ID A0A0G2DZB5_9PEZI Unreviewed; 625 AA.
AC A0A0G2DZB5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE SubName: Full=Putative choline dehydrogenase {ECO:0000313|EMBL:KKY15466.1};
GN ORFNames=UCDDS831_g07585 {ECO:0000313|EMBL:KKY15466.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY15466.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY15466.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY15466.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY15466.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY15466.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:KKY15466.1}.
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DR EMBL; LAQI01000194; KKY15466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2DZB5; -.
DR Proteomes; UP000034182; 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; 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: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; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..625
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002543152"
FT DOMAIN 299..313
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 558
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 601
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 44..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 262
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 625 AA; 66437 MW; 76C7CB721DDFD9A3 CRC64;
MVRLLVFSLF CMVVQGRLAR HAQVIGRDVD LADEYDFVIV GGGTSGLTVA NRLTENANVT
VLVVEFGPLD SGDDSVTVPG LAGNAYTPYS FNLTSTPLRG LANQSFPVLA GAVVGGGSVV
NGMFFDRGGA PDYDAWEALG NPGWGWDCLL PYFKKSETFT PNNDSFNEEW NLSYDLDVHG
SDGPVQSSYP EFMWENIKNF FEAWTGLGVP IPDDPGAGSK AGVFWAPSSI DPRNRTRSSA
RTAHHNKIAT RPNYHLLTMH AVTKIAFNGT IATGVEYVSR AGTETGAVKA RKEVILAAGA
IHTPQILQLS GIGPADLLNS LDIDVLVDLP VGYNLQDHPT LYTMWNYAND VIPNGDYFSS
NTTYNAEALA QYHATRSGPY TLGRGATVCF LPLTNVTSSL TNTTSTYSSI TSLAASTSPE
TVYPGIPSLP APVIAGFAAQ KRQLLTEYAS LSTSTTEISY GGGSLMAVVM VKPLSRGTVF
AASRDIFTAP VIDYGTMLAP SDIAVMIASV RKARAFMATA AMQGPLGPIV EVAPGANVTA
DADLEGVLRE TLNPSFAHVS CTAPMMAREE GGVVDAALRV YGVRRLRVVD ASVWPLVPAT
HTSSTVYAVA EKAADLIKAA HGGWR
//
