ID B8MJ57_TALSN Unreviewed; 620 AA.
AC B8MJ57;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=GMC oxidoreductase, putative {ECO:0000313|EMBL:EED15719.1};
GN ORFNames=TSTA_051560 {ECO:0000313|EMBL:EED15719.1};
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:EED15719.1, 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; EQ962657; EED15719.1; -; Genomic_DNA.
DR RefSeq; XP_002485672.1; XM_002485627.1.
DR AlphaFoldDB; B8MJ57; -.
DR STRING; 441959.B8MJ57; -.
DR GeneID; 8103377; -.
DR VEuPathDB; FungiDB:TSTA_051560; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_3_1; -.
DR InParanoid; B8MJ57; -.
DR OMA; HGCSWWH; -.
DR OrthoDB; 858083at2759; -.
DR PhylomeDB; B8MJ57; -.
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:SF138; DEHYDROGENASE PKFF-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..620
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002877632"
FT DOMAIN 54..376
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 476..604
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 549
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 593
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 594..595
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 620 AA; 67435 MW; BC1E0FD5C19F03D2 CRC64;
MSSFKLGLTT LVFVTCTILG THAQVPQHFN FFDYGQRGPL LGSHFGPPAT NATFDYVIAG
GGNTGLTIAT RLAQTGASVA VIEAGGFYEV DNGNLSIVPG YATFFTGSDL DNYSPLVDWG
FAKTPQPELG NRRLHYARGK TLGGSSARNY MLYQRVTVDS MQQWADEVDD QSYTWEAFLP
YYQKSINYTP PGQKLYTNSS NKQDPNAFSC TGGPLKVSFS NFVDPFGTWA QQAFIKVNMT
EIEGLDSGKL LGSAYATLTI DSRNAWRETS ESSFLMHALN AGLPVTIYKS SLARKIIFDS
NNTATGVQVF AACFSGTQSM NFTLTARKEV IVSAGVFQSP QLLMVSGIGP CDELADFGIT
CISNLIGVGQ NMQDHPIFGS AHRVNVHTAS ASLNNATLSA LSVQSYINNA TGPLSIFGPG
IYGWEKLPEP YRSQLSNQSR GVLDIGAYNG YNLNKETADP RDGHNYATLN TALVAPLSRG
TVKIQSNSMT EPPIINPNWL ADQTDRDLAI QSFKRQREIW DILAHLGSNY TTDSQIKQIT
AESMNTVYHA SATCKMGKKG DPMAVLDSHA RVYGVQNLRV VDASSFPYLP PGHPQALVYA
LAEKVADLIR AQYLHFSAAF
//
