ID A0A366S5W2_9HYPO Unreviewed; 801 AA.
AC A0A366S5W2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN ORFNames=FIESC28_02500 {ECO:0000313|EMBL:RBR24727.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR24727.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR24727.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR24727.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RBR24727.1}.
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DR EMBL; QKXC01000052; RBR24727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366S5W2; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000253153; 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 CDD; cd09630; CDH_like_cytochrome; 1.
DR Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR015920; Cellobiose_DH_cyt.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR47190:SF5; PX DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF49344; CBD9-like; 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.
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..801
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016702999"
FT DOMAIN 315..338
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
SQ SEQUENCE 801 AA; 85082 MW; A5B6E132773FE423 CRC64;
MRFTLSTMAA LLGLSSAQGI RSSAYTDPKT GIDFQRFVDD DYSVGFAVPE TLGKDLIAQM
VFPAEKGAGW GAISFRGGMI GGMLFVAYPN GDDIVTSFRM ASSYANPEEY TNSTVKATPI
PEGTFVNSTH VSYTFLCEGC VEEKVTSLLN ESPVLGYAWS SIAVDAPADP QAVLSYHGAG
FGQFGFDIKG AASAKFADWA AMAKETVSAP PTGGNGTVPV PGNSTIPPTT SNITYDVIVV
GGGPAGIIAA ERLAEKGLST LLIERGPANT VALGNTAQAL PWNNTLTPYD IPALGSSMTS
MAGTKFCSDT ASTAGCLLGG SSSINGLNFI HPPERDFQRW PQGWSWNDVS AAADRLYERN
PGTTLPSDDG KYYDDMTYKV LEKYLSGKGW KEVDSIESPN EKHEVYSRCS WSIKDNMRAG
PARTYMPFAK ALPNFTLKLE TKVIQPIRKG SMITGVLTQA ADGSKQVINV KAGGKVILAA
GAMSTPRLLW NAGIGKSDAL AIVKEGSSRT GVTLPADTID LPVGHHLQDH AQVVLQFKPK
TNFTAYKFND IATKPVASDL DLYMQGSGPI TQAAQRMHLW TSAKGADGRT RYLQGTASAM
ADGVITVRTF LTHGTSTVGE LGIAAAGNTL LKTKPWLIDQ EDRKAMGDFV QYWLDLTSGS
NSTLSYITPG ATVEDILSTK MISGDHWMGS AKMGTDDGRK ANGSAVVDLN TKVYGTDNLF
VVDASFHPDL PTGNTQAIIM IGAEHAAEKI AALKVVGGGS NSTIPDPVSA PTPVPTPSKG
VKCKRAARAA RRSMHFRRSM Y
//