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Conserved domains on  [gi|1878426118|gb|KAF5910257|]
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aldose 1-epimerase [Clarias magur]

Protein Classification

aldose epimerase family protein( domain architecture ID 10173257)

aldose epimerase family protein similar to Homo sapiens galactose mutarotase, which catalyzes the interconversion of beta-D-galactose and alpha-D-galactose during galactose metabolism

CATH:  2.70.98.10
EC:  5.1.3.-
Gene Ontology:  GO:0016857|GO:0030246|GO:0005975
PubMed:  12717027
SCOP:  4000040

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 20-210 3.87e-111

galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown 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. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.


:

Pssm-ID: 185696  Cd Length: 326  Bit Score: 321.38  E-value: 3.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  20 KWTLRSKS-VSVEIISLGCVITAIKTPDRKGQSADIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAI 98
Cdd:cd09019     1 LYTLTNGNgLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  99 NNGPNSLHGGIRGFDKAVWSSEAV-PNGVRLSHTSSDGDEGYPGNLKAAVTYTL-EENTLSIQYCAQTDQTTPINLTNHS 176
Cdd:cd09019    81 NEGPNHLHGGPKGFDKRVWDVEEVeENSVTFSLVSPDGEEGFPGNLTVTVTYTLtDDNELTIEYEATTDKPTPVNLTNHS 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1878426118 177 YFNLAGQGASDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:cd09019   161 YFNLAGEGSGDILDHELQINADRYLPVDEELIPT 194
 
Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 20-210 3.87e-111

galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown 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. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.


Pssm-ID: 185696  Cd Length: 326  Bit Score: 321.38  E-value: 3.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  20 KWTLRSKS-VSVEIISLGCVITAIKTPDRKGQSADIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAI 98
Cdd:cd09019     1 LYTLTNGNgLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  99 NNGPNSLHGGIRGFDKAVWSSEAV-PNGVRLSHTSSDGDEGYPGNLKAAVTYTL-EENTLSIQYCAQTDQTTPINLTNHS 176
Cdd:cd09019    81 NEGPNHLHGGPKGFDKRVWDVEEVeENSVTFSLVSPDGEEGFPGNLTVTVTYTLtDDNELTIEYEATTDKPTPVNLTNHS 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1878426118 177 YFNLAGQGASDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:cd09019   161 YFNLAGEGSGDILDHELQINADRYLPVDEELIPT 194
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
19-211 4.17e-79

Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 239.41  E-value: 4.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  19 EKWTLRSKSVSVEIISLGCVITAIKTPDRKGQsaDIVLGFDDLESYlTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAI 98
Cdd:COG2017     8 ELYTLENGGLRAVIPEYGATLTSLRVPDKDGR--DVLLGFDDLEDD-PPWAYGGAILGPYANRIADGRFTLDGKTYQLPI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  99 NNGPNSLHGGirgFDKAVWSSEAV-PNGVRLSHTSSDgDEGYPGNLKAAVTYTLEENTLSIQYCAQ--TDQTTPINLTNH 175
Cdd:COG2017    85 NEGPNALHGG---ARDRPWEVEEQsEDSVTLSLTSPD-EEGYPGNLELTVTYTLTDNGLTITYTATnlGDKPTPFNLGNH 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1878426118 176 SYFNLAGQGASDIYDHEVSITADSYLPVDDNMIPTE 211
Cdd:COG2017   161 PYFNLPGEGGGDIDDHRLQIPADEYLPVDEGLIPTG 196
PLN00194 PLN00194
aldose 1-epimerase; Provisional
 14-210 1.32e-74

aldose 1-epimerase; Provisional


Pssm-ID: 215098 [Multi-domain]  Cd Length: 337  Bit Score: 228.80  E-value: 1.32e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  14 GQRSVEKWTLRSKSVSVEIISLGCVITAIKTPDRKGQSADIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKV 93
Cdd:PLN00194    5 AEEKPGIYELKNGNISVKLTNYGATITSLILPDKNGKLADVVLGFDSVEPYKNDSPYFGAIVGRVANRIKGAKFTLNGVT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  94 YKLAINNGPNSLHGGIRGFDKAVWS----SEAVPNGVRLSHTSSDGDEGYPGNLKAAVTYTL-EENTLSIQYCAQT-DQT 167
Cdd:PLN00194   85 YKLPPNNGPNSLHGGPKGFSKVVWEvakyKKGEKPSITFKYHSFDGEEGFPGDLSVTVTYTLlSSNTLRLDMEAKPlNKA 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1878426118 168 TPINLTNHSYFNLAGQGASDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:PLN00194  165 TPVNLAQHTYWNLAGHNSGDILSHKIQIFGSHITPVDENLIPT 207
galM_Leloir TIGR02636
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ...
 22-210 1.29e-67

galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose 1-epimerase) and participate in the Leloir pathway for galactose/glucose interconversion. All members of the seed alignment for this model are found in gene clusters with other enzymes of the Leloir pathway. This enzyme family belongs to the aldose 1-epimerase family, described by pfam01263. However, the enzyme described as aldose 1-epimerase itself (EC 5.1.3.3) is called broadly specific for D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. The restricted genome context for genes in this family suggests members should act primarily on D-galactose.


Pssm-ID: 274240  Cd Length: 336  Bit Score: 211.07  E-value: 1.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  22 TLRSKS-VSVEIISLGCVITAIKTPDRKGqSADIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAINN 100
Cdd:TIGR02636   8 TLTNKNgMTISFMDIGATWLSCQVPLAGE-LREVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKTYQLSINQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118 101 GPNSLHGGIRGFDKAVWSSEAVPNG---VRLSHTSSDGDEGYPGNLKAAVTYTL-EENTLSIQYCAQTDQTTPINLTNHS 176
Cdd:TIGR02636  87 GPNCLHGGPEGFDKRRWTIETLEQAevqVKFSLESPDGDQGFPGNLTVSVTYTLtDDNELKIDYEATTDKATPFNLTNHV 166

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1878426118 177 YFNLAGQGA-SDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:TIGR02636 167 YFNLDGADAgSDVLNHELQLNADRYLPLDEEGIPL 201
Aldose_epim pfam01263
Aldose 1-epimerase;
19-210 1.55e-64

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 201.86  E-value: 1.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  19 EKWTLR-SKSVSVEIISLGCVITAIKTPDRKGqsaDIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKVYKLA 97
Cdd:pfam01263   1 DLITLTnGNGLSATISLYGATLLSLKVPGKLR---EVLLGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  98 INN-GPNSLHGGIRGFDkavWSSEAVPN--GVRLSHTSS-DGDEGYPGNLKAAVTYTL-EENTLSIQYCAQTD-QTTPIN 171
Cdd:pfam01263  78 QNGpGKNPLHGGARGRI---WEVEEVKPddGVTVTLVLDpDGEEGYPGDLEARVTYTLnEDNELTIEYEATNDgKPTPFN 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1878426118 172 LTNHSYFNLAGqgasDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:pfam01263 155 LGNHPYFNLSG----DIDIHELQIEADEYLEVDDDLIPT 189
 
Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 20-210 3.87e-111

galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown 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. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.


Pssm-ID: 185696  Cd Length: 326  Bit Score: 321.38  E-value: 3.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  20 KWTLRSKS-VSVEIISLGCVITAIKTPDRKGQSADIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAI 98
Cdd:cd09019     1 LYTLTNGNgLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  99 NNGPNSLHGGIRGFDKAVWSSEAV-PNGVRLSHTSSDGDEGYPGNLKAAVTYTL-EENTLSIQYCAQTDQTTPINLTNHS 176
Cdd:cd09019    81 NEGPNHLHGGPKGFDKRVWDVEEVeENSVTFSLVSPDGEEGFPGNLTVTVTYTLtDDNELTIEYEATTDKPTPVNLTNHS 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1878426118 177 YFNLAGQGASDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:cd09019   161 YFNLAGEGSGDILDHELQINADRYLPVDEELIPT 194
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
19-211 4.17e-79

Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 239.41  E-value: 4.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  19 EKWTLRSKSVSVEIISLGCVITAIKTPDRKGQsaDIVLGFDDLESYlTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAI 98
Cdd:COG2017     8 ELYTLENGGLRAVIPEYGATLTSLRVPDKDGR--DVLLGFDDLEDD-PPWAYGGAILGPYANRIADGRFTLDGKTYQLPI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  99 NNGPNSLHGGirgFDKAVWSSEAV-PNGVRLSHTSSDgDEGYPGNLKAAVTYTLEENTLSIQYCAQ--TDQTTPINLTNH 175
Cdd:COG2017    85 NEGPNALHGG---ARDRPWEVEEQsEDSVTLSLTSPD-EEGYPGNLELTVTYTLTDNGLTITYTATnlGDKPTPFNLGNH 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1878426118 176 SYFNLAGQGASDIYDHEVSITADSYLPVDDNMIPTE 211
Cdd:COG2017   161 PYFNLPGEGGGDIDDHRLQIPADEYLPVDEGLIPTG 196
PLN00194 PLN00194
aldose 1-epimerase; Provisional
 14-210 1.32e-74

aldose 1-epimerase; Provisional


Pssm-ID: 215098 [Multi-domain]  Cd Length: 337  Bit Score: 228.80  E-value: 1.32e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  14 GQRSVEKWTLRSKSVSVEIISLGCVITAIKTPDRKGQSADIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKV 93
Cdd:PLN00194    5 AEEKPGIYELKNGNISVKLTNYGATITSLILPDKNGKLADVVLGFDSVEPYKNDSPYFGAIVGRVANRIKGAKFTLNGVT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  94 YKLAINNGPNSLHGGIRGFDKAVWS----SEAVPNGVRLSHTSSDGDEGYPGNLKAAVTYTL-EENTLSIQYCAQT-DQT 167
Cdd:PLN00194   85 YKLPPNNGPNSLHGGPKGFSKVVWEvakyKKGEKPSITFKYHSFDGEEGFPGDLSVTVTYTLlSSNTLRLDMEAKPlNKA 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1878426118 168 TPINLTNHSYFNLAGQGASDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:PLN00194  165 TPVNLAQHTYWNLAGHNSGDILSHKIQIFGSHITPVDENLIPT 207
galM PRK11055
galactose-1-epimerase; Provisional
 22-211 1.27e-69

galactose-1-epimerase; Provisional


Pssm-ID: 182931  Cd Length: 342  Bit Score: 216.33  E-value: 1.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  22 TLRSKS-VSVEIISLGCVITAIKTPDRKGQSADIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAINN 100
Cdd:PRK11055   13 TLRNNAgMVVTLMDWGATWLSCRVPLSDGSVREVLLGCASPEDYPDQAAYLGASVGRYANRIANSRFTLDGETYQLSPNQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118 101 GPNSLHGGIRGFDKAVWSSEAV-PNGVRLSHTSSDGDEGYPGNLKAAVTYTL-EENTLSIQYCAQTDQTTPINLTNHSYF 178
Cdd:PRK11055   93 GGNQLHGGPEGFDKRRWQIVNQnDRQVTFSLSSPDGDQGFPGNLGATVTYRLtDDNRVSITYRATVDKPCPVNLTNHAYF 172

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1878426118 179 NLAGQGA-SDIYDHEVSITADSYLPVDDNMIPTE 211
Cdd:PRK11055  173 NLDGAEEgSDVRNHKLQINADEYLPVDEGGIPNG 206
galM_Leloir TIGR02636
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ...
 22-210 1.29e-67

galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose 1-epimerase) and participate in the Leloir pathway for galactose/glucose interconversion. All members of the seed alignment for this model are found in gene clusters with other enzymes of the Leloir pathway. This enzyme family belongs to the aldose 1-epimerase family, described by pfam01263. However, the enzyme described as aldose 1-epimerase itself (EC 5.1.3.3) is called broadly specific for D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. The restricted genome context for genes in this family suggests members should act primarily on D-galactose.


Pssm-ID: 274240  Cd Length: 336  Bit Score: 211.07  E-value: 1.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  22 TLRSKS-VSVEIISLGCVITAIKTPDRKGqSADIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAINN 100
Cdd:TIGR02636   8 TLTNKNgMTISFMDIGATWLSCQVPLAGE-LREVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKTYQLSINQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118 101 GPNSLHGGIRGFDKAVWSSEAVPNG---VRLSHTSSDGDEGYPGNLKAAVTYTL-EENTLSIQYCAQTDQTTPINLTNHS 176
Cdd:TIGR02636  87 GPNCLHGGPEGFDKRRWTIETLEQAevqVKFSLESPDGDQGFPGNLTVSVTYTLtDDNELKIDYEATTDKATPFNLTNHV 166

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1878426118 177 YFNLAGQGA-SDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:TIGR02636 167 YFNLDGADAgSDVLNHELQLNADRYLPLDEEGIPL 201
Aldose_epim pfam01263
Aldose 1-epimerase;
19-210 1.55e-64

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 201.86  E-value: 1.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  19 EKWTLR-SKSVSVEIISLGCVITAIKTPDRKGqsaDIVLGFDDLESYLTNPRYFGALVGRVANRIAKGQFVIEGKVYKLA 97
Cdd:pfam01263   1 DLITLTnGNGLSATISLYGATLLSLKVPGKLR---EVLLGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  98 INN-GPNSLHGGIRGFDkavWSSEAVPN--GVRLSHTSS-DGDEGYPGNLKAAVTYTL-EENTLSIQYCAQTD-QTTPIN 171
Cdd:pfam01263  78 QNGpGKNPLHGGARGRI---WEVEEVKPddGVTVTLVLDpDGEEGYPGDLEARVTYTLnEDNELTIEYEATNDgKPTPFN 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1878426118 172 LTNHSYFNLAGqgasDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:pfam01263 155 LGNHPYFNLSG----DIDIHELQIEADEYLEVDDDLIPT 189
Aldose_epim cd01081
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
 30-211 1.08e-34

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.


Pssm-ID: 185695 [Multi-domain]  Cd Length: 284  Bit Score: 124.50  E-value: 1.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  30 VEIISLGCVITAIktpdRKGQSADIVLGFDDLESYLTNP-RYFGALVGRVANRIAKGQFVIEGKVYKLAINNGPNSLHGG 108
Cdd:cd01081     3 AVIAPRGANIISL----KVKGDVDLLWGYPDAEEYPLAPtGGGGAILFPFANRISDGRYTFDGKQYPLNEDEGGNAIHGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118 109 IRGFDKAVWSSEAVPNGVRLSHTSSDGDEGYPGNLKAAVTYTLEENTLSIQYCAQ--TDQTTPINLTNHSYFNLAGqgaS 186
Cdd:cd01081    79 VRNLPWRVVATDEEEASVTLSYDLNDGPGGYPFPLELTVTYTLDADTLTITFTVTnlGDEPMPFGLGWHPYFGLPG---V 155

                         170       180
                  ....*....|....*....|....*
gi 1878426118 187 DIYDHEVSITADSYLPVDDNMIPTE 211
Cdd:cd01081   156 AIEDLRLRVPASKVLPLDDLLPPTG 180
PTZ00485 PTZ00485
aldolase 1-epimerase; Provisional
 62-210 5.52e-20

aldolase 1-epimerase; Provisional


Pssm-ID: 240435  Cd Length: 376  Bit Score: 86.98  E-value: 5.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  62 ESYlTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAINNGPNSLHGGIRGFDKAVWSSEAVPN----GVRLSHTSSDGDE 137
Cdd:PTZ00485   60 EAY-ADPDYMGATVGRCAGRVAGGVFTLDGVKYYTQKNRGENTCHCGDDAYHKKHWGMKLIETanviGVRFNYTSPHMEN 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118 138 GYPGNLKAAVTYTLEE---NTLSIQYCAQTDQT-----TPINLTNHSYFNLAG----QGASD--------IYDHEVSITA 197
Cdd:PTZ00485  139 GFPGELVSKVTYSIERskpNVLKTIYDSYIPETspadaTPVNIFNHAYWNLNGiperNGKKNavwvqpesVRNHWLRVPA 218

                         170
                  ....*....|...
gi 1878426118 198 DSYLPVDDNMIPT 210
Cdd:PTZ00485  219 SRVAEADRMAIPT 231
Aldose_epim_Ec_YihR cd09022
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ...
 53-211 6.02e-18

Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli YihR are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing 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.


Pssm-ID: 185699  Cd Length: 284  Bit Score: 79.92  E-value: 6.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  53 DIVLGFDDLEsylTNPRYFGALVGRVANRIAKGQFVIEGKVYKLAIN--NGPNSLHGGIRGfdkAVWS-SEAVPNGVRLS 129
Cdd:cd09022    21 DLVEPYPADE---VPPGAAGQVLAPWPNRIADGRYTFDGVEHQLPITepERGNAIHGLVRW---ADWQlVEHTDSSVTLR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118 130 HTSSDGdEGYPGNLKAAVTYTLEENTLSIQYCAQT--DQTTPINLTNHSYFNLagqGASDIYDHEVSITADSYLPVDDNM 207
Cdd:cd09022    95 TRIPPQ-PGYPFTLELTVTYELDDDGLTVTLTATNvgDEPAPFGVGFHPYLSA---GGAPLDECTLTLPADTWLPVDERL 170


                  ....
gi 1878426118 208 IPTE 211
Cdd:cd09022   171 LPTG 174
Aldose_epim_Ec_YphB cd09021
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ...
 79-214 1.53e-09

aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli YphB are uncharacterized members of the aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing 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.


Pssm-ID: 185698  Cd Length: 273  Bit Score: 56.53  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  79 ANRIAKGQFVIEGKVYKLAINNG--PNSLHGgiRGFDKAvWSSEAV-PNGVRLSHTSSDGDEGYPGnlKAAVTYTLEENT 155
Cdd:cd09021    47 SNRIRGGRFLFAGREVALPPNTAdePHPLHG--DGWRRP-WQVVAAsADSAELQLDHEADDPPWAY--RAEQRFHLAGDG 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878426118 156 LSIQYCAQT--DQTTPINLTNHSYFNLAGqgasdiyDHEVSITADSYLPVDDNMIPTEWCI 214
Cdd:cd09021   122 LSITLSVTNrgDRPMPAGLGFHPYFPRTP-------DTRLQADADGVWLEDEDHLPTGLRP 175
PRK15172 PRK15172
aldose-1-epimerase;
80-210 4.75e-07

aldose-1-epimerase;


Pssm-ID: 237918  Cd Length: 300  Bit Score: 49.43  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  80 NRIAKGQFVIEGKVYKLAINN--GPNSLHGGIRGFDKAVwsSEAVPNGVRLShTSSDGDEGYPGNLKAAVTYTLEENT-L 156
Cdd:PRK15172   64 NRIANGCYRYQGQEYQLPINEhvSKAAIHGLLAWRDWQI--SELTATSVTLT-AFLPPSYGYPFMLASQVIYSLDAATgL 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878426118 157 SIQYCAQT--DQTTPINLTNHSYF--NLAgqgasDIYDHEVSITADSYLPVDDNMIPT 210
Cdd:PRK15172  141 SVEIASQNigDVPAPYGVGIHPYLtcNLT-----SVDEYLLQLPANQVLAVDEHANPT 193
Aldose_epim_lacX cd09024
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ...
 21-160 2.18e-04

Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis lacX are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing 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.


Pssm-ID: 185701  Cd Length: 288  Bit Score: 41.38  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  21 WTLRSKSVSVEIISLGCVITAIKtpDRKgqsadivlgfDDLEsYLT--NPRYFG--A-----LVGRVANriakGQFVIEG 91
Cdd:cd09024     1 ITLENEFLTVTISEHGAELTSIK--DKK----------TGRE-YLWqgDPAYWGrhApilfpIVGRLKD----DTYTIDG 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  92 KVYKLAInngpnslHGGIRGFDKAVwsSEAVPNGVRLSHTSSDGD-EGYPGNLKAAVTYTLEENTLSIQY 160
Cdd:cd09024    64 KTYPMPQ-------HGFARDMEFEV--VEQSDDSVTFELTDNEETlKVYPFDFELRVTYTLEGNTLKVTY 124
Aldose_epim_Slr1438 cd09025
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis ...
 91-181 2.06e-03

Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis Slr1438 are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing 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.


Pssm-ID: 185702  Cd Length: 271  Bit Score: 38.38  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878426118  91 GKVYKLAInngpnslHGGIRgfdKAVWSSEAV--PNGVRLSHTSSDGD-EGYPGNLKAAVTYTLEENTLSIQ--YCAQTD 165
Cdd:cd09025    73 GQEYTLKQ-------HGFAR---DLPWEVELLgdGAGLTLTLRDNEATrAVYPFDFELELTYRLAGNTLEIAqrVHNLGD 142

                          90
                  ....*....|....*.
gi 1878426118 166 QTTPINLTNHSYFNLA 181
Cdd:cd09025   143 QPMPFSFGFHPYFAVP 158
 
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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