ID A0A161VNA9_9PEZI Unreviewed; 529 AA.
AC A0A161VNA9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KZL78544.1};
GN ORFNames=CT0861_03983 {ECO:0000313|EMBL:KZL78544.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL78544.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL78544.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL78544.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL78544.1}.
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DR EMBL; LFIV01000002; KZL78544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161VNA9; -.
DR STRING; 708197.A0A161VNA9; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000076552; 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 Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 231..245
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 450
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 493
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
SQ SEQUENCE 529 AA; 56879 MW; B1942CE1645239E9 CRC64;
MIPRFYPGAS GFAPGTRYDW NFTSVPQESL QGQTVNLTQG HAVGGSSTVN AMIFDRGMPS
NYDAWAALGN TGWDFESLLP YFKKSEGFTP ASPENTALYG MVYDPACHGF EGPVQSSYLA
WSHPNNTNFL EAMHGLGIST PTDQGCNPLG AYLTTHSIDP RNQSRSSART SHYDAILERP
NLEIAIGQQA TKLVFDASGA KPKAVGVEFS TGPDSDRQNV TASKEVILST GALNTPKLLQ
LSGIGPTSVI SKFGIVSIVD LPGVGANLQD HPFGLTLASC RWTDTIAEAL AFIPLFNFTT
ADVGNRLLST INNNAAQFLP PDTDKTVVAG YEKQLEQLLK MHKGSTTAGM ELLYVDGGRS
VVNILMHPIS RGTVNIQSSS PFLPPVINPR YFSHPYDGQV LVESLRFNRK LLAAGPIQAL
DATETLPGAA IQSDEDILTF IKGVTSTEYH YSGTCAMLPK ALGGVVDSDL KVHGVDSLRI
VDASIMPLVP SAHTQATVYA IAEKVSRRLN DCPPRRNGTR SNADLWCNV
//
