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Database: UniProt
Entry: A0A010Q4H8_9PEZI
LinkDB: A0A010Q4H8_9PEZI
Original site: A0A010Q4H8_9PEZI 
ID   A0A010Q4H8_9PEZI        Unreviewed;       340 AA.
AC   A0A010Q4H8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EXF74762.1};
GN   ORFNames=CFIO01_05432 {ECO:0000313|EMBL:EXF74762.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF74762.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF74762.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF74762.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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:EXF74762.1}.
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DR   EMBL; JARH01000945; EXF74762.1; -; Genomic_DNA.
DR   RefSeq; XP_007601598.1; XM_007601536.1.
DR   AlphaFoldDB; A0A010Q4H8; -.
DR   STRING; 1445577.A0A010Q4H8; -.
DR   KEGG; cfj:CFIO01_05432; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_0_1; -.
DR   OrthoDB; 71674at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          24..90
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          163..295
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   340 AA;  36029 MW;  B74A66B6AF0CEFB9 CRC64;
     MKRVEITAPG VVSWVDHPKP EAGPKDVLLK IKACGICGSD SLYTDHGGIP PYQGCTPLGH
     EPAGEVAEIG TDIESPDVEV GDHVVVDTMV FQDGLLGSGG AQGALCEYVV IYNYKPRKHL
     KKIPKSIPWH IAALNEPMAV ALHAVNRTSP KPGCKVVVFG AGPIGLGAVL GYRRKGASHI
     VVVDVVNTRL EKALKVGADA VVNSAEAEDL AAKLVELQGD GATAQNRGTR PSTDIFLDAA
     GAPPVPAQVC KMAKRGATFG VVGVHRKPTE LNFAQLISTE LTIVFSVGYP TEIFEVTDDI
     VDNWDKYAEI VSDQIPFDQA LEALELAKSG KANKVVVVFD
//
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