ID A0A1W5CT22_9LECA Unreviewed; 847 AA.
AC A0A1W5CT22;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Glucose-methanol-choline oxidoreductase, N-terminal {ECO:0000313|EMBL:SLM34007.1};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM34007.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWEW01000197; SLM34007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5CT22; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000192927; 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; 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:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 2.
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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..847
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010696382"
FT DOMAIN 113..136
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT REGION 276..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 847 AA; 88918 MW; C191312799A4806B CRC64;
MGAVSAIFAT FALLATSAQC VHLFGRDLNA PLLQSYDYVV VGCGISGLVV ANRLSEDSSV
QVLCIEAGEP DQGEDVIDIP VYVGADIGGV YDWDLTTVPQ TQLDGAIRPM PQGKVLGGGS
ILNAMCWNRG GQDDFDAWEA LGNPGWSWDG LLPYFMKSET YTPVYSEEIA DEYSIHYNPA
VHGTSGPVNV SYPNFFYPQS ANLFAALNYL GVPTAFDPND GTTAGAAFVP TDLNPDSQTR
ADARVSYYDP YATRENFHVI TGQHVTQVLI DGTTNNEEAS DQTNGGNVNG DGSASGGGLG
FDPGSSTTPP TGEKRSRDAN TANLRITGVE FAADAAAPRQ TVYATREVIV AAGALHSAQL
LQLSGIGPAA LLETYNITVA IDLPGVGNNL QDHCLVGTFY PYNNASFPLP TELTTNATYN
LEAEAEYDAT RTGPWTAGSP NGLAFPPLSL ISNNSWVILD NASMQNPTDY LVPGLDSTVI
AGYTAQSASL VQRLAETTVA AYEIINNNAG SLTVSVMHPF SRGTCYINSP DPFDPPLIDP
RWLTNPVDRQ VLIEALQFNR LILAAPSMLE LQAAQFVPPF DADEAALNQV IDNGIRTEFH
PSGTCAMLPL EQGGVVDSRL VVWGTQNLRV VDAGIFPLIP AAHLQAVVYG VAEKAADIIK
ADNVNVQPSI VRNASASLTA TASSIRPPYA NSTIAAFGAS LTSSVVSIHT TLVGEISTSS
ATAQNRISAS ASLTATSETS PSTVIIQTET STASDVDLVS ATLSPSVLNA SQLSSSIIAA
LTSGGVLPQV ASALESFVVG TVSAPSSLPA ATATSGASSS SDTELLQKEE EAINALVKWL
LQYFHVA
//
