ID   K7W2F2_9NOST            Unreviewed;       348 AA.
AC   K7W2F2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Zinc-containing alcohol dehydrogenase {ECO:0000313|EMBL:AFW95197.1};
DE            EC=1.1.1.1 {ECO:0000313|EMBL:AFW95197.1};
GN   ORFNames=ANA_C12474 {ECO:0000313|EMBL:AFW95197.1};
OS   Anabaena sp. 90.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW95197.1, ECO:0000313|Proteomes:UP000010101};
RN   [1] {ECO:0000313|EMBL:AFW95197.1, ECO:0000313|Proteomes:UP000010101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90 {ECO:0000313|EMBL:AFW95197.1};
RX   PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA   Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA   Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT   "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT   cyanobacterium Anabaena sp. strain 90.";
RL   BMC Genomics 13:613-613(2012).
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}.
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DR   EMBL; CP003284; AFW95197.1; -; Genomic_DNA.
DR   RefSeq; WP_015080353.1; NC_019427.1.
DR   AlphaFoldDB; K7W2F2; -.
DR   STRING; 46234.ANA_C12474; -.
DR   KEGG; anb:ANA_C12474; -.
DR   PATRIC; fig|46234.3.peg.2787; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_3; -.
DR   OrthoDB; 9770526at2; -.
DR   Proteomes; UP000010101; Chromosome chANA01.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd08235; iditol_2_DH_like; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
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   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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AFW95197.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010101};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..346
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   348 AA;  37941 MW;  68BC32BC25338476 CRC64;
     MKAQVFRGVN QLSYEEVPVP TLDADEVLVQ VRVVGLCQSD IKKIRYPLYE PPRIFGHETA
     GTIAAVGSQV KGWQVGQRVA VMHHIPCMRC AYCLNDNFSM CDVYKNISTT AGFNASGGGF
     AEYVKVPGHI VENGGLIPIP DDISFEEASF VEPTNCCLKA VKKAQIAPGQ TVLVTGAGPI
     GLMFMMLVKY FGAKAIATDL LPSRIEKALE VGAEAAFDAR DADLSTKIQA LTGGMGVDVT
     LLAVPSDKAF FQALDCTRKG GKILFFAEFP DELTIPINPN TLYRREIDLM GSYSSSYRLQ
     SLSADIVFNR RIDVKALISD RYPLQDLPQA VDQAIAPTAE TYKILIYP
//