ID A0A1J9SKC7_9PEZI Unreviewed; 660 AA.
AC A0A1J9SKC7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:OJD40196.1};
GN ORFNames=BKCO1_1000435 {ECO:0000313|EMBL:OJD40196.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD40196.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD40196.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD40196.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) 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:OJD40196.1}.
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DR EMBL; MNUE01000001; OJD40196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9SKC7; -.
DR STRING; 236234.A0A1J9SKC7; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000183809; 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:SF100; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G00630)-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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..660
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009657278"
FT DOMAIN 126..392
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 498..635
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 660 AA; 71037 MW; 3E19AEFD2B35D44A CRC64;
MLFPRILGVL ASTLPLAWAV DLTGYEYVVV GSGAGGGPLA ARLAIAGHKT LLIEAGDDQG
ANENYTIPAY SAKSSEDELL AWNFFVRHYA DDDRQARDFK TTWATPDGGE YTGVDPPEGS
TIKGTLYPRT GTLGGCTAHN ALIAVYPHQS DFEYISTLTG DASWGPDSMR QYFTRMEKNQ
YLLPGQPGHG YDGWLATENA PLSIVLEDPQ LLSLLTGGAF ALGNLTDNLF NIGTLLAGDA
NADTESRDKD PAYYQIPLST NDAHRTGSRE FVVAVRDATN PDGSKRYPLD VRLNAFVTKV
TFDQDVSPPR ATGVEFLDGA HLYSASPRSS AANKGTPGTA SASREVIVAG GVYNSPQLLK
LSGVGPADEL SKFGIDVISD LPGVGTNLQD HYEISVQGTI ENNFTAFDGC TFRLDDPNDP
CVDRWNNPVL GDRGIYSSSG LAATMFYKST ATADDSFDIF AFGGPVNFRG YFPDYSYNAT
INHNWFTWAI LKAHPRNTAG TVTLRSADPL DMPDIVFNYF DTGSGDASKD LQALYEAVEL
ARDAFDRQLV PVTETLPGPD VQTQEQIEQY AKDVAWGHHA SSTCPIGADG DEMAVLDSKF
QVRGVQGLRV VDASVYPRIP GTFTAVSTYM VAEKAADDII AAAKANSTTT ASSAKFRLRA
//