ID W9YNK7_9EURO Unreviewed; 1277 AA.
AC W9YNK7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O1_04375 {ECO:0000313|EMBL:EXJ91265.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ91265.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ91265.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ91265.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ91265.1}.
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DR EMBL; AMWN01000003; EXJ91265.1; -; Genomic_DNA.
DR RefSeq; XP_007723459.1; XM_007725269.1.
DR AlphaFoldDB; W9YNK7; -.
DR STRING; 1182541.W9YNK7; -.
DR GeneID; 19159258; -.
DR eggNOG; ENOG502QSPJ; Eukaryota.
DR HOGENOM; CLU_002483_0_0_1; -.
DR OrthoDB; 1945480at2759; -.
DR Proteomes; UP000019484; 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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019484}.
FT DOMAIN 101..133
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 182..403
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 583..647
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1277 AA; 138959 MW; BFEFC3390045350B CRC64;
MEQDLQKVAG KRGEKKSLID PDSQTANGST GTNGYGSSSS NSTEPPQSPF HHVPPYRVGT
TEPGGPLSRA QSKLEASDYH GVNNKFPRLS RPVELLRHTY DVVVIGSGYG GGVAASRMAR
AGQSVCVLER GKERWPGEYP STLAEAAPEI SVSGLFAPGD NPGTPVQIGD PTKLYQLVMG
AGQNAFVASG LGGTSLLNAN VFLRADDGTM SLPEWPKDLQ KPGALDEYYN RASQMLQPEE
YPEDFPPLPK LELLRKQAEL LGLEKNFKRV PQTTRFENGP NYAGVQMQAS ALTGMDSTGV
NDGSKSSTLV TYMSDAWNWG AEIFCECEAR YVKKHPTQEG YLVYFACHTS KRGLFKKNIY
HDLMWVHAKK FVFLGAGALG TTEILLRSKA LGMKMSSRVG KDMSGNGDIL AFGYNTNYDA
NGLGSPSPSP DRPVGPTITG VIDCRAQPNP LDGFVIEEGA ITGALVPVLQ GLLESLPGKT
FPRHYTLKDK LQHHLARRLS RLYPYAPMGS LEKTQTYLIM SHDSNQAVMS MGTNDKPTLS
FLGVGRSDHV KYLNGKLAQA TNAVGGTYIN SPFFAALGEQ EITVHIMGGA TISSDDTGVN
GAVNQFGQVL QGKGKEVHDG LIVVDGAALP TALGVNPFAT ITALAERSVE AAAKRKDLRI
DLITQNGTLD LFGRPAHPKP MDKELRKADR IIQMAMASDS EGIEFTEVMS GYINIEDQVN
TGNETADFAV ATDAAQAAGS TARFFLSCHA WDTDELIGRS DHPAMLTGTF TCAGLPGSPF
MVLRGAFNLF NEDKRTPDTT NLTYDFDMIS TRGEIVHFHG YKIVDRSIAF KPWSTWKATS
TLYVTLTKGD RTVGKGTLHI LPQDFASELS TFTPHGSTTL SKMFSTVKFL TFFARQVLSN
FLGPLGFMQF PTTTYQGYEV NKKPPVETIK VTSTDKIVST LQRWAPTTTS SQGRKVLFIP
GASVDHQIFA LPTIKTNAVE YFQAAGYEVF CITHRTGKTP NAQRGFTTYD ARLDIQAAFE
EIHRLQGSAS PIYVIAHCAG SVALSAGLLD GTINSKWISG MTASQVFFNP MFGTVNKVKA
SLPIPLTKIY KLLAGSWFSC ISTEHDSLVQ RLLNQVVRLY PAGSPSELCN SVVCHRSELV
FGRLWSHKRL NAATHSNLSK FLGGTSMNAL SQLMYQGTHG EVTNNILESL VRPENLQRLR
GLPILFISGT DNVVYTPENT DKSYTTLTTI FGQGIYQREL FPGYGHLDCW MGAEAVKDVY
PTVLAHAESI FNGAARD
//
