ID A0A166VGL7_9PEZI Unreviewed; 360 AA.
AC A0A166VGL7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Alcohol dehydrogenase (Nadp+) {ECO:0000313|EMBL:KZL74543.1};
GN ORFNames=CI238_11395 {ECO:0000313|EMBL:KZL74543.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL74543.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL74543.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL74543.1,
RC ECO:0000313|Proteomes:UP000076584};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KZL74543.1}.
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DR EMBL; LFIW01002325; KZL74543.1; -; Genomic_DNA.
DR STRING; 1573173.A0A166VGL7; -.
DR OrthoDB; 5353053at2759; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF14; NADP-DEPENDENT ALCOHOL DEHYDROGENASE C; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
SQ SEQUENCE 360 AA; 39133 MW; 020A4B39F19C7A3E CRC64;
MSYPEKFQGF CVSGPKSWNQ FKKETLTPKP FGDRDIDVQI ECCGVCGSDV HTITGGWGEY
EGPLCVGHEV VGKAVAVGKS VKDIKVGDRV GVGAQVWACL KCDQCKNENE NYCPHLVDTY
NATYEDGSQA HGGFASHIRA HEYFTFKIPD AIKSEDAAPL MCAGLTTYSP LVRGGVGPGK
TVAIVGIGGL GHLGVQWAKA LGAEVYALTH SPDKAEDCKK LGAKEVINTN EKDWAKPYAF
KFDFMLNCSD MTNEFDLQTY LSTLKVGGHF HMVGLPDKPL PQFPVALFAT NSAKMSGSHI
GNNQEMNALL KLAAEKGITP WVETIDMSEE GCKEAVERVK ENKVHYRFTL VGHQKAFGTA
//
