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Database: UniProt
Entry: A0A162VTA2_DIDRA
LinkDB: A0A162VTA2_DIDRA
Original site: A0A162VTA2_DIDRA 
ID   A0A162VTA2_DIDRA        Unreviewed;       627 AA.
AC   A0A162VTA2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KZM18610.1};
GN   ORFNames=EKO05_000680 {ECO:0000313|EMBL:KAF9712950.1}, ST47_g10247
GN   {ECO:0000313|EMBL:KZM18610.1};
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:KZM18610.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM18610.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM18610.1,
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:KAF9712950.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9712950.1};
RA   Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF9712950.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9712950.1};
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:KAF9712950.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9712950.1};
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.
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:KZM18610.1}.
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DR   EMBL; RYYQ01000002; KAF9712950.1; -; Genomic_DNA.
DR   EMBL; JYNV01000324; KZM18610.1; -; Genomic_DNA.
DR   STRING; 5454.A0A162VTA2; -.
DR   OrthoDB; 2392848at2759; -.
DR   Proteomes; UP000076837; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT   DOMAIN          301..315
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         254
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         557..558
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   627 AA;  68809 MW;  2247E019D9263DD6 CRC64;
     MSQHTRTTFP LELLDTIVKM GIQNKLADGI DEVDVIIAGG GTAGCIIAGR LAESNPDLSV
     LVIEGGANNK DVASIQYPVF YLQNLLPTQK TALFYKGNKS KQLADREPIV PSGGTLGGGS
     SINFMMYTRA QRDDFESWKS EGWSADEMLH HMKKLETYHG PGEKKNHGFD GPINVSDGGF
     REKRVEDDFI KAAGEVGYPE IDDLQSLDNN NGVQRWLRYV SPEGKRQDTA SRYIHPKLED
     EAHSNLHVLV ESKVVRVLFD DNKRAVGVEY TPNAEFQAVI GLTAHPVKTI KARKLVVVTC
     GACGTPPVLE RSGVGERSIL ERAGVPVVEE LPGVGKDYQD HHLLLYPYRT SLEPDQTIDG
     ILSGRVDATE LVKNNDKTLG WNAIDIASKL RPTEEEVAGL GPEFKAAWDR DFKNTPNRPL
     VLCGIVSCFL GDPSSVPEGQ YVTAGVYTAY PYSRGHMHIT GSSVEDPLDF DVGFFNDDHD
     IDVKKQIWAY KKQREILRRT DLYRGELAAG HPRFPEGSKA AAVEFEEPLS NVQNLVYSQE
     DDAAIEQWLR ENVNTTWHSL GTCKMAPREE NGVVDSKLNV YGVSGLKIAD LSIPPQNVGA
     NTNNTALAIG EKAADIIIAE LSAAGTP
//
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