EzCatDB: S00608
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DB codeS00608
RLCP classification9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.268

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

Q56840
Protein name2-(R)-hydroxypropyl-CoM dehydrogenase2-(R)-Hydroxypropyl-CoM dehydrogenase
2-(2-(R)-Hydroxypropylthio)ethanesulfonate dehydrogenase
SynonymsR-HPCDH
EC 1.1.1.268
Aliphatic epoxide carboxylation component III
RefSeqYP_001409315.1 (Protein)
NC_009717.1 (DNA/RNA sequence)
PfamPF00106 (adh_short)
[Graphical view]


UniProtKB:Accession NumberQ56840
Entry nameHCDR_XANP2
Activity2-(R)-hydroxypropyl-CoM + NAD(+) = 2-oxopropyl-CoM + NADH.
SubunitHomodimer. Component III of the aliphatic epoxide carboxylation complex together with components I, II and IV.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC11496C00003C11497C00004C00080
Compound2-(R)-hydroxypropyl-CoMNAD+2-oxopropyl-CoMNADHH+
Typecarbohydrate,sulfide group,sulfonate groupamide group,amine group,nucleotidecarbohydrate,sulfide group,sulfonate groupamide group,amine group,nucleotideothers
ChEBI18354
15846
15881
16908
15378
PubChem443230
5893
443231
439153
1038
             
2cfcA00UnboundUnboundBound:KPCBound:NAD 
2cfcB00UnboundUnboundBound:KPCBound:NAD 
2cfcC00UnboundUnboundBound:KPCBound:NAD 
2cfcD00UnboundUnboundBound:KPCBound:NAD 

Active-site residues
pdbCatalytic residues
         
2cfcA00SER 142;TYR 155;LYS 159
2cfcB00SER 142;TYR 155;LYS 159
2cfcC00SER 142;TYR 155;LYS 159
2cfcD00SER 142;TYR 155;LYS 159

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.2737-2738
[4]Fig.1, p.8832

references
[1]
PubMed ID12198305
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages1470-3
AuthorsNocek B, Clark DD, Ensign SA, Peters JW
TitleCrystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase.
[2]
PubMed ID11851420
JournalBiochemistry
Year2002
Volume41
Pages2727-40
AuthorsClark DD, Ensign SA
TitleCharacterization of the 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase from Xanthobacter strain Py2: product inhibition, pH dependence of kinetic parameters, site-directed mutagenesis, rapid equilibrium inhibition, and chemical modification.
[3]
PubMed ID15157110
JournalBiochemistry
Year2004
Volume43
Pages6763-71
AuthorsClark DD, Boyd JM, Ensign SA
TitleThe stereoselectivity and catalytic properties of Xanthobacter autotrophicus 2-[(R)-2-Hydroxypropylthio]ethanesulfonate dehydrogenase are controlled by interactions between C-terminal arginine residues and the sulfonate of coenzyme M.
[4]
PubMed ID16846226
JournalBiochemistry
Year2006
Volume45
Pages8831-40
AuthorsKrishnakumar AM, Nocek BP, Clark DD, Ensign SA, Peters JW
TitleStructural basis for stereoselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases.
Related PDB2cfc
[5]
PubMed ID20302306
JournalBiochemistry
Year2010
Volume49
Pages3487-98
AuthorsSliwa DA, Krishnakumar AM, Peters JW, Ensign SA
TitleMolecular basis for enantioselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of stereoselective short-chain dehydrogenases/reductases involved in aliphatic epoxide carboxylation.

comments
This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily.
Since the active site is the same as those of the homologous enzymes (S00320, S00327, S00328, S00330, S00332, S00602, S00604, S00605 and S00610 in EzCatDB), this enzyme must catalyzes the same reaction as those homologues.

createdupdated
2012-09-142012-09-28


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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