ID   OTC_PACTA               Reviewed;         347 AA.
AC   P14995;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Ornithine transcarbamylase, mitochondrial {ECO:0000305|PubMed:2327179};
DE            Short=OTCase {ECO:0000303|PubMed:2327179};
DE            EC=2.1.3.3 {ECO:0000250|UniProtKB:P00480};
DE   AltName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE   Flags: Precursor;
GN   Name=OTC;
OS   Pachysolen tannophilus (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX   NCBI_TaxID=4918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 32691 / BCRC 20329 / CBS 4044 / DSM 70352 / NBRC 1007 / NRRL
RC   Y-2460;
RX   PubMed=2327179; DOI=10.1002/yea.320060208;
RA   Skrzypek M., Borsuk P., Maleszka R.;
RT   "Cloning and sequencing of the ornithine carbamoyltransferase gene from
RT   Pachysolen tannophilus.";
RL   Yeast 6:141-148(1990).
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: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X15412; CAA33458.1; -; Genomic_DNA.
DR   PIR; S08643; OWCKPT.
DR   AlphaFoldDB; P14995; -.
DR   SMR; P14995; -.
DR   PRIDE; P14995; -.
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..25
FT                   /note="Mitochondrion"
FT   CHAIN           26..347
FT                   /note="Ornithine transcarbamylase, mitochondrial"
FT                   /id="PRO_0000020345"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         84..87
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         135
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         162
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         165
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         194
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         258
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         262
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         263
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         300..301
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         328
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
SQ   SEQUENCE   347 AA;  38313 MW;  7B89324C829F7CB4 CRC64;
     MINSISNTVL LKSVVSKRFF SSSAKMSSQA KPRHLVSMLE LSIKELESLV NRAAYHKQQI
     RSGLVNTTQP LSGKTVSLIF NKRSTRTRVS SEGAAAYLGG CPMFLGKDDI QLGVNESLHD
     TTKIISSMTS SIFARVNKHS DIQEMCKYSS VPIINALCDT FHPLQAITDI LTIKESFGNT
     TKGLKLAWIG DVNNVINDLC IAALKSGIDV SIAVPSGLKF EELILSGAKE ISAENGTTLK
     ITNDPLEAIN GANVIVTDTW ISMGQEDERL QKLKQFEGFQ ITKEMISKGK AAENWKFMHC
     LPRHPEEVHD EVFYDEERSL VFEEGENRLY AAIAVLEGFV VNKGKLL