OTC_NEILA
ID OTC_NEILA Reviewed; 262 AA.
AC Q01324; O86391; P95366; P95367; Q9R813; Q9R814;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ornithine carbamoyltransferase;
DE Short=OTCase;
DE EC=2.1.3.3;
DE Flags: Fragment;
GN Name=argF;
OS Neisseria lactamica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23970 / DSM 4691 / CCUG 5853 / CIP 72.17 / NCTC 10617 / NCDC
RC A7515;
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 23971 / CIP 102541 / NCTC 10618 / NCDC A5906, CCUC 7757,
RC CCUG 7852, LCDC 77-143, LCDC 80-111, and LCDC 845;
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; X64871; CAA46083.1; -; Genomic_DNA.
DR EMBL; AJ223884; CAA11615.1; -; Genomic_DNA.
DR EMBL; AJ223885; CAA11616.1; -; Genomic_DNA.
DR EMBL; AJ223886; CAA11617.1; -; Genomic_DNA.
DR EMBL; AJ223887; CAA11618.1; -; Genomic_DNA.
DR EMBL; Y10876; CAA71826.1; -; Genomic_DNA.
DR EMBL; Y10877; CAA71827.1; -; Genomic_DNA.
DR PIR; S24723; S24723.
DR AlphaFoldDB; Q01324; -.
DR SMR; Q01324; -.
DR STRING; 486.B2G52_10125; -.
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_0000112963"
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 26
FT /note="S -> P (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 36
FT /note="S -> R (in strain: CCUC 7757)"
FT VARIANT 60
FT /note="T -> V (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 96
FT /note="G -> S (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 103
FT /note="T -> I (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 136..137
FT /note="EG -> QS (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 140
FT /note="P -> A (in strain: CCUG 7852)"
FT VARIANT 149..153
FT /note="NAVAE -> HAAAK (in strain: LCDC 845)"
FT VARIANT 149..151
FT /note="NAV -> HAA (in strain: CCUC 7757)"
FT VARIANT 150
FT /note="A -> R (in strain: LCDC 77-143)"
FT VARIANT 163..165
FT /note="ANP -> ENA (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 171..173
FT /note="GVG -> NVD (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 189
FT /note="I -> V (in strain: CCUC 7757, CCUG 7852, LCDC 80-111
FT and LCDC 845)"
FT VARIANT 199
FT /note="D -> N (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 204
FT /note="S -> P (in strain: CCUC 7757 and LCDC 845)"
FT VARIANT 214
FT /note="Q -> K (in strain: CCUG 7852 and LCDC 80-111)"
FT VARIANT 231
FT /note="I -> V (in strain: CCUC 7757 and LCDC 845)"
FT NON_TER 1
FT NON_TER 262
SQ SEQUENCE 262 AA; 28665 MW; 41F593C81A5078CC CRC64;
KTSTRTRCAF EVAARDQGAG VTYLESSASQ IGHKESIKDT ARVLGRMYDA IEYRGFGQET
VEELAKYAGV PVFNGLTNEF HPTQMLADAL TMREHGGKPL NQTSFAYVGD ARYNMGNSLL
ILGAKLGMDV RIGAPEGLWP SEGIIAAANA VAEETGAKIT LTANPQEAVK GVGFIHTDVW
VSMGEPKEIW QERIDLLKDY RVTSELMAAS GNPQVKFMHC LPAFHNRETK IGEWIYETFG
LNGVEVTEEV FESPAGIVFD QA
