ID   A0A1J5GBZ9_9BACT        Unreviewed;       341 AA.
AC   A0A1J5GBZ9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Sorbitol dehydrogenase {ECO:0000313|EMBL:OIP70245.1};
GN   ORFNames=AUK42_04350 {ECO:0000313|EMBL:OIP70245.1};
OS   Candidatus Atribacteria bacterium CG2_30_33_13.
OC   Bacteria; Atribacterota.
OX   NCBI_TaxID=1805029 {ECO:0000313|EMBL:OIP70245.1, ECO:0000313|Proteomes:UP000182763};
RN   [1] {ECO:0000313|EMBL:OIP70245.1, ECO:0000313|Proteomes:UP000182763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_33_13 {ECO:0000313|EMBL:OIP70245.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:OIP70245.1}.
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DR   EMBL; MNYY01000087; OIP70245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5GBZ9; -.
DR   STRING; 1805029.AUK42_04350; -.
DR   Proteomes; UP000182763; Unassembled WGS sequence.
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; cd08258; Zn_ADH4; 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          10..337
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   341 AA;  37293 MW;  F7FE1D88B7C8BBFC CRC64;
     MKALVKYGKG QNDIELRDIP EPIPQENEVK VKVEATGICG TDLYGYSAVK PPVVLGHETA
     GIVVKVGKGV KDIRVGDKVT TETTAYICGQ CKFCQSKNYN LCIHRKGLGS AVNGAFAEYF
     VIRKESIHLI PPHINFISAS LFEPLSCATH AVMEQANLLK GETTLILGPG PFGLLIAQVA
     QVIGARVIMV GIKGDEKRLA LAKNLGISLV FNIEKKDLED YLSNIITENG IDVIFECSGS
     IAAVKYGLKI IRKGGRFIQA GIVHQPIKLR FDKILFDKEL TIIGSRTQKP SSWDKAINLV
     NKGEVNLGKL VSDVLPLSNW KEGYKRAKEK NSIKVVLQPD K
//