ID A0A166ECN2_9AGAM Unreviewed; 598 AA.
AC A0A166ECN2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:KZV68613.1};
GN ORFNames=PENSPDRAFT_508840 {ECO:0000313|EMBL:KZV68613.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV68613.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV68613.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV68613.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR EMBL; KV424554; KZV68613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166ECN2; -.
DR STRING; 1314672.A0A166ECN2; -.
DR InParanoid; A0A166ECN2; -.
DR OrthoDB; 3215324at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0140907; F:flavin-dependent halogenase activity; IEA:UniProt.
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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..598
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007872667"
FT DOMAIN 110..133
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 304..318
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 532
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 576
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 262
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 531..532
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 598 AA; 64607 MW; AD636674A6B97905 CRC64;
MLTAIFVLLT LLTDSSYARY LSGPTELAED GYDFIIVGAG TAGGVLANRL SGDAKNTVLV
LEAGESDEGI VALQIPFTAH STIANESLIW DYTTVNQTGL DNRPLAYQRG RVLGGSSSVN
FMFYTRGSRD DYDRFANFTS DEGWSWDALF PYMLKAERFV QPVDGYDSTG RIIASDHGYN
GSLLTTTNGF EMPFDNLTLE TSGMYVDTSN FSFNQDFNSG DTIGTSWIQT TSGGGVRSSA
ATAYLHPVSD RDHLHILLGA KVTKLSDVGG TQRPDLREIT FMMANDNGID YTARANKEII
LAAGAVNTPQ LLLLSGIGRS SELAPLNIST VVESPAVGKE MQDHPLLSVQ WETSSDKTLD
ALLRNTTATD AILTEWETNK TGLYTDVSAN LFSWVRLPDN SSAIQTFGDP SAGPTSSHIE
LIPVPFFSSF TEATPGNGSY LSMILNVASP ASRGSVRLAS PNPLEFPLID PGYFTDDYDV
NAMVAALHLA EDFFGTSAWA GMDLKRYGPW TNATTDAELA DMTRARVTTF WHPCCTARMG
KPDDDTAVVD SKLLLKGADG LRIVDASVFP FIPSAHLQAP VYAIAERAAD IILEAYSG
//