ID H6CA69_EXODN Unreviewed; 657 AA.
AC H6CA69;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Aryl-alcohol dehydrogenase {ECO:0000313|EMBL:EHY60033.1};
GN ORFNames=HMPREF1120_08006 {ECO:0000313|EMBL:EHY60033.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY60033.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY60033.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY60033.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH226136; EHY60033.1; -; Genomic_DNA.
DR RefSeq; XP_009160494.1; XM_009162246.1.
DR AlphaFoldDB; H6CA69; -.
DR STRING; 858893.H6CA69; -.
DR GeneID; 20312645; -.
DR VEuPathDB; FungiDB:HMPREF1120_08006; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_0_1; -.
DR InParanoid; H6CA69; -.
DR OMA; GINYMMY; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 114..137
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 307..321
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 271
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 657 AA; 71099 MW; 6D750E3F02447B1A CRC64;
MTNTNGVTGL DGVNGTDGSG KSGHVSVEEF VQQQSYDYII CGGGTAGLTV AARLTENPEV
TVGVIEAGKN RLGDALVDTP ALFLQMLGNK EYDWTFDTVP QVGNKSKIHH VPRGRALGGS
SAINYMMYVR GSDHDYDDWA ELANDPAWSS AKLKEYMRKH QSLEPIDEQV IDRTCMPFVG
DNHGTSGPVR TSFNDFRLPL EDDIVKAADQ ATGFDKKPID PWSGDHIGFY NTLGTVVRTG
ADKGKRSYAA RGYFQANQHR PNLKVITESL VSRVILDENK TATGVEFIHN GHKHTIRANR
EVIVAGGAIN TPQILELSGI GDPKVLEAAG IECLVELPSV GTNYQDHVVS AIVYQLAPDQ
MSGDSIYKPE VMAEAQKALA EMQGGPLTSI QSVQGFFPCS LFLEPGELDE IVASTRKTQE
DPSTPAFQKK QLDKVIAHLR DPHSANLQFV FIAATADMVH GVQDQSKLWP PPSDTSGATP
DGITLAVCVQ YPVSRGHVHI RSADPTAYPE VDPGYLSHEA DVAVLAAGIK FIESLARAPA
LQGKLGPRIQ PSRKDFPHLD TVDARRAAVR EFCLGEYHSC GSCAMGDTVD SRLRVLGGVK
KLRVVDASVF PNNVSGNIVS SVYMLAEKAA DLIKEDWEFD VLGKVKAQVQ AKAEKGP
//
