ID   OTC_MYCBO               Reviewed;         307 AA.
AC   P0A5M9; A0A1R3XYY7; P94991; Q02095; X2BI29;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=argF; OrderedLocusNames=BQ2027_MB1684;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC   STRAIN=BCG;
RX   PubMed=1406593; DOI=10.1007/bf00538708;
RA   Timm J., van Rompaey I., Tricot C., Massaer M., Haeseleer F.,
RA   Fauconnier A., Stalon V., Bollen A., Jacobs P.;
RT   "Molecular cloning, characterization and purification of ornithine
RT   carbamoyltransferase from Mycobacterium bovis BCG.";
RL   Mol. Gen. Genet. 234:475-480(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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, which is a substrate for argininosuccinate
CC       synthetase, the enzyme involved in the final step in arginine
CC       biosynthesis. {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   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:1406593}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
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DR   EMBL; X64203; CAA45530.1; -; Genomic_DNA.
DR   EMBL; LT708304; SIU00287.1; -; Genomic_DNA.
DR   PIR; S26215; S26215.
DR   RefSeq; NP_855336.1; NC_002945.3.
DR   RefSeq; WP_003408165.1; NC_002945.4.
DR   AlphaFoldDB; P0A5M9; -.
DR   SMR; P0A5M9; -.
DR   EnsemblBacteria; SIU00287; SIU00287; BQ2027_MB1684.
DR   PATRIC; fig|233413.5.peg.1837; -.
DR   OMA; DGNNVCN; -.
DR   BRENDA; 2.1.3.3; 3494.
DR   UniPathway; UPA00068; UER00112.
DR   Proteomes; UP000001419; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Transferase.
FT   CHAIN           1..307
FT                   /note="Ornithine carbamoyltransferase"
FT                   /id="PRO_0000112956"
FT   BINDING         50..53
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         77
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         101
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         128..131
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         160
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         224
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         228..229
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         264..265
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         292
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   CONFLICT        217
FT                   /note="G -> A (in Ref. 1; CAA45530)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299
FT                   /note="L -> V (in Ref. 1; CAA45530)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   307 AA;  33057 MW;  7DC982EE07357F7E CRC64;
     MIRHFLRDDD LSPAEQAEVL ELAAELKKDP VSRRPLQGPR GVAVIFDKNS TRTRFSFELG
     IAQLGGHAVV VDSGSTQLGR DETLQDTAKV LSRYVDAIVW RTFGQERLDA MASVATVPVI
     NALSDEFHPC QVLADLQTIA ERKGALRGLR LSYFGDGANN MAHSLLLGGV TAGIHVTVAA
     PEGFLPDPSV RAAAERRAQD TGASVTVTAD AHAAAAGADV LVTDTWTSMG QENDGLDRVK
     PFRPFQLNSR LLALADSDAI VLHCLPAHRG DEITDAVMDG PASAVWDEAE NRLHAQKALL
     VWLLERS