ID   A0A3N1XCH3_9BURK        Unreviewed;       348 AA.
AC   A0A3N1XCH3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=L-iditol 2-dehydrogenase/threonine 3-dehydrogenase {ECO:0000313|EMBL:ROR24446.1};
GN   ORFNames=EC845_0471 {ECO:0000313|EMBL:ROR24446.1};
OS   Comamonas sp. BIGb0124.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=2485130 {ECO:0000313|EMBL:ROR24446.1, ECO:0000313|Proteomes:UP000267274};
RN   [1] {ECO:0000313|EMBL:ROR24446.1, ECO:0000313|Proteomes:UP000267274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIGb0124 {ECO:0000313|EMBL:ROR24446.1,
RC   ECO:0000313|Proteomes:UP000267274};
RA   Samuel B.;
RT   "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL   Submitted (NOV-2018) 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:ROR24446.1}.
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DR   EMBL; RJVF01000008; ROR24446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1XCH3; -.
DR   OrthoDB; 5484143at2; -.
DR   Proteomes; UP000267274; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000267274};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          12..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   348 AA;  36350 MW;  52CCEE211463D0FE CRC64;
     MQALRKTRPE HGLELLDLPS PASPGAGDVL IRVHATGVCG TDLHIDEWTP SYHFMKAALP
     VTIGHEFSGV VEAIGAGVED LKLGQLVAVR PSTVCGRCAS CQAGDFDGCV TRRGIGVARD
     GAFAPWVVAP ARNCLRMPEG VSPEVASLAE PLTVSHEAVR VGGVRPGDRV LVLGPGNIGQ
     GIALFARDAG ASQVVVAGHG DAPRLAVLRA MGFEHVVDFA ESGMQAGLAP YLADGPFDVV
     IEATGAAGVI APALQALKPR GVLVITGIHA APVPIDLAAL VRRHQEIRGS YRAPEANWQQ
     VVDFMERNHD TLALMITHRV PLAQALEGFA LARNKVATKV VVLPQAGA
//