ID A0A094JNU3_9PEZI Unreviewed; 609 AA.
AC A0A094JNU3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=V502_07968 {ECO:0000313|EMBL:KFZ10718.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ10718.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ10718.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFZ10718.1}.
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DR EMBL; JPKE01002812; KFZ10718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094JNU3; -.
DR STRING; 1420915.A0A094JNU3; -.
DR HOGENOM; CLU_002865_5_1_1; -.
DR OrthoDB; 2392848at2759; -.
DR Proteomes; UP000029308; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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; PS00624; GMC_OXRED_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000029308}.
FT DOMAIN 284..298
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 540..541
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 609 AA; 66351 MW; 5D5EC37646A41F34 CRC64;
MGLHTKLAEG IDEVDVIIAG GGTASCIIAA RLAEADPNLS ILVIEGGANN YNVASVVYPA
LFLQNLAPNN TTAIFYKGNK AKQLADREPI VPSGGILGGG SSINFMMYAR AQRSDLDSWK
TPGWSADELL PFMKKLETYH GPGEKEHHGF NGPIHVSNST YRASRPETDF IDAAQKVGYP
EIKDLQNLDA NNGVERWLRY VSPDGKRQDT AHTYLHPKLR DSNAYPNLHV LVEAKVLRVV
IDDSGRAVGV EYTPNPDCQA AGISLTKHPK RTVKARKLVV VSCGACGTPA VLERSGVGNA
KVLERAGVPV VVDLPGVGND YQDHHLVLYP YRTNLEADET IDGILSGRAD AAELIAKNDK
IMGWNSVDIS SKVRPTDDEV SALGPEFQVA WDRDFKNAPN KPLMLMGLVS CFLGDPSSIP
AGQYVTIGNY TAYPYSRGHM HITGSDHSDP LDFDVGFFTD PHDIDLKKQI WAYKKQREIM
RRTKMYRGEL ALGHPQFPAG SNAACVETNG PLNEVSDLKY SAEDDKAIEQ WLRENVNTTW
HSLGTAKMAP LEEMGVVKPN LDVHGVKGLK IADMSIAPEN VGANTNNTAL VIGEKAADII
MQELGLNQH
//