ID   OTC_ASPTE               Reviewed;         361 AA.
AC   P0C2P2; Q00291; Q0CLE2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE            EC=2.1.3.3;
DE   AltName: Full=Ornithine transcarbamylase;
DE            Short=OTCase;
DE   Flags: Precursor;
GN   Name=arg1; Synonyms=arg-1;
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10690 / CBS 377.64 / CECT 2663 / IFO 6346 / NRRL 571;
RX   PubMed=9141661; DOI=10.1111/j.1574-6968.1997.tb10330.x;
RA   Ventura L., Perez-Gonzalez J.A., Ramon D.;
RT   "Cloning and molecular analysis of the Aspergillus terreus arg1 gene coding
RT   for an ornithine carbamoyltransferase.";
RL   FEMS Microbiol. Lett. 149:207-212(1997).
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; Z67741; CAA91554.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C2P2; -.
DR   SMR; P0C2P2; -.
DR   PRIDE; P0C2P2; -.
DR   EnsemblFungi; EAU34561; EAU34561; ATEG_05492.
DR   VEuPathDB; FungiDB:ATEG_05492; -.
DR   OMA; DGNNVCN; -.
DR   UniPathway; UPA00068; UER00112.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:1903269; C:ornithine carbamoyltransferase inhibitor complex; IEA:EnsemblFungi.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:EnsemblFungi.
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..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..361
FT                   /note="Ornithine carbamoyltransferase, mitochondrial"
FT                   /id="PRO_0000042693"
FT   ACT_SITE        315
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         89..92
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         140
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         167
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         170
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         207
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         273
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         277
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         278
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         315..316
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         342
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
SQ   SEQUENCE   361 AA;  39129 MW;  9306AD775E499D75 CRC64;
     MIPTARCGAL RQKIPVQAVR QYSSSTTLKT SPFAPRHLLS IADLTPTEFT TLVRNASSHK
     HSIKSGSIPT NLQGSLAGKT VAMMFSKRST RTRISTEGAT VQLGGHPMFL GKDDIQLGVN
     ESLYDTAVVV SSMVSAIVAR VGKHAEVADL AKHSTVPVIN ALCDSFHPLQ AIADFQTIYE
     TFTPKAHHLS SLGLEGLKIA WVGDANNVLF DMAISAAKMG VDLAVATPKG YEIPASMREL
     IQEAGKGVAN PGKLIQTNVP EEAVKKADIL VTDTWVSMGQ EEESLKRMKA FEGFQITSEL
     AKRGGANENW KFMHCLPRHP EEVSDEVFYS NRSLVFPEAE NRLWAAISAL EGFVVNKGKI
     A