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Database: UniProt
Entry: A0A364KKN1_9EURO
LinkDB: A0A364KKN1_9EURO
Original site: A0A364KKN1_9EURO 
ID   A0A364KKN1_9EURO        Unreviewed;       374 AA.
AC   A0A364KKN1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Ornithine carbamoyltransferase, mitochondrial {ECO:0000256|ARBA:ARBA00021536};
DE            EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007};
DE   AltName: Full=Ornithine transcarbamylase {ECO:0000256|ARBA:ARBA00033269};
GN   ORFNames=BHQ10_000118 {ECO:0000313|EMBL:RAO64106.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO64106.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO64106.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO64106.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAO64106.1}.
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DR   EMBL; MIKG01000001; RAO64106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364KKN1; -.
DR   STRING; 1196081.A0A364KKN1; -.
DR   OrthoDB; 2782890at2759; -.
DR   Proteomes; UP000249363; Unassembled WGS sequence.
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:UniProt.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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   NCBIfam; TIGR00658; orni_carb_tr; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249363};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          48..192
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          208..359
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
SQ   SEQUENCE   374 AA;  40510 MW;  D21B6FBB0087C15C CRC64;
     MATSLNIGAV RTGLAPRLKQ AKPRTSMLRR TYTSATATTP PVSPFAPRHF LSIADLTPAE
     FTTLVRNASQ HKKTIKSGSV PRNLLGALSG KTVAMMFSKR STRTRISTEG AVAQLGGQPM
     FLGKDDIQLG VNESLYDTAV VVSSMVSCIV ARVGKHQEVA DLAKHSTVPV INALCDSFHP
     LQIVADFLTI HETFSARPTA GVNSLGMEGR KIAWVGDANN VLFDMAIAAA KMGVDLAVAT
     PKGYEIPSTM LEIIKQAGAG VQSPGKLIQT NVPEEAVKDA DVLVTDTWVS MGQEEETIKR
     MKAFEGFQIT SELAQRGGAK KDWKFMHCLP RHPEEVSDEV FYSRRSLVFP EAENRLWAAI
     SALEGFVVNK GKIE
//
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