DB code: D00840

CATH domain 3.40.50.1970 : Rossmann fold
1.20.1090.10 : Dehydroquinate synthase-like, alpha domain Catalytic domain
E.C. 1.1.1.77
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.20.1090.10 : Dehydroquinate synthase-like, alpha domain D00835
3.40.50.1970 : Rossmann fold D00835

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0A9S1 Lactaldehyde reductase
EC 1.1.1.77
Propanediol oxidoreductase
NP_417279.2 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491007.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00465 (Fe-ADH)
[Graphical View]

KEGG enzyme name
Lactaldehyde reductase
Propanediol:nicotinamide adenine dinucleotide (NAD+) oxidoreductase
L-Lactaldehyde:propanediol oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A9S1 FUCO_ECOLI (R)[or (S)]-propane-1,2-diol + NAD(+) = (R)[or (S)]-lactaldehyde + NADH. Iron (Potential).

KEGG Pathways
Map code Pathways E.C.
MAP00620 Pyruvate metabolism
MAP00630 Glyoxylate and dicarboxylate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00023 C02912 C02917 C00003 C00937 C00424 C00004 C00080
E.C. 1.1.1.77
Compound Iron (R)-propane-1,2-diol (S)-propane-1,2-diol NAD+ (R)-lactaldehyde (S)-lactaldehyde NADH H+
Type heavy metal carbohydrate carbohydrate amide group,amine group,nucleotide carbohydrate carbohydrate amide group,amine group,nucleotide others
ChEBI 18248
82664
28972
29002
15846
17167
18041
16908
15378
PubChem 23925
259994
439846
5893
439350
439231
439153
1038
1rrmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:APR Unbound Unbound Unbound
1rrmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:APR Unbound Unbound Unbound
2bi4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:NAD Unbound Unbound Unbound
2bi4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:NAD Unbound Unbound Unbound
2bl4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:NAD Unbound Unbound Unbound
2bl4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:NAD Unbound Unbound Unbound
1rrmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_ZN Analogue:PGO Unbound Unbound Unbound Unbound Unbound
1rrmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_ZN Analogue:PGO Unbound Unbound Unbound Unbound Unbound
2bi4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Unbound Unbound Unbound Unbound Unbound Unbound
2bi4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_FE Unbound Unbound Unbound Unbound Unbound Unbound
2bl4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2bl4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2], [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1rrmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1rrmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2bi4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2bi4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2bl4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2bl4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1rrmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 267 ASP 196;HIS 200;HIS 263;HIS 277
1rrmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 267 ASP 196;HIS 200;HIS 263;HIS 277
2bi4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 267 ASP 196;HIS 200;HIS 263;HIS 277
2bi4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 1267 ASP 1196;HIS 1200;HIS 1263;HIS 1277
2bl4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 267 ASP 196;HIS 200;HIS 263;HIS 277
2bl4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 1267 ASP 1196;HIS 1200;HIS 1263;HIS 1277

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.211-212
[5]
p.4960-4961

References
[1]
Resource
Comments
Medline ID
PubMed ID 8185833
Journal Crit Rev Microbiol
Year 1994
Volume 20
Pages 13-56
Authors Reid MF, Fewson CA
Title Molecular characterization of microbial alcohol dehydrogenases.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 9851711
Journal Eur J Biochem
Year 1998
Volume 258
Pages 207-13
Authors Obradors N, Cabiscol E, Aguilar J, Ros J
Title Site-directed mutagenesis studies of the metal-binding center of the iron-dependent propanediol oxidoreductase from Escherichia coli.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 11566129
Journal Structure
Year 2001
Volume 9
Pages 789-802
Authors Ruzheinikov SN, Burke J, Sedelnikova S, Baker PJ, Taylor R, Bullough PA, Muir NM, Gore MG, Rice DW
Title Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 15995211
Journal J Bacteriol
Year 2005
Volume 187
Pages 4957-66
Authors Montella C, Bellsolell L, Perez-Luque R, Badia J, Baldoma L, Coll M, Aguilar J
Title Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli.
Related PDB 2bi4 2bl4
Related UniProtKB

Comments
This enzyme belongs to the group III "iron-activated" dehydrogenases.
This enzyme is homologous to glycerol dehydrogenase (D00835 in EzCatDB), whose metal cofactor is zinc ion, instead of iron (see [3]). However, this enzyme adopts iron ion as a cofactor, with slightly different binding site from that of the homologous enyzme (see [4]).
According to the literature [4], although His267 does not interact with the hydroxyl group of the substrate, it might interact with it through a water molecule. Possibly, it may act as a general base-acid.
Moreover, the substrate hydroxyl group is bound to the iron ion, along with Asp196, His200, His263 and His277. The iron cofactor seems to lower the pKa of the hydroxyl group, facilitating the hydride transfer from the substrate to the nicotinamide C4 atom of NAD (see [4]).

Created Updated
2010-02-17 2011-05-19