OTC_NEIEL
ID OTC_NEIEL Reviewed; 232 AA.
AC Q9R3D1; O86383; Q9R809; Q9R810; Q9R811;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Ornithine carbamoyltransferase;
DE Short=OTCase;
DE EC=2.1.3.3;
DE Flags: Fragment;
GN Name=argF;
OS Neisseria elongata.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=495;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25295 / DSM 17712 / CCUG 2130 / CIP 72.27 / LMG 5124 / NCTC
RC 10660 / NRL 30006 / M2, ATCC 29315 / CIP 82.85 / CCUG 6508 / NCTC 11050,
RC CCUG 2131, CCUG 4165A, CCUG 4557, and NHITCC 2376;
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; AJ223898; CAA11629.1; -; Genomic_DNA.
DR EMBL; AJ223899; CAA11630.1; -; Genomic_DNA.
DR EMBL; AJ223900; CAA11631.1; -; Genomic_DNA.
DR EMBL; AJ223901; CAA11632.1; -; Genomic_DNA.
DR EMBL; AJ223902; CAA11633.1; -; Genomic_DNA.
DR EMBL; AJ223903; CAA11634.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9R3D1; -.
DR SMR; Q9R3D1; -.
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; 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; 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..>232
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000112959"
FT BINDING 15
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 66..69
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 167..168
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 204..207
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="Important for structural integrity"
FT /evidence="ECO:0000250"
FT VARIANT 5..6
FT /note="GV -> AL (in strain: CCUG 4165A)"
FT VARIANT 14
FT /note="S -> T (in strain: CCUG 4165A)"
FT VARIANT 45
FT /note="V -> I (in strain: NCTC 11050)"
FT VARIANT 51..53
FT /note="RYA -> CYP (in strain: CCUG 4165A)"
FT VARIANT 51
FT /note="R -> C (in strain: CCUG 4557)"
FT VARIANT 75
FT /note="L -> F (in strain: CCUG 4165A)"
FT VARIANT 81
FT /note="S -> C (in strain: NCTC 11050)"
FT VARIANT 84
FT /note="P -> T (in strain: CCUG 4165A and CCUG 4557)"
FT VARIANT 93
FT /note="V -> I (in strain: NHITCC 2376)"
FT VARIANT 148..151
FT /note="EDPQ -> DNPK (in strain: NCTC 11050)"
FT VARIANT 148..149
FT /note="ED -> DN (in strain: CCUG 4165A, CCUG 4557 and
FT NHITCC 2376)"
FT VARIANT 176
FT /note="H -> Q (in strain: CCUG 4165A, CCUG 4557, NHITCC
FT 2376 and NCTC 11050)"
FT VARIANT 187
FT /note="V -> F (in strain: NHITCC 2376)"
FT NON_TER 1
FT NON_TER 232
SQ SEQUENCE 232 AA; 25718 MW; 8BC2636F273DA433 CRC64;
DQGAGVTYLE PSGSQIGHKE SIKDTARVLG RMFDGIEYRG YGQEVVEELA RYAGVPVFNG
LTDEFHPTQI LADLLTMREH SGKPLQQTAY TYVGDARYNM GNSLLLIGAL LGMDTRIGAP
KALWPSENII AQAHSLAEKS GARLLLTEDP QEAVRGTDFI HTDVWVSMGE PKEVWHERID
LLRGYRVTAD LMAAAGNPQV KFMHCLPAFH NRETKVGEWI YKTFGLDGVE VT
