ID G3BDX0_CANTC Unreviewed; 428 AA.
AC G3BDX0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Nucleotide-binding domain-containing protein {ECO:0000313|EMBL:EGV60402.1};
GN ORFNames=CANTEDRAFT_116454 {ECO:0000313|EMBL:EGV60402.1};
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:EGV60402.1, 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; EGV60402.1; -; Genomic_DNA.
DR RefSeq; XP_006689616.1; XM_006689553.1.
DR AlphaFoldDB; G3BDX0; -.
DR STRING; 590646.G3BDX0; -.
DR GeneID; 18248314; -.
DR KEGG; cten:CANTEDRAFT_116454; -.
DR eggNOG; KOG2820; Eukaryota.
DR HOGENOM; CLU_007884_0_1_1; -.
DR OrthoDB; 1952715at2759; -.
DR Proteomes; UP000000707; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR PANTHER; PTHR10961:SF7; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT DOMAIN 8..379
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 428 AA; 47732 MW; BD8FC5165A3FFE96 CRC64;
MSDDYDYDVL VVGCGVFGLS TCLELSKQGH KVLGLDAYPV PSELSAAKDY NKIIRVEYPD
ELSAKLAVEA LRCWENDELY KPYFVKSGRL TLTPGDSTSI RSQYENKSLE ILAKLGVTQS
FEKLTTPKQV ADTISHFKKN NLPAKFNSTY NADCGTGLSA DALKAVYERA TTSGAQFVFG
DDGRAVSIKS NEVRVKSGKI FTAKKIVVTA GASTGLIIPL DNQTKVFGTF VTHIKLTDAE
YEKYKDMPIF FSAEYGYFFP PDKVDHVIKI GVTTCDAWAE IDHPFEAGNK LRAPRYTVDH
PNETFPLGHE KDIKVLLNLV VPELADHELV DSKVCWIADS CDSYFLIDEC PYYKDVIVAT
GDSSHAFKFL PTIGKYISQK VNGALPADLS ETWKWRSNPS FDNGANTKSR FPRPHYNLEE
IKFIKSKL
//
