ID A0A014PQF7_9HYPO Unreviewed; 577 AA.
AC A0A014PQF7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:EXU99934.1};
GN ORFNames=X797_007063 {ECO:0000313|EMBL:EXU99934.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXU99934.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXU99934.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXU99934.1,
RC ECO:0000313|Proteomes:UP000030151};
RA Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA Gibson D.M.;
RT "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT ARSEF 2575.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXU99934.1}.
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DR EMBL; JELW01000016; EXU99934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A014PQF7; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_011025_2_1_1; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000030151; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..577
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001474525"
FT DOMAIN 282..296
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 545..546
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 577 AA; 62396 MW; A3F87043DAE43652 CRC64;
MTLLASLWLG ALFLATLGRA SAVANWTLQS WDVIVVGAGT AGIIVADRLS EAGYKTLLLQ
QGGQSYGITG GRERPGWLDN TTLSRVDVPG LYSSIFAGGS SLLCGPGQVD AFQACTVGGN
SAINAGLYFQ PPASDWDDFH PGGWHSADVA NATARLLKRQ PALTSYSQDH KYYLQSGYEA
VKKWIVEAAG YQDVSLLEQV NDKKRVFGRP VYNYIDGQRG GPTRTYLQTA LRRNHFHLQT
GVQVEHINHV RGVASSVEVA LDSGEKKAIQ LTKRGRVVLS AGAMLSPRIL MLSGIGPRDA
LEKLAAKSAT PYNASSWMVR PDVGRGLFDN PNTFIVLSSP DVKSYVYKYD DPAPADRDLY
LESRSGPYSF ASQTSVFWTY IEHNGTRSGV QGTVSSSGYR DFVGNNTITL NIYGTSGLLS
SGHVELADDG NFAAKPSAGV YYGHPRDADT VAEFIHSLFQ HLPPSTPTSP AKEGLTPLNL
ARNSTLQEIW RYITDPNSPY AVGSVQHWSS SCRIGKCVDV DTKVIGTQNI HVVDASILAP
LTVNPQFGVM VAAEKGSERI IASMKNVTEG CRGRRRV
//