HCDS1_XANP2
ID HCDS1_XANP2 Reviewed; 249 AA.
AC Q56841; A7IPY4;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=2-(S)-hydroxypropyl-CoM dehydrogenase 1 {ECO:0000303|PubMed:10411892};
DE Short=S-HPCDH 1 {ECO:0000303|PubMed:11851420};
DE EC=1.1.1.269 {ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:20302306};
DE AltName: Full=2-[(S)-2-hydroxypropylthio]ethanesulfonate dehydrogenase 1 {ECO:0000303|PubMed:11851420};
DE AltName: Full=Aliphatic epoxide carboxylation component IV;
DE AltName: Full=Epoxide carboxylase component IV {ECO:0000303|PubMed:9405410};
DE AltName: Full=SHPCDH1 {ECO:0000303|PubMed:20302306};
GN Name=xecE1 {ECO:0000303|PubMed:20302306};
GN Synonyms=xecE {ECO:0000303|PubMed:11851420}; OrderedLocusNames=Xaut_4869;
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 [GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RX PubMed=7704278; DOI=10.1099/13500872-141-2-477;
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 degradation;
RT expression and nucleotide sequence of the complementing DNA fragment.";
RL Microbiology 141:477-484(1995).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC BAA-1158 / Py2;
RX 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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC BAA-1158 / Py2;
RX PubMed=10411892; DOI=10.1073/pnas.96.15.8432;
RA Allen J.R., Clark D.D., Krum J.G., Ensign S.A.;
RT "A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial
RT pathway of aliphatic epoxide carboxylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8432-8437(1999).
RN [5]
RP NOMENCLATURE.
RC STRAIN=ATCC BAA-1158 / Py2;
RX PubMed=11851420; DOI=10.1021/bi0118005;
RA Clark D.D., Ensign S.A.;
RT "Characterization of the 2-[(R)-2-hydroxypropylthio]ethanesulfonate
RT dehydrogenase from Xanthobacter strain Py2: product inhibition, pH
RT dependence of kinetic parameters, site-directed mutagenesis, rapid
RT equilibrium inhibition, and chemical modification.";
RL Biochemistry 41:2727-2740(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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).
RN [7]
RP REVIEW.
RX PubMed=12524213; 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: Involved in aliphatic epoxide carboxylation (PubMed:9405410,
CC PubMed:10411892). Catalyzes the reversible oxidation of (2S)-2-
CC hydroxypropyl-coenzyme M (S-HPC) to 2-oxopropyl-coenzyme M (2-KPC)
CC (PubMed:10411892, PubMed:20302306). The enzyme is highly specific for
CC the S enantiomers (PubMed:10411892, PubMed:20302306).
CC {ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:20302306,
CC ECO:0000269|PubMed:9405410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxypropyl-coenzyme M + NAD(+) = 2-oxopropyl-
CC coenzyme M + H(+) + NADH; Xref=Rhea:RHEA:21052, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57552, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58430; EC=1.1.1.269;
CC Evidence={ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:20302306};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21053;
CC Evidence={ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:20302306};
CC -!- ACTIVITY REGULATION: Not inhibited by 2-(2-methyl-2-
CC hydroxypropylthio)ethanesulfonate (M-HPC), an achiral analog of both R-
CC HPC and S-HPC. {ECO:0000269|PubMed:20302306}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=220 uM for S-HPC {ECO:0000269|PubMed:20302306};
CC KM=240 uM for 2-KPC {ECO:0000269|PubMed:20302306};
CC KM=5200 uM for R-HPC {ECO:0000269|PubMed:20302306};
CC Note=kcat is 28 sec(-1) with S-HPC as substrate. kcat is 20 sec(-1)
CC with 2-KPC as substrate. kcat is 2.4 sec(-1) with R-HPC as substrate.
CC {ECO:0000269|PubMed:20302306};
CC -!- PATHWAY: Alkene metabolism; propylene degradation.
CC {ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:9405410}.
CC -!- SUBUNIT: Homodimer (PubMed:9405410). Component IV of the aliphatic
CC epoxide carboxylation complex together with components I, II and III
CC (PubMed:9405410, PubMed:10411892). {ECO:0000269|PubMed:10411892,
CC ECO:0000269|PubMed:9405410}.
CC -!- INDUCTION: By aliphatic and chlorinated alkenes.
CC -!- MISCELLANEOUS: Enantioselectivity is dictated largely by changes in Km.
CC {ECO:0000269|PubMed:20302306}.
CC -!- MISCELLANEOUS: Is difficult to express due to its tendency to form
CC inclusion bodies in heterologous expression systems.
CC {ECO:0000269|PubMed:11851420}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305|PubMed:11851420}.
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DR EMBL; X79863; CAA56245.1; -; Genomic_DNA.
DR EMBL; CP000782; ABS70080.1; -; Genomic_DNA.
DR PIR; S47055; S47055.
DR RefSeq; WP_011992984.1; NC_009717.1.
DR AlphaFoldDB; Q56841; -.
DR SMR; Q56841; -.
DR STRING; 78245.Xaut_4869; -.
DR EnsemblBacteria; ABS70080; ABS70080; Xaut_4869.
DR KEGG; xau:Xaut_4869; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_2_10_5; -.
DR OMA; FTVSNQY; -.
DR OrthoDB; 1356861at2; -.
DR PhylomeDB; Q56841; -.
DR BioCyc; MetaCyc:MON-13284; -.
DR BRENDA; 1.1.1.269; 1641.
DR UniPathway; UPA00776; -.
DR Proteomes; UP000002417; Plasmid pXAUT01.
DR GO; GO:0050575; F:2-(S)-hydroxypropyl-CoM dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0042208; P:propylene catabolic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Nucleotide-binding; Oxidoreductase;
KW Plasmid; Reference proteome.
FT CHAIN 1..249
FT /note="2-(S)-hydroxypropyl-CoM dehydrogenase 1"
FT /id="PRO_0000054706"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 58..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 137
FT /ligand="(2S)-2-hydroxypropyl-coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58430"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 150
FT /ligand="(2S)-2-hydroxypropyl-coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58430"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 182
FT /ligand="(2S)-2-hydroxypropyl-coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58430"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 183..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT BINDING 209
FT /ligand="(2S)-2-hydroxypropyl-coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58430"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT SITE 137
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT SITE 154
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:A7IQH5"
FT CONFLICT 4
FT /note="A -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
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
