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Database: UniProt
Entry: G0MS16_CAEBE
LinkDB: G0MS16_CAEBE
Original site: G0MS16_CAEBE 
ID   G0MS16_CAEBE            Unreviewed;       347 AA.
AC   G0MS16;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Sorbitol dehydrogenase {ECO:0000256|ARBA:ARBA00026132};
DE   AltName: Full=Polyol dehydrogenase {ECO:0000256|ARBA:ARBA00032485};
GN   ORFNames=CAEBREN_11804 {ECO:0000313|EMBL:EGT42724.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; GL379809; EGT42724.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0MS16; -.
DR   STRING; 135651.G0MS16; -.
DR   EnsemblMetazoa; CBN11804.1; CBN11804.1; WBGene00150529.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_5_1; -.
DR   InParanoid; G0MS16; -.
DR   OMA; VCEMSGH; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05285; sorbitol_DH; 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   InterPro; IPR045306; SDH-like.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161:SF9; SORBITOL 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:UP000008068};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          12..345
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   347 AA;  37477 MW;  E5DA500FF11A1B76 CRC64;
     MSEDNLSAVL YGVDDLRLEQ VAIPKPGPKQ VQIRVHTVGI CGSDVHYWTH GSIGPFVVKE
     PMIVGHETSG VVSEVGSEVT HLKVGDRIAM EPGLPCKLCE HCKTGRYNLC PEMKFFATPP
     INGTLSRYVV HDADFCFKLP DNLSFEDGAL IEPLSVAIHS CRRGNVQMGH RVLVCGAGPI
     GVLNLLTAKA VGAGKVVITD LDEGRLALAK KLGADATINV KGKSIETVRA EIITALEYQQ
     PQVCIECTGA QPSIETAITT TKSGGVIVLV GLGADRVDIP IIESATREVD MRGIFRYVNC
     YPTAIELLSS GKLDLSGLTR AHYKLEETLE AFKRTQKADV IKVFIQC
//
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