ID A0A0A2IZQ0_PENEN Unreviewed; 610 AA.
AC A0A0A2IZQ0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KGO62892.1};
GN ORFNames=PEX2_044150 {ECO:0000313|EMBL:KGO62892.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO62892.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO62892.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO62892.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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, 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:KGO62892.1}.
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DR EMBL; JQFZ01000018; KGO62892.1; -; Genomic_DNA.
DR RefSeq; XP_016603392.1; XM_016741690.1.
DR AlphaFoldDB; A0A0A2IZQ0; -.
DR STRING; 27334.A0A0A2IZQ0; -.
DR GeneID; 27677109; -.
DR HOGENOM; CLU_002865_6_3_1; -.
DR OrthoDB; 858083at2759; -.
DR PhylomeDB; A0A0A2IZQ0; -.
DR Proteomes; UP000030143; 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 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:SF138; DEHYDROGENASE PKFF-RELATED; 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|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..610
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009752516"
FT DOMAIN 116..139
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 306..320
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 543
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 587
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 126..129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 542..543
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 588..589
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 610 AA; 66539 MW; 8B9DDA246ABCA4C6 CRC64;
MLFQTTLVLL ALQASGVASV PLEQRAVPLA EQTFDYVVVG GGTAGSVIAT RLAQNDFKVA
LIEAGGHYEL ESVAEFPASD ALSVGSDPTF RSPEDWGFVT RDQPGTNRRA IHFARGKCLG
GSSALNFMVY QRPTLESMDT WASAVNDSSY GFDKVLPFYK KSVQFTPPNT DYRAQNASAD
YGVDAYDSDS GPLQVSYANF AQPFSSWMSL GMEAIGINQV QDFNLGDIMG SQYCASTIDP
SNELRSSSEQ SFLSKITPSS LTTYTNTLAK KVVFDENNKA TGVQVKGLLG DTVTISASEE
VIISAGAFQS PQLLMVSGIG PIDQLQEHEI NVIADRPGVG QNMWDHPFFA PSYRVRVTTF
TRLATDLLYA AGQIIEGLVS KKGFITNPIA DFLAFEKIPR FLRSAFSEET QSKLDKFPSD
WPEAEYISGA GYMGNASNLL AIQPKDGYQY ASILGVLITP MSRGNITLQS ADTSDLPVIN
PNWLDDQADQ EVVIAMFKRI RQAFQSEAME PVVIGEEYNP GPQVQSDHQI LEFIKNHVMT
LWHPSCTCKM GTSDDDMAVV DSQARVYGVD GLRVVDASAF PFLPPGHPQS TVYMLAEKIA
ADIIRDSQVH
//
