ID   A0A0K2M2V2_9NOST        Unreviewed;       348 AA.
AC   A0A0K2M2V2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Sorbitol dehydrogenase {ECO:0000313|EMBL:ALB42393.1};
GN   ORFNames=AA650_19720 {ECO:0000313|EMBL:ALB42393.1};
OS   Anabaena sp. WA102.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB42393.1, ECO:0000313|Proteomes:UP000056652};
RN   [1] {ECO:0000313|EMBL:ALB42393.1, ECO:0000313|Proteomes:UP000056652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA102 {ECO:0000313|EMBL:ALB42393.1,
RC   ECO:0000313|Proteomes:UP000056652};
RA   Brown N.M.;
RT   "The finished genome of an anatoxin-a-producing Anabaena isolate reveals
RT   extensive genome rearrangement.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP011456; ALB42393.1; -; Genomic_DNA.
DR   RefSeq; WP_053540319.1; NZ_CP011456.1.
DR   AlphaFoldDB; A0A0K2M2V2; -.
DR   STRING; 1647413.AA650_19720; -.
DR   KEGG; awa:AA650_19720; -.
DR   PATRIC; fig|1647413.5.peg.4650; -.
DR   OrthoDB; 9770526at2; -.
DR   Proteomes; UP000056652; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   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;  37945 MW;  C2EDAAF1AA9DF74D CRC64;
     MKAQVFRGVN QLSYEEVPVP TLDADEVLVQ VRVVGLCQSD IKKIRYPLYE PPRIFGHETA
     GTIAAVGSQV KGWQVGQRVA VMHHIPCMRC AYCLNDNFSM CDVYKNISTT AGFNASGGGF
     AEYVKVPAHI VENGGLIPIP DDISFEEASF VEPTNCCLKA VKKAEIAPGQ TVLVTGAGPI
     GLMFMMLVKY FGAKAIATDL LPSRIEKALE VGAEAAFDAR DADLSTKIQA LTGGMGVDVT
     LLAVPSDKAF FQALDCTRKG GKILFFAEFP DELTIPINPN TLYRREIDLM GSYSSSYRLQ
     SLSADIVFNR RIDVKALISD RYPLQNLSQA VDQAIAPTAE TYKILIYP
//