ID B8MQB4_TALSN Unreviewed; 415 AA.
AC B8MQB4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=GMC type oxidoreductase, putative {ECO:0000313|EMBL:EED13316.1};
GN ORFNames=TSTA_058050 {ECO:0000313|EMBL:EED13316.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED13316.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; EQ962659; EED13316.1; -; Genomic_DNA.
DR RefSeq; XP_002487427.1; XM_002487382.1.
DR AlphaFoldDB; B8MQB4; -.
DR STRING; 441959.B8MQB4; -.
DR GeneID; 8108941; -.
DR VEuPathDB; FungiDB:TSTA_058050; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_3_1; -.
DR InParanoid; B8MQB4; -.
DR OrthoDB; 3714148at2759; -.
DR PhylomeDB; B8MQB4; -.
DR Proteomes; UP000001745; 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:SF111; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 2.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..415
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002877706"
FT DOMAIN 157..171
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 415 AA; 44489 MW; 77D730DAB50E8210 CRC64;
MGQLFFQVHL LAVAAIAVGV AARGGQGHGR HGTQPADYVI VGAGPAGLVL GEQLFVMEKR
ALSSLKLVRT ASTMLPLILL RCTLLLDPFF DAVQNELGLD EVDMTDGRGI GLDRGLSSIT
AINRTRSYGR TTAVSVTYRV DGKATTIKGK EIIVSGGAIN TPRLLLLSGV GPKETLKPPG
IEVVAGIPDV GSKLRDHALS IIELEVVPEI ILHTNVNRTG ILGSNNGFVY AAFRLPDSTW
DGIDSSHHTS LPEDCPHILL EFSALPFLAT PDSALTAWAS LFQPEGSGSV TINTADYTVD
PLIYTNYYST EAERAAIIVG FKILMNVIQN EEIKKLTINQ IYPTTPLTTD DEIWAVIQAQ
TDTFHHPMGT VAICIRVVDS STFPLPVTCH PQATVYALAN RAAKDIIAAD ADDEN
//
