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Database: UniProt
Entry: G3BCP1_CANTC
LinkDB: G3BCP1_CANTC
Original site: G3BCP1_CANTC 
ID   G3BCP1_CANTC            Unreviewed;       572 AA.
AC   G3BCP1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=CANTEDRAFT_128518 {ECO:0000313|EMBL:EGV60842.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV60842.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; GL996528; EGV60842.1; -; Genomic_DNA.
DR   RefSeq; XP_006690056.1; XM_006689993.1.
DR   AlphaFoldDB; G3BCP1; -.
DR   STRING; 590646.G3BCP1; -.
DR   GeneID; 18249312; -.
DR   KEGG; cten:CANTEDRAFT_128518; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_017779_3_3_1; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        43..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          138..315
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   572 AA;  63891 MW;  D5E6B0836CF5AE0A CRC64;
     MYLRGDDFRE PKGQMSQSHR ELTSRDLCII VYNSNHILMS RYLFSRTAAV VGAVAASSFA
     TYTLTRAHLQ SNLPSDWFPN ESTTKLHSIS TPQYATPSQL QHAIRELRDV LGDTNVVNTP
     VVLEYHTRNE FNPHEPKPHE KPKYVIYPRS TNDVSEAMAI LNRYRVPVVP FSGGTSLEGH
     FYSTREGIVM DTSKMDQVLA INSEDLDVQV QAGVNWVRLN EQLAPHQLMI GSDCGPDGLI
     SGMINTNASG INASKYGAMI SNVISLTVVL PDGKIVRTKQ RPRKSSSGYS LTQLFVGSEG
     TLGIVTEATL KLHPIPRYET VIVGQFPTLL DSTKTVSQLY RAGVHPNAIE LLDRDMMHCI
     NYSGYFTQEW AEVPTLFFKV GGMSKAMVDE QVKVLKEISV KNNCKDFIAA KSEEEGKELF
     SARKNAFYAI LNYGRNEIDP DIRLWVTDIA VPLSKLPPVL DQIYAMIRES GFQSVILAHA
     GDANFHCDVF YKDHEKDKCE SLINKMMDLG LVNEGTASGE HGIGNGKRTF LIQELGQDAV
     DLMRRIKLAV DPNRILNPDK IFKIDPNDKG EF
//
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