ID A0A194S9Q1_RHOGW Unreviewed; 728 AA.
AC A0A194S9Q1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=RHOBADRAFT_49619 {ECO:0000313|EMBL:KPV76126.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV76126.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV76126.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV76126.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KQ474077; KPV76126.1; -; Genomic_DNA.
DR RefSeq; XP_018272175.1; XM_018415262.1.
DR AlphaFoldDB; A0A194S9Q1; -.
DR STRING; 578459.A0A194S9Q1; -.
DR GeneID; 28975710; -.
DR OrthoDB; 1704824at2759; -.
DR Proteomes; UP000053890; 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 GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 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.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890}.
FT DOMAIN 373..387
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 79496 MW; E99D770D85A757D9 CRC64;
MGRFARLTHG RKQGPSTAAI QTATRSPVVL RSQVASAVPS SLAAPCRAAQ PTPTRTPYHE
PHLPASRLVP LDVHGVLSLR DRVERECLEG ELAARKFSYI VVGGGTAGLV LARRLSEDPE
NKVLVLEAGP WKDKCAEIDV PNMSGKLWHT AVDWAYHSAQ QEGLHERRVL WPRGKLLGGS
SNFNACMLTR APALDYDAWA RLGNPGWDWQ SLLEYHRRSE SFHLPTPALN LSPATAHDPT
WTPSAHGHDG PVQASYSPYV SEQMQGLFEA LREDGLKEID PNGGAAAGVG YAPASIDPKT
QTRSSAEAAY YTPIKDRDNL LVITCAQATR LVFSSKSAVG GPLMAKAVEF VDPHDPTHKL
VARVADEVIL CGGTFESPQL LELSGIGNAH HLQQVGVKPF VNLPGVGENL QDHPMVAMSF
RLGRQHDSLD LLEPDHHYAN EVIEEYHHQQ GPLTQGAPIV AYLRPSSFLT RTELAHGNDL
NRVTTDHYGE LFEISARQLQ VEQGLYEARG KLEIVAMNRF LGGTKYEPGR SYIGVIAALQ
HALSRGSVHI TSSDPLKKPR IDPRFLSHPS DAFHLALGAR HVHELMTDPH GRMAAFVDLD
HHAPPLSGIN MAGDVHEGGD EGWEDWVRGN AGTEHHPSST CSMLPRSEGG VVDSSLRVYG
TLNVRVADMS VVPLLPGTHT QSIAYMIGEK ASEMILEDQV RRRVDSSLRD RGRMGETRSY
GGEAEDAV
//
