OTC_NEIPO
ID OTC_NEIPO Reviewed; 262 AA.
AC Q01327; P95397; P95398;
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 polysaccharea.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=489;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43768 / DSM 22809 / CCUG 18030 / CIP 100113 / NCTC 11858 / LNP
RC N 462;
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=CCUG 18031, CCUG 24845 / N6817, CCUG 24846 / N6665, and INS MA3008;
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; X64870; CAA46082.1; -; Genomic_DNA.
DR EMBL; Y10878; CAA71828.1; -; Genomic_DNA.
DR EMBL; Y10879; CAA71829.1; -; Genomic_DNA.
DR EMBL; Y10880; CAA71830.1; -; Genomic_DNA.
DR EMBL; Y10881; CAA71831.1; -; Genomic_DNA.
DR PIR; S24749; S24749.
DR AlphaFoldDB; Q01327; -.
DR SMR; Q01327; -.
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_0000112970"
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 21
FT /note="A -> V (in strain: INS MA3008)"
FT VARIANT 61
FT /note="V -> I (in strain: CCUG 24846)"
FT VARIANT 136
FT /note="E -> Q (in strain: CCUG 24846)"
FT VARIANT 146
FT /note="A -> T (in strain: CCUG 24846 and INS MA3008)"
FT VARIANT 151
FT /note="A -> V (in strain: CCUG 24846 and INS MA3008)"
FT VARIANT 171..173
FT /note="GVG -> NVD (in strain: CCUG 24846 and INS MA3008)"
FT NON_TER 1
FT NON_TER 262
SQ SEQUENCE 262 AA; 28781 MW; F1457F8FBBC7EB6D CRC64;
KTSTRTRCAF EVAARDQGAG ATYLEPSASQ IGHKESIKDT ARVLGRMYDA IEYRGFGQEI
VEELAKYAGV PVFNGLTNEF HPTQMLADAL TMREHSSKPL NQTAFAYVGD ARYNMGNSLL
ILGAKLGMDV RIGAPESLWP SEGIIAAAHA AAKETGAKIT LTENAHEAVK GVGFIHTDVW
VSMGEPKEVW QERIDLLKDY RVTPELMAAS GNPQVKFMHC LPAFHNRETK VGEWIYETFG
LNGVEVTEEV FESPASIVFD QA
