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Database: UniProt
Entry: A0A1J9SKC7_9PEZI
LinkDB: A0A1J9SKC7_9PEZI
Original site: A0A1J9SKC7_9PEZI 
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
//
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