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Conserved domains on  [gi|79320733|ref|NP_001031233|]
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NDH-dependent cyclic electron flow 1 [Arabidopsis thaliana]

Protein Classification

aldose epimerase family protein( domain architecture ID 52393)

aldose epimerase family protein catalyzes the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose

CATH:  2.70.98.10
Gene Ontology:  GO:0016853|GO:0030246
SCOP:  4000040

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Aldose_epim super family cl14648
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
52-203 1.52e-04

aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism; they catalyze the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen.


The actual alignment was detected with superfamily member cd09020:

Pssm-ID: 449342  Cd Length: 269  Bit Score: 42.60  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79320733  52 MVELKvRNGSSLKLSLSDAHVLSYKPKvywkdeGFEEVLYTVDgdesrggvgvvivngEEPKGGSSVISG---------- 121
Cdd:cd09020   1 AIVLD-HPGASAEIALQGAQVLSWKPK------GGQDLLWLSP---------------QAPFDGGKAIRGgipvcwpwfg 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79320733 122 ----------------CDWSVKDTDSDAiDALQIELSCTAGVLD---------ITYIVSLYPVSMATALVVKNNGRKPVT 176
Cdd:cd09020  59 phgpnadlpahgfartRLWELLEVSEDE-DGVTVSLELDDTDETraiwphafeLRLTVTLGFDTLELELTVTNTGDKPFS 137
                       170       180
                ....*....|....*....|....*..
gi 79320733 177 LKPGIMSYLRFKKRSGAGIQGLKGCSY 203
Cdd:cd09020 138 FTAALHTYFRVSDIEQVRVEGLEGATY 164
 
Name Accession Description Interval E-value
D-hex-6-P-epi_like cd09020
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces ...
52-203 1.52e-04

D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces cerevisiae belongs to the large superfamily of aldose-1-epimerases. Its active site is very similar to the catalytic site of galactose mutarotase, the best studied member of the superfamily. It also contains the conserved glutamate and histidine residues that have been shown in galactose mutarotase to be critical for catalysis, the glutamate serving as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. In addition Ymr099c contains 2 conserved arginine residues which are involved in phosphate binding, and exhibits hexose-6-phosphate mutarotase activity on glucose-6-P, galactose-6-P and mannose-6-P.


Pssm-ID: 185697  Cd Length: 269  Bit Score: 42.60  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79320733  52 MVELKvRNGSSLKLSLSDAHVLSYKPKvywkdeGFEEVLYTVDgdesrggvgvvivngEEPKGGSSVISG---------- 121
Cdd:cd09020   1 AIVLD-HPGASAEIALQGAQVLSWKPK------GGQDLLWLSP---------------QAPFDGGKAIRGgipvcwpwfg 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79320733 122 ----------------CDWSVKDTDSDAiDALQIELSCTAGVLD---------ITYIVSLYPVSMATALVVKNNGRKPVT 176
Cdd:cd09020  59 phgpnadlpahgfartRLWELLEVSEDE-DGVTVSLELDDTDETraiwphafeLRLTVTLGFDTLELELTVTNTGDKPFS 137
                       170       180
                ....*....|....*....|....*..
gi 79320733 177 LKPGIMSYLRFKKRSGAGIQGLKGCSY 203
Cdd:cd09020 138 FTAALHTYFRVSDIEQVRVEGLEGATY 164
 
Name Accession Description Interval E-value
D-hex-6-P-epi_like cd09020
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces ...
52-203 1.52e-04

D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces cerevisiae belongs to the large superfamily of aldose-1-epimerases. Its active site is very similar to the catalytic site of galactose mutarotase, the best studied member of the superfamily. It also contains the conserved glutamate and histidine residues that have been shown in galactose mutarotase to be critical for catalysis, the glutamate serving as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. In addition Ymr099c contains 2 conserved arginine residues which are involved in phosphate binding, and exhibits hexose-6-phosphate mutarotase activity on glucose-6-P, galactose-6-P and mannose-6-P.


Pssm-ID: 185697  Cd Length: 269  Bit Score: 42.60  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79320733  52 MVELKvRNGSSLKLSLSDAHVLSYKPKvywkdeGFEEVLYTVDgdesrggvgvvivngEEPKGGSSVISG---------- 121
Cdd:cd09020   1 AIVLD-HPGASAEIALQGAQVLSWKPK------GGQDLLWLSP---------------QAPFDGGKAIRGgipvcwpwfg 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79320733 122 ----------------CDWSVKDTDSDAiDALQIELSCTAGVLD---------ITYIVSLYPVSMATALVVKNNGRKPVT 176
Cdd:cd09020  59 phgpnadlpahgfartRLWELLEVSEDE-DGVTVSLELDDTDETraiwphafeLRLTVTLGFDTLELELTVTNTGDKPFS 137
                       170       180
                ....*....|....*....|....*..
gi 79320733 177 LKPGIMSYLRFKKRSGAGIQGLKGCSY 203
Cdd:cd09020 138 FTAALHTYFRVSDIEQVRVEGLEGATY 164
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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