ID A0A0F7ZG43_9HYPO Unreviewed; 586 AA.
AC A0A0F7ZG43;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=HIM_10355 {ECO:0000313|EMBL:KJZ70241.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ70241.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ70241.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ70241.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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; KQ030637; KJZ70241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZG43; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000054481; 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 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; PTHR47190:SF1; -; 1.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000054481};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..586
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002525686"
FT DOMAIN 281..295
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 243
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 544..545
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 586 AA; 63253 MW; B2CEC5CED6B0A46F CRC64;
MKLLSTFLVG TLVQLSNAAP TAQDWASQQW DAIVIGAGTA GIIVADRLSE AGLKTLLLEQ
GGNSYGITGG TEKPEWLKGT NMSRVDVPGL YSTIFAGKSS LLCPDGVVNA YQACTIGGNS
AINAGLYFQP PASDWDNFHP PGWHSADVKA ATDRLLRRQP PVTKYSSDDQ FYVQSGYDAV
REWIVDGVGY KDVSFADDPN NKNGVFGRPV YNYIQGQRGG PTRTYLQSAL KRSNFHLQTK
VRVKYVKRNN GAATGVVVDD GRGATKTVAL KPKGRVVLSA GAILSPQILM YSGIGPKDTL
EKLASKSFTP YNASSWIEKP AVGRGLFDNP NTFIELSGPS VESYTYAYEN PKPADGQMYL
KSRSGPYAFA SQTSAFWTYI PHADGSRAGV QGTVSSAGYA DFTKNKTITL NVYGTSGLRS
AGRVVLSDDG KFIAGPSQGV YYAHPQDAED IATFIHTLFQ RLPPSTPTAP AATGLTPLNL
ARDSSREDII KYITTPSKYA VGSVQHWSSS CRIGECVDVD TKVIGTDNIH VIDASILAPL
TVNPQFAVMV AAEKGAERIL QSRGKTPKGK RDADDMELWR YLPTRR
//
