ID W2LQZ8_PHYPR Unreviewed; 551 AA.
AC W2LQZ8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=L917_03356 {ECO:0000313|EMBL:ETL99867.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL99867.1};
RN [1] {ECO:0000313|EMBL:ETL99867.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL99867.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KI678222; ETL99867.1; -; Genomic_DNA.
DR AlphaFoldDB; W2LQZ8; -.
DR EnsemblProtists; ETL99867; ETL99867; L917_03356.
DR VEuPathDB; FungiDB:PPTG_08452; -.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..345
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 551 AA; 60157 MW; FBB344D4615A9457 CRC64;
MAASYSDERS PLLRPGVQRI GRRTRLLVSG LALLLLFAGG AACVAIVLRL LRPGALSTIT
PLVLSEEYDA IVIGGGPAGS VVAKLLSDDP WRRVLLVEAG NASQTQLGGK DAIPSPLNSK
KLTPFDVPFY WTNVANTPSL HWAYPDVNVA KALGGCGIHN AMLYVRALPS DLRRWQMENW
TWEKALDIYL SIEDFDGPNS SYHSKQGFIR TSPPALALDM SREFIEACVE LGIPRTADFN
APDGRYGAGY YHFNTRDGVR ESAAKAFLGP ILDSKTAESK RENFRLMLDT TVTRISINDD
NVTEGVEVRF GNGTGQLIRL AEHGEVIVTA GAINTPKILM LSGLGNQDAL KKAGLPLKKH
LPRVGMNLQD HPVIGMVFEY KSPRVVDLKA DLDSYFTATN AKHTNVSSFG LFGSAGLSTG
AFLIPPGATL PEIQLTLFPR KSEPHMSNSA GLDHMTEVVV TIALLHPLAR SRVVLIHDEN
DYVDDNDIDD HLIPRVVSEI PDAKPEHLRH GDVWKISWAI GVVREIAAKL GECAPAASFT
HGWLIYCWFD S
//
