ID A0A409YCP1_9AGAR Unreviewed; 1880 AA.
AC A0A409YCP1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=pyranose dehydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00013177};
DE EC=1.1.99.29 {ECO:0000256|ARBA:ARBA00013177};
GN ORFNames=CVT26_012401 {ECO:0000313|EMBL:PPR00776.1};
OS Gymnopilus dilepis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Gymnopilus.
OX NCBI_TaxID=231916 {ECO:0000313|EMBL:PPR00776.1, ECO:0000313|Proteomes:UP000284706};
RN [1] {ECO:0000313|EMBL:PPR00776.1, ECO:0000313|Proteomes:UP000284706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRW20 {ECO:0000313|EMBL:PPR00776.1,
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 -!- 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, ECO:0000256|RuleBase:RU003968}.
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:PPR00776.1}.
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DR EMBL; NHYE01000986; PPR00776.1; -; Genomic_DNA.
DR STRING; 231916.A0A409YCP1; -.
DR InParanoid; A0A409YCP1; -.
DR OrthoDB; 1704824at2759; -.
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; 4.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 3.
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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 3.
DR Pfam; PF00732; GMC_oxred_N; 3.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 3.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
DR PROSITE; PS00623; GMC_OXRED_1; 2.
DR PROSITE; PS00624; GMC_OXRED_2; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000284706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 93..116
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 285..299
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT DOMAIN 762..785
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 1561..1575
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 1880 AA; 206791 MW; 2F7E9B70BE0445B3 CRC64;
MPFIVVEDVV RKDFDYVVIG GGTAGLTAAV RLSEDPSVTV LVLEAGGSEA FDDPNIDLPL
QFAHVIGNPK YDWTFVTSKQ KHANDNQLRW TRGKILGGSS AINFLIWNKP PASDIDAFEK
LGNPGWNWKD YLEYSKKCET VHPPAKEQTD LYPHTFKDDN GGKSGPIQVS LGPHFHTIDK
LFQETMARKG FHTVDDPYGG NVTGIWMAGT NLDPKSWTRS SAASAYLRPN LSRTNLHIVT
NALASRILFD HLDSEDGVAA YAVEFIHADQ YHTVKVGKEV ILSAGTINSP KILELSGIGQ
PEILSRTGVD LVVDLPGVGE NVQDHILVTM PHELASSHET LDLLLDPAYA AKAKELHRAN
ILNRDILHSA LGKGIQRNSI TSLPFFPLSA TPDGEEVFAL IDRLEADVEE KAKNGVLAPG
MEEQLRLQIS ALRDEAIPDC EILVYPGMFS RKASAEPGKS YVTPALCLNH PISRGSIHVQ
SKDPTIPPII DPHCLENKFD LENLVQQVKF IRSLLDVEPW KSGVLREVFP GPDCSSENEI
RGKSFWLRLM NVEPDSFSWF WVEFIKDNVG SVWRTLTCPK IFCLCNAMAS DAAGSCSMLP
QNKRGVVDAR LKVYGTKNVR VADLSIIPLH IAAHTQGWIV YLIMLTALTA YVIGEKGRFM
MSLLPTSSRP IIDETEEVVK KEYDYIVVGG GTAGIPAAVR LSEDPSVSVL ILEAGPVENL
GDFKIDIPAQ YGHTFGNPQY DWAFMTTKQK DLNDNQVLWS RGKGLGGSSA MNFYVWSKPP
AEDIDNFEKL GNPGWNWADY KKFSNKSETQ VFSTSHFQSG ILICKVSVHL PLQEQMDLYP
HTFTNKSGGT SGPIQVIIPP HVHTVDKLFQ ETMVNRGLKA LDDPYGGNIT GTFIAANNLD
PKTWTRSYAA PAYLLPNIDR PNLHVVTSAA VSRVVFEDPE GNEDRRIIAV EFIHDGTTYE
VNVRKEVVLS AGGIQSPQIL ELSGIGQPEN LSKIGVDVVV DLPGVGENVQ DHILVPIPFE
LPPGHESLEL LLDPDYAAKA KELHAVGKGL HRLGATSVAF FPLSATKHDG IAELIDNLEA
EVNAKAKAGS LPPGLEEQLR LQIAALRDNK IPDCEVVVFP GYYFPRAPPE KGKCYTTPIV
CLNHPISRGS IHATSKDPSV PPVCDPHYFE SNADLEILVH MVKFIRSIVE VEPWKSSGAK
EAHPGPECTS DDDIKQYIKE NLGTVFHTAG ACSMLPRDKR GVVDSKLKVY GTSNLRVADI
SIIPLHIAAH TQATAYVIGE KANEISRKSF DYVVIGGGTA GIPAAVRLAE NPKASVLVLE
AGRIENLGDF QIDVPAQFGR TIGNPLYDWF FMTQKQKFSN DNQVVWSRGK GLGGSSAMCF
YVWSKPPAAD INNFEKLGNP GWNWEDYKKY STKSETVHLP AKEQMDLYPH NFTNESCGKS
GPIQVIIPPH VHTVDKLFQE TMINMGLKSN KDPYGGNTVG AWIAASSLDP KTWTRSYAAP
AYLLPNIRRP NLNVVTSALV SRIIFDESRG DEDRRATAVE FLCDGQTYRV GVNKEVILTA
GAIKSPQILE LSGIGQPELL SRLGIDVVID LPGVGENVQD HALISIPFEL PPGHESLELL
LDPAFAAKAK ELHARGQGLH RIGITSTAWF PLSATGLGRE KIAKLIDELE AEVNKKAQNG
VLPPGLEEQL RLQIATLRDE KVPDCEIILF PGYYYSRAPV EKGKNYTTPI VCLNHPTSRG
TIHAASKDPA QPPVCDPHYF ENKIDLEIML ETVKFVRRMK EVEPWKSGTV KEAFPGSKCS
SDDDLREMIK NQLETVFHTA GSCSMLPREK RGVVDPKLKV YGTKNLRVAD LSIIPLHFAA
HTQVADIIKS ENIANATVKN
//
