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Database: UniProt
Entry: A0A166ECN2_9AGAM
LinkDB: A0A166ECN2_9AGAM
Original site: A0A166ECN2_9AGAM 
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
//
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