171..172
FT /note="GA -> NV (in strain: NCTC 10294)"
FT VARIANT 205
FT /note="E -> D (in strain: Vedros M601 and LCDC 81-176)"
FT VARIANT 209
FT /note="V -> A (in strain: Vedros M601, LCDC 81-176 and NCTC
FT 10294)"
FT VARIANT 213..214
FT /note="SK -> PQ (in strain: Vedros M601, LCDC 81-176 and
FT NCTC 10294)"
FT NON_TER 1
FT NON_TER 262
SQ SEQUENCE 262 AA; 29037 MW; 589D1721FD5E8B4A CRC64;
KTSTRTRCAF EVAARDQGAG VTYLEPSASQ IGHKESIKDT ARVLGRMYDG IEYRGFAQET
VEELAKYAGV PVFNGLTNEF HPTQMLADAL TMREHSGKPL NQTAFAYIGD ARYNMANSLL
VLGAKLGMDV RIGAPKTLWP SENIVARARA VAEETGGKIL LTENTKEAVK GADFIHTDVW
VSMGEPKEVW QERIDLLKDY RVTPELMAVS GNSKVKFMHC LPAFHNRETK VGEWIYETFG
LNGVEVTEEV FESPASIVFD QA
