Information on EC 1.1.1.251 - galactitol-1-phosphate 5-dehydrogenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.1.1.251
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RECOMMENDED NAME
GeneOntology No.
galactitol-1-phosphate 5-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
galactitol-1-phosphate + NAD+ = L-tagatose 6-phosphate + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
galactitol degradation
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degradation of sugar alcohols
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Galactose metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
galactitol-1-phosphate:NAD+ oxidoreductase
The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway. It contains two zinc atoms per subunit.
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CAS REGISTRY NUMBER
COMMENTARY hide
167618-25-9
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60120-43-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K12 JWL194BN
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
structure shows a pentacoordinated zinc ion in complex with a polyol
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37422
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x * 37422, calculation from nucleotide sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modeling of structure and docking analysis of substrate, Zn2+ and NAD+. Cys 37, His 58, Glu 59, Glu 142 residues form an active site pocket similar to known GPDH. A catalytic Zn2+-binding domain and a cofactor NAD+-binding domain with strong hydrogen bonding contacts with the substrate and the cofactor are identified
structures of open state with Zn2+ in the catalytic site and of the closed state in complex with the polyols Tris and glycerol, respectively. The closed state reveals no bound cofactor. The glycerol binding mode reveals a pentacoordinated zinc ion in complex with a polyol and also a strong hydrogen bond between the primary hydroxyl group and the conserved Glu144
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gat genes isolated from the wild-type isolate Escherichia coli EC3132 and cloned on a 7.8-kbp PstI DNA fragment, catD codes for EC 1.1.1.251
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Show AA Sequence (143 entries)
Please use the Sequence Search for a specific query.
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.251)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)