ID D4AZH9_ARTBC Unreviewed; 359 AA.
AC D4AZH9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=ARB_01597 {ECO:0000313|EMBL:EFE31449.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE31449.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE31449.1}.
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DR EMBL; ABSU01000021; EFE31449.1; -; Genomic_DNA.
DR RefSeq; XP_003012089.1; XM_003012043.1.
DR AlphaFoldDB; D4AZH9; -.
DR STRING; 663331.D4AZH9; -.
DR GeneID; 9519576; -.
DR KEGG; abe:ARB_01597; -.
DR eggNOG; KOG1504; Eukaryota.
DR HOGENOM; CLU_043846_3_0_1; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 2782890at2759; -.
DR Proteomes; UP000008866; 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:UP000008866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT DOMAIN 30..174
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 193..344
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
SQ SEQUENCE 359 AA; 39027 MW; 90BDF399802ECBCB CRC64;
MHSILRRRCI GHVAKLQSRT YATPSAIPPR HLLSIADLTP AEFTALVRNG LSHKQAIKSG
SIPQSLRGAL SGQTVAMVFH KRSTRTRVST EAAVTRMGGH PMFLGKDDIQ LGVNESLYDT
SVVLSSMVSC IVARVGPHSD VANLAKHSAV PVINALCDTF HPLQTIADFI TIKETFAPQL
TPGQSTSPSL GLEGLKIAWV GDANNVLFDL AIGATKMGVD VAVATPKGYE MPTHIVDLVK
HAGEGVQTPG SLTQTYSPEE AVKKADVIVT DTWVSMGQEE EKLQRLKAFE NFQVTSELAR
RGGANEGWRF MHCLPRHPEE VSDEVFYGKR SLVFPEAENR LWAAISAIQS FVVQKGRIV
//
