DB code: S00608

RLCP classification 9.5010.536200.8010 : Hydride transfer
9.1050.440000.8010 : Hydride transfer
CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.268
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase
R-HPCDH
EC 1.1.1.268
Aliphatic epoxide carboxylation component III
YP_001409315.1 (Protein)
NC_009717.1 (DNA/RNA sequence)
PF00106 (adh_short)
[Graphical View]

KEGG enzyme name
2-(R)-Hydroxypropyl-CoM dehydrogenase
2-(2-(R)-Hydroxypropylthio)ethanesulfonate dehydrogenase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q56840 HCDR_XANP2 2-(R)-hydroxypropyl-CoM + NAD(+) = 2-oxopropyl-CoM + NADH. Homodimer. Component III of the aliphatic epoxide carboxylation complex together with components I, II and IV.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C11496 C00003 C11497 C00004 C00080
E.C.
Compound 2-(R)-hydroxypropyl-CoM NAD+ 2-oxopropyl-CoM NADH H+
Type carbohydrate,sulfide group,sulfonate group amide group,amine group,nucleotide carbohydrate,sulfide group,sulfonate group amide group,amine group,nucleotide others
ChEBI 18354
15846
15881
16908
15378
PubChem 443230
5893
443231
439153
1038
2cfcA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:KPC Bound:NAD
2cfcB00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:KPC Bound:NAD
2cfcC00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:KPC Bound:NAD
2cfcD00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:KPC Bound:NAD

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
2cfcA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 142;TYR 155;LYS 159
2cfcB00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 142;TYR 155;LYS 159
2cfcC00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 142;TYR 155;LYS 159
2cfcD00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 142;TYR 155;LYS 159

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.2737-2738
[4]
Fig.1, p.8832

References
[1]
Resource
Comments
Medline ID
PubMed ID 12198305
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 1470-3
Authors Nocek B, Clark DD, Ensign SA, Peters JW
Title Crystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 11851420
Journal Biochemistry
Year 2002
Volume 41
Pages 2727-40
Authors Clark DD, Ensign SA
Title Characterization 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.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 15157110
Journal Biochemistry
Year 2004
Volume 43
Pages 6763-71
Authors Clark DD, Boyd JM, Ensign SA
Title The 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.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 16846226
Journal Biochemistry
Year 2006
Volume 45
Pages 8831-40
Authors Krishnakumar AM, Nocek BP, Clark DD, Ensign SA, Peters JW
Title Structural basis for stereoselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases.
Related PDB 2cfc
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 20302306
Journal Biochemistry
Year 2010
Volume 49
Pages 3487-98
Authors Sliwa DA, Krishnakumar AM, Peters JW, Ensign SA
Title Molecular basis for enantioselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of stereoselective short-chain dehydrogenases/reductases involved in aliphatic epoxide carboxylation.
Related PDB
Related UniProtKB

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.

Created Updated
2012-09-14 2012-09-28