OTC_NEIMB
ID OTC_NEIMB Reviewed; 331 AA.
AC P0DH57; Q9JYI3; Q9R812; Q9S6H2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Ornithine carbamoyltransferase;
DE Short=OTCase;
DE EC=2.1.3.3;
GN Name=argF; OrderedLocusNames=NMB1573;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CDC 8201085 / NMB / Serogroup B;
RA Kahler C.M., Stephens D.S.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-314.
RC STRAIN=CCUG 23094 / S3446 / Serogroup B / Serotype 14,
RC CCUG 23103 / M470 / Serogroup B, HF130 / Serogroup B / Serotype NT, and
RC P63 / Serogroup B / Serotype NT / Subtype 2;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-299.
RC STRAIN=NCTC 8249 / Serogroup B;
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; AF125563; AAD32177.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF41926.1; -; Genomic_DNA.
DR EMBL; X64861; CAA46073.1; -; Genomic_DNA.
DR EMBL; X64862; CAA46074.1; -; Genomic_DNA.
DR EMBL; X64863; CAA46075.1; -; Genomic_DNA.
DR EMBL; X64868; CAA46080.1; -; Genomic_DNA.
DR EMBL; AJ223888; CAA11619.1; -; Genomic_DNA.
DR PIR; E81066; E81066.
DR PIR; S24734; S24734.
DR RefSeq; NP_274579.1; NC_003112.2.
DR RefSeq; WP_002212820.1; NC_003112.2.
DR AlphaFoldDB; P0DH57; -.
DR SMR; P0DH57; -.
DR STRING; 122586.NMB1573; -.
DR PaxDb; P0DH57; -.
DR EnsemblBacteria; AAF41926; AAF41926; NMB1573.
DR GeneID; 61281739; -.
DR KEGG; nme:NMB1573; -.
DR PATRIC; fig|122586.8.peg.2024; -.
DR HOGENOM; CLU_043846_3_1_4; -.
DR OMA; VYVKNWS; -.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000000425; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_01109; OTCase; 1.
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 InterPro; IPR024904; OTCase_ArgI.
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.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..331
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000112965"
FT BINDING 55..58
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 82
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 106
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 133..136
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 166
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 230
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 234..235
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 272..273
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 317
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT VARIANT 302
FT /note="I -> V (in strain: NMB, HF130 and P63)"
SQ SEQUENCE 331 AA; 36716 MW; B169D6C717FA1C81 CRC64;
MNLKNRHFLK LLDFTPEEIT AYLDLAAELK AAKKAGREIQ RMKGKNIALI FEKTSTRTRC
AFEVAARDQG AGVTYLEPSA SQIGHKESIK DTARVLGRMY DAIEYRGFGQ EVVEELAKYA
GVPVFNGLTN EFHPTQMLAD ALTMREHSGK PLNQTAFAYV GDARYNMGNS LLILGAKLGM
DVRIGAPQSL WPSEGIIAAA HAAAKETGAK ITLTENAHEA VKNVDFIHTD VWVSMGEPKE
VWQERIDLLK DYRVTPELMA ASGNPQVKFM HCLPAFHNRE TKVGEWIYET FGLNGVEVTE
EIFESPASIV FDQAENRMHT IKAVMVAALG D
