ID A0A163LV42_DIDRA Unreviewed; 615 AA.
AC A0A163LV42;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KZM28149.1};
GN ORFNames=EKO05_0005836 {ECO:0000313|EMBL:UPX15389.1}, EKO05_004655
GN {ECO:0000313|EMBL:KAF9708578.1}, ST47_g698
GN {ECO:0000313|EMBL:KZM28149.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM28149.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM28149.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM28149.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9708578.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708578.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9708578.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708578.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9708578.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708578.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX15389.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX15389.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) 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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; RYYQ01000008; KAF9708578.1; -; Genomic_DNA.
DR EMBL; JYNV01000032; KZM28149.1; -; Genomic_DNA.
DR EMBL; CP095296; UPX15389.1; -; Genomic_DNA.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 9.
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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..615
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041046693"
FT DOMAIN 112..135
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 298..312
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 550
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 593
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 615 AA; 66286 MW; 441C1CA59D60B373 CRC64;
MAPSLRSLVS FAAVLPFVVA VPAVKRDDVS SIKNKAYDYV IVGGGLTGLV VANRLSENKF
RSVLVLETGP ITEDINTVIP ASGNNINSAM QYDVESAPDA ALDGLSAPVL IGRVVGGGSV
VNGMAFDRAS AADYDAWEQL GNPGWGWNGL LPYFKKSTTF TPPILAKEFN ITHDASVYGK
NGPIQASFPN FEFPDVKVMW EAWRAGGYPT PKEHAAGDAV GALWVPTSLD PKTQTRSDAR
RTYYDSVKSR PNLKLVTGVE ATEVLFDKLT AKGVLFTNLA DKTTSRVYAK REVILAAGSV
FTPKILQLSG VGPANVLKAA GVKVKKDLAA VGANLQDHPN ADMFFSTQNL STPNPNFATD
PVQNATAWEQ YYANRTGPVT QSHGSSLAFL SLQSVASDYK QIVSTIRGQK SVDYLPAVYK
NNPNLLRGYE VAKAITLELL SGTKAAAFEF PMNAFGLAIS AVERPLSRGY VALNPTNPTG
NPIIQFNTFQ NPADRTMIVE AIRWLRRHWK SPVLARFSPV ELTPGAAAQT DDEIIHALLE
NDALHPTWAH QSGTCSMLPE KYGGCVGSDL RVYGTKSLSI IDASIIPLIP ATHLQATMYA
VAEKAADLIK LRNIF
//
