ID A0A409VZJ2_9AGAR Unreviewed; 608 AA.
AC A0A409VZJ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=pyranose dehydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00013177};
DE EC=1.1.99.29 {ECO:0000256|ARBA:ARBA00013177};
GN ORFNames=CVT26_007649 {ECO:0000313|EMBL:PPQ71682.1};
OS Gymnopilus dilepis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Gymnopilus.
OX NCBI_TaxID=231916 {ECO:0000313|EMBL:PPQ71682.1, ECO:0000313|Proteomes:UP000284706};
RN [1] {ECO:0000313|EMBL:PPQ71682.1, ECO:0000313|Proteomes:UP000284706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRW20 {ECO:0000313|EMBL:PPQ71682.1,
RC ECO:0000313|Proteomes:UP000284706};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- FUNCTION: Catalyzes the single-oxidation or sequential double oxidation
CC reaction of carbohydrates primarily at carbon-2 and/or carbon-3 with
CC the concomitant reduction of the flavin. The enzyme exhibits a broad
CC sugar substrate specificity, oxidizing different aldopyranoses to the
CC corresponding C-1, C-2, C-3 or C-1,2, C-2,3 and C-3,4 (di)dehydro
CC sugars with substrate-specific regioselectivity. Accepts only a narrow
CC range of electron acceptors such as substituted benzoquinones and
CC complexed metal ions and reacts extremely slowly with O(2) as acceptor.
CC May play a role in the natural recycling of plant matter by oxidizing
CC all major monosaccharides in lignocellulose and by reducing quinone
CC compounds or reactive radical species generated during lignin
CC depolymerization. {ECO:0000256|ARBA:ARBA00024699}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3,4-diulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00034059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3-ulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00034050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00034010};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00033986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-3-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00034029};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:PPQ71682.1}.
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DR EMBL; NHYE01005492; PPQ71682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409VZJ2; -.
DR STRING; 231916.A0A409VZJ2; -.
DR InParanoid; A0A409VZJ2; -.
DR OrthoDB; 3215324at2759; -.
DR Proteomes; UP000284706; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000284706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..608
FT /note="pyranose dehydrogenase (acceptor)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019221383"
FT DOMAIN 36..354
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 459..598
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 542
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 586
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 608 AA; 64864 MW; 06DD932A4AE2D441 CRC64;
MQLSALTVFL AIASLVPSSL AVTVSSAAQV KGSLTYDYII VGGGNAGLVV ASRLTEDPSV
SVLVLEAGVS DEGVLTAQVP FFGPMVTPNT PYDWNYTVVP QKGMNGRTFA YPRGHILGGS
SSANYLIHQY GTDEDWNRLA SVSGDNGWSW SNMKQYVQKH EKFVPPIDGH NTTGQFIPSL
HGFHGEVSVT LPGFNQTIDP RVLEVTKQLP QFPFNEDTSA GDHDILGIGF VQSSGGGGVR
SSSSTTYLAN ANKRSGLTVV VNAYVTKLVS TGNGRSPGTK AFRAVQFTSS PGTVPGATTL
TATARKEVIV SAGSVGTAQL LQLSGIGNSA DLKKVGINTI IQNSDVGENL SDHTLLPNLF
TVRGNQSFDS VLRSTDLVTD ALNQWMQNKT GMFANNVLNN YGFARLPSNS DIFKTTRDPA
PGPKSPHWEM IFSNLYFNPG VPRPDTGSFM TMIVVLLTPT SRGTIKLKSN NPFDKPLIDP
QYLTTQFDVV AIREGVKAVK NILAAPAFAD YVEGPFGSAF ASAKTDAQIE SYVRGLTSTI
FHPVGTASMS SQFSKSGVVN PDLTVKGTEG LRVVDASVFP FIPSTHTQGP VYLLAERASD
IIKQADHI
//
