ID   W6MKN4_9ASCO            Unreviewed;       511 AA.
AC   W6MKN4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=KUCA_T00002933001 {ECO:0000313|EMBL:CDK26956.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK26956.1};
RN   [1] {ECO:0000313|EMBL:CDK26956.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26956.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK26956.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26956.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; HG793127; CDK26956.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MKN4; -.
DR   STRING; 1382522.W6MKN4; -.
DR   HOGENOM; CLU_017779_3_3_1; -.
DR   OrthoDB; 1664005at2759; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF117; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          73..251
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   511 AA;  55592 MW;  4EC3F94795F760F9 CRC64;
     MKSDDAKFSE ALLTRSTIAL TEVTQPKYCN GEEFLEGVEL FKKVLGAANV SVDQDQLLLH
     SNNPACTHHP PKEGQVPECV VYPESTEQVV EMLKISNRLR IPVVPFGAGS SLEGHIYSTR
     QPCVVVDLRR MNKILEIHDD DMDVVVQAGV PYGEVNRVLE PYGLMMGSDC APDAVIGGMI
     ATNASGINAC AYGPMRDNVI SATVVLADGT VVKTKQRPRK SSAGYNLTGL VVGSEGTLGI
     VTQATIKVHV KPKHEKVAVV QFKSVEEATT AVTKILKSGI KLNAIELLDA NMMRCINYAG
     SSSRTWDNAP SLFLKINGVN PVITNELVKE VKTIANGSGA IRFTLAKDEA EAKELFDIRK
     NAHYSVLEYT YGTIGDDGRM WGTDVAVPLS KLTPVLEASH RDLDKANIDY VILGHVGDSN
     FHFNVLYKPE QESVVRAIVD KMVYTGLANE GTCTGEHGVG NGKRKYLEAE LGPDAINLMR
     KLKLAVDPNR IMNPDKVFAI DPFDTIDSYS A
//