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Database: UniProt
Entry: C9SDC8_VERA1
LinkDB: C9SDC8_VERA1
Original site: C9SDC8_VERA1 
ID   C9SDC8_VERA1            Unreviewed;       352 AA.
AC   C9SDC8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EEY17080.1};
GN   ORFNames=VDBG_03189 {ECO:0000313|EMBL:EEY17080.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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DR   EMBL; DS985216; EEY17080.1; -; Genomic_DNA.
DR   RefSeq; XP_003007050.1; XM_003007004.1.
DR   AlphaFoldDB; C9SDC8; -.
DR   GeneID; 9533205; -.
DR   KEGG; val:VDBG_03189; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   HOGENOM; CLU_026673_3_4_1; -.
DR   OMA; YISHFDG; -.
DR   OrthoDB; 2656459at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08276; MDR7; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR45033; -; 1.
DR   PANTHER; PTHR45033:SF1; OXIDOREDUCTASE (EUROFUNG); 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   DOMAIN          15..348
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          173..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  37931 MW;  6FD694565126864B CRC64;
     MAGIQAQKWQ TKLDGLENLS RAAGAMPKPS KGEVLVKISA VSLNYRDTEV IMGLYNHHKT
     VNAGDIDPLV PCSDMCGTVV AVGVDNDNDA PLWAVGDRVL STFNQAHLTG QIKAPIMASG
     LGLPLEGVLQ THRVFPATGL VRAPSHMSDE EAACLPIAAV TAWMAINQFR PLGAPGGPRR
     DGAAAGHRRR QRQRAADCQG PRGRRLEKAK ALGADHVINY RTTPDWQAQV MALTGEEGAD
     VILETGGAQT LRKSFDCVAY GGVIACIGYL SGKQDEAGDR TNVNLLALAR NVTLKGILNG
     PRDRFEEMVR FYEAHAIRPV VDRVFGFEEG REALQYLFSG SHFGKVVVKV DV
//
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