ID   OTC_TRAHI               Reviewed;         375 AA.
AC   P78605; P78606;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE            EC=2.1.3.3;
DE   AltName: Full=Ornithine transcarbamylase;
DE            Short=OTCase;
DE   Flags: Precursor;
OS   Trametes hirsuta (White-rot fungus) (Coriolus hirsutus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=5327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 4917;
RA   Tsukamoto A., Kono S., Tatarazako N., Sugiura J., Sakaino M., Kita Y.;
RT   "Cloning and characterization of the ornithine carbamoyltransferase gene
RT   from the white-rot basidiomycete Coriolus hirsutus.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
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DR   EMBL; D26061; BAA05060.1; -; Genomic_DNA.
DR   EMBL; D26062; BAA05061.1; -; Genomic_DNA.
DR   AlphaFoldDB; P78605; -.
DR   SMR; P78605; -.
DR   UniPathway; UPA00068; UER00112.
DR   GO; GO:0005759; C:mitochondrial matrix; 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.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Mitochondrion; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..375
FT                   /note="Ornithine carbamoyltransferase, mitochondrial"
FT                   /id="PRO_0000020347"
FT   ACT_SITE        318
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         78..81
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         129
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         156
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         159
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         212
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         276
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         280
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         281
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         318..319
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         345
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   CONFLICT        237
FT                   /note="K -> R (in Ref. 1; BAA05061)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   375 AA;  41294 MW;  B75F9073980C853A CRC64;
     MALSTKVPHL MTLADLTPGQ IQRIITHSYH LKRTAQPWLA PQGRAGSGGK YSNAPHKLRM
     PSQSLFSKSI ALLFSKRSTR TRLSAETAAL LLGGQALFLG REDIQLGVNE TVPDSARVIG
     GMCQGIFARV GDHSEIEELA RYSPVPVLNA LSSLWHPTQV LADILTLHEH AALFDPASAS
     PTPSAADAFS QKYTKLGEVR PLTVAYVGDS ANVLHDMLVT YPRLGHQLRV ASPENDKYRA
     PKAVWDRVVE LGCDKNIFWT ADPRAAVKGA DLVVTDTWIS MGQEAEKAQR LKDFAGYQVT
     EALCREGGAN PDWKFMHCLP RKQDEVDDEV FYGPRSLVFQ ESDNRKWTIM ALFDLLFGKW
     SLLARNGEGA DAGSE