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Conserved domains on  [gi|487407277|ref|WP_001675324|]
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MULTISPECIES: aldose-1-epimerase [Salmonella]

Protein Classification

aldose-1-epimerase( domain architecture ID 10014991)

aldose-1-epimerase catalyzes the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose; similar to Escherichia coli protein YihR

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK15172 PRK15172
aldose-1-epimerase;
1-285 0e+00

aldose-1-epimerase;


:

Pssm-ID: 237918  Cd Length: 300  Bit Score: 564.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   1 MRMAAMHSGGKTIQLNAGHYQAKIVTVGAGLAELTHHGRHVVIPHKPEEIPMAHLGKVLIPWPNRVTNGCYSYNGKVFQL 80
Cdd:PRK15172   1 MQITNMHSSGQTISLAAGDYQATIVTVGAGLAELTFQGRHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  81 AVNDPVSQTAIHGLLAWRDWQINYQSTTEASLTIFLPPSYGYPFALISEVIYRLDAASGLHVLIRTQNIGDESAPYGAGA 160
Cdd:PRK15172  81 PINEHVSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATGLSVEIASQNIGDVPAPYGVGI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 161 HPYLTCNLQSIDSCVLTLPASEELPA---------------GRDFSASCLLGETRLDHAVKTATTPaeWEVRLTSPTQNM 225
Cdd:PRK15172 161 HPYLTCNLTSVDEYLLQLPANQVLAVdehanpttlhhvdelDLDFSQAKKIAATKIDHTFKTANDL--WEVRITHPQQAL 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 226 STFLRSTQPWLQIYTGEKLSRKGLAVEPMSCPPDAFNSGIALIHLAPKAIHQLHFSIGCD 285
Cdd:PRK15172 239 SVSLCSDQPWLQIYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLEPGKTHRLFFNIGGQ 298
 
Name Accession Description Interval E-value
PRK15172 PRK15172
aldose-1-epimerase;
1-285 0e+00

aldose-1-epimerase;


Pssm-ID: 237918  Cd Length: 300  Bit Score: 564.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   1 MRMAAMHSGGKTIQLNAGHYQAKIVTVGAGLAELTHHGRHVVIPHKPEEIPMAHLGKVLIPWPNRVTNGCYSYNGKVFQL 80
Cdd:PRK15172   1 MQITNMHSSGQTISLAAGDYQATIVTVGAGLAELTFQGRHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  81 AVNDPVSQTAIHGLLAWRDWQINYQSTTEASLTIFLPPSYGYPFALISEVIYRLDAASGLHVLIRTQNIGDESAPYGAGA 160
Cdd:PRK15172  81 PINEHVSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATGLSVEIASQNIGDVPAPYGVGI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 161 HPYLTCNLQSIDSCVLTLPASEELPA---------------GRDFSASCLLGETRLDHAVKTATTPaeWEVRLTSPTQNM 225
Cdd:PRK15172 161 HPYLTCNLTSVDEYLLQLPANQVLAVdehanpttlhhvdelDLDFSQAKKIAATKIDHTFKTANDL--WEVRITHPQQAL 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 226 STFLRSTQPWLQIYTGEKLSRKGLAVEPMSCPPDAFNSGIALIHLAPKAIHQLHFSIGCD 285
Cdd:PRK15172 239 SVSLCSDQPWLQIYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLEPGKTHRLFFNIGGQ 298
Aldose_epim_Ec_YihR cd09022
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ...
 20-282 8.90e-103

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: 301.41  E-value: 8.90e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  20 YQAKIVTVGAGLAELTHHGRHVVIPHKPEEIPMAHLGKVLIPWPNRVTNGCYSYNGKVFQLAVNDPVSQTAIHGLLAWRD 99
Cdd:cd09022    1 YRAVVTEVGAGLRSLTVGGRDLVEPYPADEVPPGAAGQVLAPWPNRIADGRYTFDGVEHQLPITEPERGNAIHGLVRWAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 100 WQINYQSTTEASLTIFLPPSYGYPFALISEVIYRLDAAsGLHVLIRTQNIGDESAPYGAGAHPYLTCNLQSIDSCVLTLP 179
Cdd:cd09022   81 WQLVEHTDSSVTLRTRIPPQPGYPFTLELTVTYELDDD-GLTVTLTATNVGDEPAPFGVGFHPYLSAGGAPLDECTLTLP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 180 ASEE-------LPAGR--------DFSASCLLGETRLDHAVKTATTPA--EWEVRLTSPTQN-MSTFLRSTQPWLQIYTG 241
Cdd:cd09022  160 ADTWlpvderlLPTGTepvagtpyDFRTGRRLGGTALDTAFTDLTRDAdgRARARLTGPDGRgVELWADESFPWVQVFTA 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 487407277 242 EKLS----RKGLAVEPMSCPPDAFNSGIALIHLAPKAIHQLHFSI 282
Cdd:cd09022  240 DTLPppgrRRGLAVEPMTCPPNAFNSGTDLIVLAPGETHTASWGI 284
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
8-282 6.43e-72

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


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 223.62  E-value: 6.43e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   8 SGGKTIQLNAGHYQAKIVTVGAGLAELTH---HGRHVVIPHK--PEEIPMAHLGKVLIPWPNRVTNGCYSYNGKVFQLAV 82
Cdd:COG2017    5 PDGELYTLENGGLRAVIPEYGATLTSLRVpdkDGRDVLLGFDdlEDDPPWAYGGAILGPYANRIADGRFTLDGKTYQLPI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  83 NDPvsQTAIHGLLAWRDWQINYQSTTEASLTIFLPPSYGYPFALISEVIYRLDAAsGLHVLIRTQNIGDESAPYGAGAHP 162
Cdd:COG2017   85 NEG--PNALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGNLELTVTYTLTDN-GLTITYTATNLGDKPTPFNLGNHP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 163 YLTCNLQ---SIDSCVLTLPASEEL-------PAGR---------DFSASCLLGETRLDHAVKTATTPAEWEVRLTSPTQ 223
Cdd:COG2017  162 YFNLPGEgggDIDDHRLQIPADEYLpvdegliPTGElapvagtpfDFREPRPLGDGGFDHAFVGLDSDGRPAARLTDPDS 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487407277 224 NMSTFLRSTQ-PWLQIYTGEKLS--RKGLAVEPMSCPPDAFNSG--IALIHLAPKAIHQLHFSI 282
Cdd:COG2017  242 GRRLEVSTDEfPGLQVYTGNFLDpgRDGVCLEPQTGPPDAPNHPgfEGLIVLAPGETYSATTRI 305
Aldose_epim pfam01263
Aldose 1-epimerase;
11-282 3.29e-55

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 180.29  E-value: 3.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   11 KTIQLNAGH-YQAKIVTVGAGLAELTHHG--RHVVIPHKPEEI---PMAHLGKVLIPWPNRVTNGCYSYNGKVFQLAVND 84
Cdd:pfam01263   1 DLITLTNGNgLSATISLYGATLLSLKVPGklREVLLGSDDAEGylkDSNYFGATLGPYANRIANGRFELDGIPYCLPQNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   85 PvSQTAIHGLLAWRDWQINYQST---TEASLTIFLPPSYGYPFALISEVIYRLDAASGLHVLIRTQNIGdESAPYGAGAH 161
Cdd:pfam01263  81 P-GKNPLHGGARGRIWEVEEVKPddgVTVTLVLDPDGEEGYPGDLEARVTYTLNEDNELTIEYEATNDG-KPTPFNLGNH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  162 PYLTCNLqSIDSCVLTLPASEELP----------------AGRDFSASCLLGET--RLDHAVKtaTTPAEWEVRLTSPTQ 223
Cdd:pfam01263 159 PYFNLSG-DIDIHELQIEADEYLEvdddliptgelkdvkgTPFDFRQPTPIGEDilGYDHVYL--LDPLKAVIIDPDPGS 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487407277  224 NMSTFLRSTQPWLQIYTG-----EKLSRKGLAVEPMSCPPDAFNSGIALIHLAPKAIHQLHFSI 282
Cdd:pfam01263 236 GIVLEVSTTQPGLVVYTPnflkgKYLSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAETSY 299
 
Name Accession Description Interval E-value
PRK15172 PRK15172
aldose-1-epimerase;
1-285 0e+00

aldose-1-epimerase;


Pssm-ID: 237918  Cd Length: 300  Bit Score: 564.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   1 MRMAAMHSGGKTIQLNAGHYQAKIVTVGAGLAELTHHGRHVVIPHKPEEIPMAHLGKVLIPWPNRVTNGCYSYNGKVFQL 80
Cdd:PRK15172   1 MQITNMHSSGQTISLAAGDYQATIVTVGAGLAELTFQGRHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  81 AVNDPVSQTAIHGLLAWRDWQINYQSTTEASLTIFLPPSYGYPFALISEVIYRLDAASGLHVLIRTQNIGDESAPYGAGA 160
Cdd:PRK15172  81 PINEHVSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATGLSVEIASQNIGDVPAPYGVGI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 161 HPYLTCNLQSIDSCVLTLPASEELPA---------------GRDFSASCLLGETRLDHAVKTATTPaeWEVRLTSPTQNM 225
Cdd:PRK15172 161 HPYLTCNLTSVDEYLLQLPANQVLAVdehanpttlhhvdelDLDFSQAKKIAATKIDHTFKTANDL--WEVRITHPQQAL 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 226 STFLRSTQPWLQIYTGEKLSRKGLAVEPMSCPPDAFNSGIALIHLAPKAIHQLHFSIGCD 285
Cdd:PRK15172 239 SVSLCSDQPWLQIYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLEPGKTHRLFFNIGGQ 298
Aldose_epim_Ec_YihR cd09022
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ...
 20-282 8.90e-103

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: 301.41  E-value: 8.90e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  20 YQAKIVTVGAGLAELTHHGRHVVIPHKPEEIPMAHLGKVLIPWPNRVTNGCYSYNGKVFQLAVNDPVSQTAIHGLLAWRD 99
Cdd:cd09022    1 YRAVVTEVGAGLRSLTVGGRDLVEPYPADEVPPGAAGQVLAPWPNRIADGRYTFDGVEHQLPITEPERGNAIHGLVRWAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 100 WQINYQSTTEASLTIFLPPSYGYPFALISEVIYRLDAAsGLHVLIRTQNIGDESAPYGAGAHPYLTCNLQSIDSCVLTLP 179
Cdd:cd09022   81 WQLVEHTDSSVTLRTRIPPQPGYPFTLELTVTYELDDD-GLTVTLTATNVGDEPAPFGVGFHPYLSAGGAPLDECTLTLP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 180 ASEE-------LPAGR--------DFSASCLLGETRLDHAVKTATTPA--EWEVRLTSPTQN-MSTFLRSTQPWLQIYTG 241
Cdd:cd09022  160 ADTWlpvderlLPTGTepvagtpyDFRTGRRLGGTALDTAFTDLTRDAdgRARARLTGPDGRgVELWADESFPWVQVFTA 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 487407277 242 EKLS----RKGLAVEPMSCPPDAFNSGIALIHLAPKAIHQLHFSI 282
Cdd:cd09022  240 DTLPppgrRRGLAVEPMTCPPNAFNSGTDLIVLAPGETHTASWGI 284
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
8-282 6.43e-72

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


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 223.62  E-value: 6.43e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   8 SGGKTIQLNAGHYQAKIVTVGAGLAELTH---HGRHVVIPHK--PEEIPMAHLGKVLIPWPNRVTNGCYSYNGKVFQLAV 82
Cdd:COG2017    5 PDGELYTLENGGLRAVIPEYGATLTSLRVpdkDGRDVLLGFDdlEDDPPWAYGGAILGPYANRIADGRFTLDGKTYQLPI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  83 NDPvsQTAIHGLLAWRDWQINYQSTTEASLTIFLPPSYGYPFALISEVIYRLDAAsGLHVLIRTQNIGDESAPYGAGAHP 162
Cdd:COG2017   85 NEG--PNALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGNLELTVTYTLTDN-GLTITYTATNLGDKPTPFNLGNHP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 163 YLTCNLQ---SIDSCVLTLPASEEL-------PAGR---------DFSASCLLGETRLDHAVKTATTPAEWEVRLTSPTQ 223
Cdd:COG2017  162 YFNLPGEgggDIDDHRLQIPADEYLpvdegliPTGElapvagtpfDFREPRPLGDGGFDHAFVGLDSDGRPAARLTDPDS 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487407277 224 NMSTFLRSTQ-PWLQIYTGEKLS--RKGLAVEPMSCPPDAFNSG--IALIHLAPKAIHQLHFSI 282
Cdd:COG2017  242 GRRLEVSTDEfPGLQVYTGNFLDpgRDGVCLEPQTGPPDAPNHPgfEGLIVLAPGETYSATTRI 305
Aldose_epim pfam01263
Aldose 1-epimerase;
11-282 3.29e-55

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 180.29  E-value: 3.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   11 KTIQLNAGH-YQAKIVTVGAGLAELTHHG--RHVVIPHKPEEI---PMAHLGKVLIPWPNRVTNGCYSYNGKVFQLAVND 84
Cdd:pfam01263   1 DLITLTNGNgLSATISLYGATLLSLKVPGklREVLLGSDDAEGylkDSNYFGATLGPYANRIANGRFELDGIPYCLPQNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277   85 PvSQTAIHGLLAWRDWQINYQST---TEASLTIFLPPSYGYPFALISEVIYRLDAASGLHVLIRTQNIGdESAPYGAGAH 161
Cdd:pfam01263  81 P-GKNPLHGGARGRIWEVEEVKPddgVTVTLVLDPDGEEGYPGDLEARVTYTLNEDNELTIEYEATNDG-KPTPFNLGNH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  162 PYLTCNLqSIDSCVLTLPASEELP----------------AGRDFSASCLLGET--RLDHAVKtaTTPAEWEVRLTSPTQ 223
Cdd:pfam01263 159 PYFNLSG-DIDIHELQIEADEYLEvdddliptgelkdvkgTPFDFRQPTPIGEDilGYDHVYL--LDPLKAVIIDPDPGS 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487407277  224 NMSTFLRSTQPWLQIYTG-----EKLSRKGLAVEPMSCPPDAFNSGIALIHLAPKAIHQLHFSI 282
Cdd:pfam01263 236 GIVLEVSTTQPGLVVYTPnflkgKYLSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAETSY 299
Aldose_epim cd01081
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
 20-273 3.70e-46

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: 156.47  E-value: 3.70e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  20 YQAKIVTVGAGLAELTH-HGRHVVIPHKPEEIPMAHL----GKVLIPWPNRVTNGCYSYNGKVFQLAVNDPVSqtAIHGL 94
Cdd:cd01081    1 AVAVIAPRGANIISLKVkGDVDLLWGYPDAEEYPLAPtgggGAILFPFANRISDGRYTFDGKQYPLNEDEGGN--AIHGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  95 LAWRDWQINYQSTTEASLTIFL---PPSYGYPFALISEVIYRLDAaSGLHVLIRTQNIGDESAPYGAGAHPYLTCNLQSI 171
Cdd:cd01081   79 VRNLPWRVVATDEEEASVTLSYdlnDGPGGYPFPLELTVTYTLDA-DTLTITFTVTNLGDEPMPFGLGWHPYFGLPGVAI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 172 DSCVLTLPASEELPAGR--------------DFSASCLLGETRLDHA----VKTATTPaewEVRLTSPTQNMSTFLRSTQ 233
Cdd:cd01081  158 EDLRLRVPASKVLPLDDllpptgelevpgeeDFRLGRPLGGGELDDCflllGNDAGTA---EARLEDPDSRISVEFETGW 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 487407277 234 PWLQIYTGEKLSRKGLAVEPMSCPPDAF-NSGIALIHLAPK 273
Cdd:cd01081  235 PFWQVYTGDGGRRGSVAIEPMTSAPDAFfNNNGGLITLKPP 275
Aldose_epim_Ec_YphB cd09021
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ...
 27-272 5.81e-21

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: 89.66  E-value: 5.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  27 VGAGLAELTHHG--RHVVIPHKPEEipmAHLGKV----LIPWPNRVTNGCYSYNGKVFQLAVNDPVSQTAIHGLlAWRD- 99
Cdd:cd09021    8 LGGSIAALTSRGdpTPLLRPADPDA---ADALAMacfpLVPFSNRIRGGRFLFAGREVALPPNTADEPHPLHGD-GWRRp 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 100 WQINYQSTTEASLTIFLPPSYGyPFALISEVIYRLDAAsGLHVLIRTQNIGDESAPYGAGAHPYLTCNLQS---IDSCVL 176
Cdd:cd09021   84 WQVVAASADSAELQLDHEADDP-PWAYRAEQRFHLAGD-GLSITLSVTNRGDRPMPAGLGFHPYFPRTPDTrlqADADGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 177 TLPASEELPAGR-------DFSASCLLGETRLDHA-----VKTATTPAEWEVRLTSPTQNMStflrstqPWLQIYT--GE 242
Cdd:cd09021  162 WLEDEDHLPTGLrphppdwDFSQPRPLPDRWIDNCftgwdGAALIWPPERGLALTIEADAPF-------SHLVVYRppGE 234

                        250       260       270
                 ....*....|....*....|....*....|..
gi 487407277 243 KLsrkgLAVEPMSCPPDAFNSGIA--LIHLAP 272
Cdd:cd09021  235 DF----FCLEPVSHAPDAHHGPGDpgLRVLAP 262
Aldose_epim_Slr1438 cd09025
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis ...
 58-282 1.51e-15

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: 74.59  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  58 VLIPWPNRVTNGCYSYNGKVFQLAvndpvsqtaIHGLlAwRD--WQINYQSTTeASLTIFLPPS----YGYPFALISEVI 131
Cdd:cd09025   56 ILFPICGNLPDDGYPLAGQEYTLK---------QHGF-A-RDlpWEVELLGDG-AGLTLTLRDNeatrAVYPFDFELELT 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 132 YRLdAASGLHVLIRTQNIGDESAPYGAGAHPYLTCNlqSIDSCVLTLPAS--------EELPAGRDFSAScllgETRLDH 203
Cdd:cd09025  124 YRL-AGNTLEIAQRVHNLGDQPMPFSFGFHPYFAVP--DKAKLSLDLPPTrcfdqktdEEANTPGQFDET----EEGVDL 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 204 AVKTATtpaewEVRLTSPTQNMSTFLRSTQPW--LQIYTgEKlSRKGLAVEPMSCPPDAFNSGIALIHLAPKAIHQLHFS 281
Cdd:cd09025  197 LFRPLG-----PASLTDGARGLKITLDHDEPFsnLVVWT-DK-GKDFVCLEPWTGPRNALNTGERLLLLPPGETEEASVR 269


                 .
gi 487407277 282 I 282
Cdd:cd09025  270 I 270
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 16-262 5.08e-11

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: 62.14  E-value: 5.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  16 NAGHYQAKIVTVGAGLAELTHHGRHvvipHKPEEI------------PMAHLGKVLIPWPNRVTNGCYSYNGKVFQLAVN 83
Cdd:cd09019    6 NGNGLRVSILNYGATIQSLKVPDKN----GKLRDVvlgfddledylkNSPYFGATVGRVANRIANGRFTLDGKTYQLEAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  84 DPVsqTAIH-GLLAW--RDWQINYQSTTEASLTIFLPPSY-GYPFALISEVIYRLDAASGLHVLIR-----------TQn 148
Cdd:cd09019   82 EGP--NHLHgGPKGFdkRVWDVEEVEENSVTFSLVSPDGEeGFPGNLTVTVTYTLTDDNELTIEYEattdkptpvnlTN- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 149 igdesapygagaHPYLtcNL-----QSIDSCVLTLPAS-------EELPAGR---------DFSASCLLGETR------- 200
Cdd:cd09019  159 ------------HSYF--NLagegsGDILDHELQINADrylpvdeELIPTGEilpvagtpfDFRKPKPIGRIDlddeqlk 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 201 ----LDHA--VKTATTPAEWEVRLTSPTQN--MSTFlrSTQPWLQIYTGEKLS------------RKGLAVEPmSCPPDA 260
Cdd:cd09019  225 lgggYDHNfvLDKGGGKLRPAARLTSPESGrkLEVY--TTQPGVQFYTGNFLDgtpggggkvygkRSGFCLET-QHFPDA 301


                 ..
gi 487407277 261 FN 262
Cdd:cd09019  302 PN 303
Aldose_epim_lacX cd09024
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ...
 58-162 3.14e-08

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: 53.70  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  58 VLIPWPNRVTNGCYSYNGKVFQLavndpvSQtaiHGLLAWRDWQINYQSTTEASLTIflppSYG------YPFALISEVI 131
Cdd:cd09024   46 ILFPIVGRLKDDTYTIDGKTYPM------PQ---HGFARDMEFEVVEQSDDSVTFEL----TDNeetlkvYPFDFELRVT 112

                         90       100       110
                 ....*....|....*....|....*....|.
gi 487407277 132 YRLDAAsGLHVLIRTQNIGDESAPYGAGAHP 162
Cdd:cd09024  113 YTLEGN-TLKVTYEVKNPDDKTMPFSIGGHP 142
galM PRK11055
galactose-1-epimerase; Provisional
 46-262 1.15e-07

galactose-1-epimerase; Provisional


Pssm-ID: 182931  Cd Length: 342  Bit Score: 52.23  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277  46 KPEEIP--MAHLGKVLIPWPNRVTNGCYSYNGKVFQLAVNDPVSQtaIHGLLAW---RDWQINYQSTTEASLTIFLPP-S 119
Cdd:PRK11055  52 SPEDYPdqAAYLGASVGRYANRIANSRFTLDGETYQLSPNQGGNQ--LHGGPEGfdkRRWQIVNQNDRQVTFSLSSPDgD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 120 YGYPFALISEVIYRLDAASGLHvlIRTQNIGDESAPYGAGAHPYLtcNLQSIDS---CV---LTLPASEELP-------- 185
Cdd:PRK11055 130 QGFPGNLGATVTYRLTDDNRVS--ITYRATVDKPCPVNLTNHAYF--NLDGAEEgsdVRnhkLQINADEYLPvdeggipn 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487407277 186 --------AGRDFSASCLLGETRL-----------DHA-----VKTATTPAeweVRLTSPTQNMSTFLRSTQPWLQIYTG 241
Cdd:PRK11055 206 gglksvagTSFDFRQPKTIAQDFLadddqqkvkgyDHAfllqaKGDGKKPA---AHLWSPDEKLQMKVYTTAPALQFYSG 282

                        250       260       270
                 ....*....|....*....|....*....|...
gi 487407277 242 EKL----SRK--------GLAVEPmSCPPDAFN 262
Cdd:PRK11055 283 NFLagtpSRGggpyadyaGLALES-QFLPDSPN 314
 
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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