ID   HCDS_XANP2              Reviewed;         249 AA.
AC   Q56841; A7IPY4;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=2-(S)-hydroxypropyl-CoM dehydrogenase;
DE            Short=S-HPCDH;
DE            EC=1.1.1.269;
DE   AltName: Full=Aliphatic epoxide carboxylation component IV;
GN   Name=xecE; OrderedLocusNames=Xaut_4869;
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG   Plasmid pXAUT01.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95219103; PubMed=7704278;
RA   Swaving J., Weijers C.A.G.M., van Ooyen A.J.J., de Bont J.A.M.;
RT   "Complementation of Xanthobacter Py2 mutants in epoxyalkane
RT   degradation; expression and nucleotide sequence of the complementing
RT   DNA fragment.";
RL   Microbiology 141:477-484(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.,
RA   Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Ensigns S.A., Richardson P.;
RT   "Complete sequence of plasmid pXAUT01 of Xanthobacter autotrophicus
RT   Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-10, AND CHARACTERIZATION.
RX   MEDLINE=98070376; PubMed=9405410; DOI=10.1074/jbc.272.51.32121;
RA   Allen J.R., Ensign S.A.;
RT   "Purification to homogeneity and reconstitution of the individual
RT   components of the epoxide carboxylase multiprotein enzyme complex from
RT   Xanthobacter strain Py2.";
RL   J. Biol. Chem. 272:32121-32128(1997).
RN   [4]
RP   REVIEW.
RX   MEDLINE=22889473; PubMed=12524213;
RX   DOI=10.1146/annurev.biochem.72.121801.161820;
RA   Ensign S.A., Allen J.R.;
RT   "Aliphatic epoxide carboxylation.";
RL   Annu. Rev. Biochem. 72:55-76(2003).
CC   -!- FUNCTION: Catalyzes the oxidation of 2-(S)-hydroxyalkyl thioesters
CC       of CoM to 2-oxoalkyl thioesters of CoM. The enzyme highly specific
CC       for the S enantiomers.
CC   -!- CATALYTIC ACTIVITY: 2-(S)-hydroxypropyl-CoM + NAD(+) = 2-
CC       oxopropyl-CoM + NADH.
CC   -!- PATHWAY: Alkene metabolism; propylene degradation.
CC   -!- SUBUNIT: Homodimer. Component IV of the aliphatic epoxide
CC       carboxylation complex together with components I, II and III.
CC   -!- INDUCTION: By aliphatic and chlorinated alkenes.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X79863; CAA56245.1; -; Genomic_DNA.
DR   EMBL; CP000782; ABS70080.1; -; Genomic_DNA.
DR   PIR; S47055; S47055.
DR   RefSeq; YP_001409316.1; -.
DR   HSSP; Q12634; 1G0N.
DR   GeneID; 5420357; -.
DR   GenomeReviews; CP000782_GR; Xaut_4869.
DR   KEGG; xau:Xaut_4869; -.
DR   BioCyc; MetaCyc:MON-13284; -.
DR   GO; GO:0050575; F:2-(S)-hydroxypropyl-CoM dehydrogenase activity; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; NAD; Oxidoreductase;
KW   Plasmid.
FT   CHAIN         1    249       2-(S)-hydroxypropyl-CoM dehydrogenase.
FT                                /FTId=PRO_0000054706.
FT   ACT_SITE    150    150       Proton acceptor (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   CONFLICT      4      4       A -> N (in Ref. 3; AA sequence).
SQ   SEQUENCE   249 AA;  24941 MW;  B5E0B82C1D8D9782 CRC64;
     MLDAEVIAIT GGAAGIGLAV AHAAIRAGAR VALIDRDGAC AQRAAAEFGA AAWGVGADVT
     DEAAITAAMA GAQRALGPLT GLVNNAGIAG FGSVHATEVE TWSRIMAVNV TGTFLASKAA
     LFGMLERGRG AIVNFGSVAG LVGIPTMAAY CAAKGAVVNL TRQMAADYSG RGIRVNVVCP
     GTVAGTDMGR QLLGTDCDPE LEARRLAKYP MGRFGTPEDI AEAAVFLLST KAAFVTGSVL
     AVDGGMTAI
//