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Information on EC 1.1.1.251 - galactitol-1-phosphate 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.251
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.251 galactitol-1-phosphate 5-dehydrogenase
IUBMB Comments
The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway. It contains two zinc atoms per subunit.
The enzyme appears in viruses and cellular organisms
showSynonyms
galactitol-1-phosphate 5-dehydrogenase, gat1p-specific nad-dependent dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
galactitol-1-phosphate dehydrogenase (Escherichia coli strain EC3132 gene gatD)
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-
-
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Gat1P-specific NAD-dependent dehydrogenase
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-
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GatD
Genbank X79837-derived protein
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-
-
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NAD-dependent Gat1P-dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
galactitol 1-phosphate + NAD+ = D-tagatose 6-phosphate + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
galactitol degradation
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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
167618-25-9
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60120-43-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Substrates: -
Products: -
Products: -
?
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Substrates: enzyme is involved in the galactitol metabolism
Products: -
Products: -
?
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Substrates: -
Products: -
Products: -
?
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
Substrates: -
Products: -
Products: -
?
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Substrates: enzyme is involved in the galactitol metabolism
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Substrates: enzyme is involved in the galactitol metabolism
Products: -
Products: -
?
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Substrates: enzyme is involved in the galactitol metabolism
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
structure shows a pentacoordinated zinc ion in complex with a polyol
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A090NXS5_SHIDY
346
0
37392
TrEMBL
other Location (Reliability: 1)
A0A0E0Y0I1_ECO1C
Escherichia coli O104:H4 (strain 2011C-3493)
346
0
37438
TrEMBL
-
A0A0H3PTH3_ECO5C
Escherichia coli O157:H7 (strain EC869)
346
0
37390
TrEMBL
other Location (Reliability: 4)
A0A2S8DSF7_SHIBO
346
0
37480
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2X2I7G7_SHIDY
346
0
37392
TrEMBL
other Location (Reliability: 5)
A0A2Y4YCC6_SHIFL
346
0
37405
TrEMBL
other Location (Reliability: 5)
A0A376K4Z0_ECOLX
346
0
37375
TrEMBL
other Location (Reliability: 3)
A0A376M5S8_ECOLX
346
0
37445
TrEMBL
Secretory Pathway (Reliability: 1)
A0A377D7X2_ECOLX
338
0
36628
TrEMBL
other Location (Reliability: 1)
A0A377HE03_ECOLX
346
0
37371
TrEMBL
other Location (Reliability: 2)
A0A6D0USK8_ECOLX
346
0
37375
TrEMBL
other Location (Reliability: 2)
A0A6L6I5A0_ECOLX
346
0
37418
TrEMBL
Secretory Pathway (Reliability: 3)
A0A836ZAK6_ECOLX
346
0
37478
TrEMBL
-
A0A979GG09_ECOSE
Escherichia coli (strain SE11)
346
0
37368
TrEMBL
other Location (Reliability: 2)
A0A9P2UZT9_ECOLX
346
0
37390
TrEMBL
other Location (Reliability: 2)
A0AAD2VF19_ECOLX
346
0
37390
TrEMBL
Mitochondrion (Reliability: 3)
A0AAN3MA09_ECOLX
346
0
37420
TrEMBL
other Location (Reliability: 1)
A0AAN3ZHI9_SHIDY
346
0
37371
TrEMBL
other Location (Reliability: 2)
A0AAN4NTF0_ECOLX
346
0
37452
TrEMBL
-
A0AAW7UVQ1_ECOLX
346
0
37540
TrEMBL
Mitochondrion (Reliability: 4)
A0ABD7FL08_ECOLX
346
0
37390
TrEMBL
Secretory Pathway (Reliability: 3)
A7ZNR0_ECO24
Escherichia coli O139:H28 (strain E24377A / ETEC)
346
0
37390
TrEMBL
-
B2TY97_SHIB3
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
346
0
37480
TrEMBL
-
B7L9W1_ECO55
Escherichia coli (strain 55989 / EAEC)
346
0
37438
TrEMBL
-
C3SCQ0_ECOLX
346
0
37390
TrEMBL
other Location (Reliability: 4)
E0J6P5_ECOLW
Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB 8666 / NRRL B-766 / W)
346
0
37390
TrEMBL
Secretory Pathway (Reliability: 3)
Q32EB2_SHIDS
Shigella dysenteriae serotype 1 (strain Sd197)
346
0
37392
TrEMBL
-
Q323D0_SHIBS
Shigella boydii serotype 4 (strain Sb227)
346
0
37436
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0H3N4Z0_CLODC
Clostridioides difficile (strain CD196)
350
0
38278
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nobelmann, B.; Lengeler, J.W.
Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli
Biochim. Biophys. Acta
1262
69-72
1995
Escherichia coli, Escherichia coli EC3132
brenda
Nobelmann, B.; Lengeler, J.W.
Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism
J. Bacteriol.
178
6790-6795
1996
Escherichia coli, Escherichia coli K12 JWL194BN
brenda
Benavente, R.; Esteban-Torres, M.; Kohring, G.W.; Cortes-Cabrera, A.; Sanchez-Murcia, P.A.; Gago, F.; Acebron, I.; de las Rivas, B.; Munoz, R.; Mancheno, J.M.
Enantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coli
Acta Crystallogr. Sect. D
71
1540-1554
2015
Escherichia coli (P0A9S3), Escherichia coli
brenda
Razali, S.; Sarah Diana, P.; Shamsir, M.; Mahadi, N.; Mohd Illias, R.
Substrate and cofactor binding interaction studies of galactitol-1-phosphate 5-dehydrogenase from Peptoclostridium difficile
J. Teknol.
78
199-210
2016
Clostridioides difficile (A0A0H3N4Z0), Clostridioides difficile CD196 (A0A0H3N4Z0)
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.251)
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