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
//