ID   HCDS2_XANP2             Reviewed;         230 AA.
AC   A7IQF2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Inactive 2-(S)-hydroxypropyl-CoM dehydrogenase 2 {ECO:0000305};
DE   AltName: Full=SHPCDH2 {ECO:0000303|PubMed:20302306};
GN   Name=xecE2 {ECO:0000303|PubMed:20302306};
GN   OrderedLocusNames=Xaut_5050 {ECO:0000312|EMBL:ABS70248.1};
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG   Plasmid pXAUT01.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of plasmid pXAUT01 of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   LACK OF ACTIVITY.
RC   STRAIN=ATCC BAA-1158 / Py2;
RX   PubMed=20302306; DOI=10.1021/bi100294m;
RA   Sliwa D.A., Krishnakumar A.M., Peters J.W., Ensign S.A.;
RT   "Molecular basis for enantioselectivity in the (R)- and (S)-
RT   hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of
RT   stereoselective short-chain dehydrogenases/reductases involved in aliphatic
RT   epoxide carboxylation.";
RL   Biochemistry 49:3487-3498(2010).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Lacks 2-(S)-hydroxypropyl-CoM dehydrogenase activity. Contains
CC       apparent mutations in the N-terminal region, including the lack of key
CC       NAD(+)-binding residues, which may explain the lack of activity.
CC       {ECO:0000269|PubMed:20302306}.
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DR   EMBL; CP000782; ABS70248.1; -; Genomic_DNA.
DR   STRING; 78245.Xaut_5050; -.
DR   EnsemblBacteria; ABS70248; ABS70248; Xaut_5050.
DR   KEGG; xau:Xaut_5050; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_0_5; -.
DR   OMA; VWDTTMA; -.
DR   PhylomeDB; A7IQF2; -.
DR   Proteomes; UP000002417; Plasmid pXAUT01.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Plasmid; Reference proteome.
FT   CHAIN           1..230
FT                   /note="Inactive 2-(S)-hydroxypropyl-CoM dehydrogenase 2"
FT                   /id="PRO_0000454345"
SQ   SEQUENCE   230 AA;  23190 MW;  EE5DF7A58A2B1F7D CRC64;
     MARAAVRAGA KVALIDRDGA CAEKAAAEIG AAAWGVGADV TDEAAIAAAM AGAERALGPL
     TGLVNNAGIA GFGSVHTTEV ETWGRIMAVN VTGTFLASKA ALSGMLERRR GAIVNFGSVA
     GLVGIPSMAA YCAAKGAVVS LTRQMAAEYS GQGIRVNVVC PGTVASTDMG RQLLGQDADP
     ELEARRLAKY PIGRFGTPED IAEAAIFLLS TKAAFVTGCV FAVDGGMTAI