ID V5EYA9_KALBG Unreviewed; 610 AA.
AC V5EYA9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EST07674.1};
GN ORFNames=PSEUBRA_SCAF2g02776 {ECO:0000313|EMBL:EST07674.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST07674.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KI545862; EST07674.1; -; Genomic_DNA.
DR RefSeq; XP_016292663.1; XM_016437173.1.
DR AlphaFoldDB; V5EYA9; -.
DR STRING; 1365824.V5EYA9; -.
DR GeneID; 27419845; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_0_1; -.
DR OMA; HIYCTSS; -.
DR OrthoDB; 1704824at2759; -.
DR Proteomes; UP000019377; 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 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377}.
FT DOMAIN 96..119
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 289..303
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 543
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 586
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 106..109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 610 AA; 66733 MW; 310A404124A797A9 CRC64;
MATPFTDTGV KADDFKEFDY VVVGGGTAGL AVAARLSEDS SVTVGVIEAG LWRPEDPKIN
YPAFIGQSLM NPDYDWCLET EPQQYSNGRK YTWPRGKVLG GSSALNFLVW QRGYKGEYDD
IRKLGNEGWS WDDYATFSRK TATLDYPSTE LQKANLATCD EELHGKDGPI QTSYSKWYTE
AQKPWFDALK SLGVSNVSDG LGGSNTGFWV SPVTVDTKTS VRSYSANAYF APNADRSNLK
VITGAQASKI IFADEKSGSG DLVASGVEFT VDGQTYTVKA RKEVVVSGGT VNSPHLLELS
GIGKADILKA AGVEQRLELD VGENVQDHIY CTSSFKLKPG YITWDKMRQD DFAKAAMEQY
HAEGEDRGII ASAFSGFAYV PLKQYLSADE IAKIKDDVAA VDWSKHSKGV QETVKMQLAR
IEDEQCPFTE FIFAPGFFAT ASPPADGQEY YSILSCLQQP FSRGTIHIAS ADAKQPPKIN
ADYFSVDADL EILSKAVKYS ETISTTSPLK DITVARQDPD PEKYSSDADF REFTKDQSVT
EYHPIGSCSM MPKEKGGVVD ARLKVYGTAN VRVADASVIP IHVSSHIVAT VYAIGEKAAH
MIKEDAAKKN
//
