|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15172 |
PRK15172 |
aldose-1-epimerase; |
9-308 |
0e+00 |
|
aldose-1-epimerase;
Pssm-ID: 237918 Cd Length: 300 Bit Score: 590.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 9 MQITNMHCSGQTVSLAAGDYHATIVTVGAGLAELTFQGCHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQL 88
Cdd:PRK15172 1 MQITNMHSSGQTISLAAGDYQATIVTVGAGLAELTFQGRHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 89 PINEHSSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVVYSLNAHTGLSVEIASQNIGTVAAPYGVGI 168
Cdd:PRK15172 81 PINEHVSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATGLSVEIASQNIGDVPAPYGVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 169 HPYLTCNLTSVDEYLFQLPANQVYAVDEHANPTTLHHVDELDLNFTQAKKIAATKIDHTFKTANDLWEMTITHPQQALSV 248
Cdd:PRK15172 161 HPYLTCNLTSVDEYLLQLPANQVLAVDEHANPTTLHHVDELDLDFSQAKKIAATKIDHTFKTANDLWEVRITHPQQALSV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 249 SLCSDQLWVQVYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLESGKPHRLFFNIYGQRK 308
Cdd:PRK15172 241 SLCSDQPWLQIYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLEPGKTHRLFFNIGGQRK 300
|
|
| Aldose_epim_Ec_YihR |
cd09022 |
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ... |
28-303 |
4.65e-130 |
|
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: 371.52 E-value: 4.65e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 28 YHATIVTVGAGLAELTFQGCHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQLPINEHSSKAAIHGLLAWRD 107
Cdd:cd09022 1 YRAVVTEVGAGLRSLTVGGRDLVEPYPADEVPPGAAGQVLAPWPNRIADGRYTFDGVEHQLPITEPERGNAIHGLVRWAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 108 WQISELTATSVTLTAFLPPSYGYPFMLASQVVYSLNAHtGLSVEIASQNIGTVAAPYGVGIHPYLTCNLTSVDEYLFQLP 187
Cdd:cd09022 81 WQLVEHTDSSVTLRTRIPPQPGYPFTLELTVTYELDDD-GLTVTLTATNVGDEPAPFGVGFHPYLSAGGAPLDECTLTLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 188 ANQVYAVDEHANPTTLHHVDELDLNFTQAKKIAATKIDHTFKT----ANDLWEMTITHPQQaLSVSLCSDQL--WVQVYS 261
Cdd:cd09022 160 ADTWLPVDERLLPTGTEPVAGTPYDFRTGRRLGGTALDTAFTDltrdADGRARARLTGPDG-RGVELWADESfpWVQVFT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 49176437 262 GEKL----QRQGLAVEPMSCPPNAFNSGIDLLLLESGKPHRLFFNI 303
Cdd:cd09022 239 ADTLpppgRRRGLAVEPMTCPPNAFNSGTDLIVLAPGETHTASWGI 284
|
|
| GalM |
COG2017 |
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism]; |
17-303 |
2.33e-79 |
|
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
Pssm-ID: 441620 [Multi-domain] Cd Length: 309 Bit Score: 243.26 E-value: 2.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 17 SGQTVSLAAGDYHATIVTVGAGLAELTF---QGCHLVIPHK--PEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQLPIN 91
Cdd:COG2017 6 DGELYTLENGGLRAVIPEYGATLTSLRVpdkDGRDVLLGFDdlEDDPPWAYGGAILGPYANRIADGRFTLDGKTYQLPIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 92 EHssKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVVYSLNAHtGLSVEIASQNIGTVAAPYGVGIHPY 171
Cdd:COG2017 86 EG--PNALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGNLELTVTYTLTDN-GLTITYTATNLGDKPTPFNLGNHPY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 172 LTCNL---TSVDEYLFQLPANQVYAVDEHANPT-TLHHVDELDLNFTQAKKIAATKIDHTFKTAN--DLWEMTITHPQQA 245
Cdd:COG2017 163 FNLPGeggGDIDDHRLQIPADEYLPVDEGLIPTgELAPVAGTPFDFREPRPLGDGGFDHAFVGLDsdGRPAARLTDPDSG 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49176437 246 LSVSLCSDQL-WVQVYSGEKLQ--RQGLAVEPMSCPPNAFNS--GIDLLLLESGKPHRLFFNI 303
Cdd:COG2017 243 RRLEVSTDEFpGLQVYTGNFLDpgRDGVCLEPQTGPPDAPNHpgFEGLIVLAPGETYSATTRI 305
|
|
| Aldose_epim |
pfam01263 |
Aldose 1-epimerase; |
19-304 |
1.66e-59 |
|
Aldose 1-epimerase;
Pssm-ID: 396013 Cd Length: 300 Bit Score: 192.23 E-value: 1.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 19 QTVSLAAGD-YHATIVTVGAGLAELTFQGC--HLVIPHKPEEMPL---AHLGKVLIPWPNRIANGCYRYQGQEYQLPINE 92
Cdd:pfam01263 1 DLITLTNGNgLSATISLYGATLLSLKVPGKlrEVLLGSDDAEGYLkdsNYFGATLGPYANRIANGRFELDGIPYCLPQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 93 HsSKAAIHGLLAWRDWQISELTA---TSVTLTAFLPPSYGYPFMLASQVVYSLNAHTGLSVEIASQNIGTvAAPYGVGIH 169
Cdd:pfam01263 81 P-GKNPLHGGARGRIWEVEEVKPddgVTVTLVLDPDGEEGYPGDLEARVTYTLNEDNELTIEYEATNDGK-PTPFNLGNH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 170 PYLTCNLTsVDEYLFQLPANQVYAVDEHANPTTLH-HVDELDLNFTQAKKIAAT--KIDHTFKTANDLWEMTITHPQQAL 246
Cdd:pfam01263 159 PYFNLSGD-IDIHELQIEADEYLEVDDDLIPTGELkDVKGTPFDFRQPTPIGEDilGYDHVYLLDPLKAVIIDPDPGSGI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49176437 247 SVSLCSDQLWVQVYSG-----EKLQRQGLAVEPMSCPPNAFNSGIDLLLLESGKPHRLFFNIY 304
Cdd:pfam01263 238 VLEVSTTQPGLVVYTPnflkgKYLSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAETSYS 300
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15172 |
PRK15172 |
aldose-1-epimerase; |
9-308 |
0e+00 |
|
aldose-1-epimerase;
Pssm-ID: 237918 Cd Length: 300 Bit Score: 590.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 9 MQITNMHCSGQTVSLAAGDYHATIVTVGAGLAELTFQGCHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQL 88
Cdd:PRK15172 1 MQITNMHSSGQTISLAAGDYQATIVTVGAGLAELTFQGRHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 89 PINEHSSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVVYSLNAHTGLSVEIASQNIGTVAAPYGVGI 168
Cdd:PRK15172 81 PINEHVSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATGLSVEIASQNIGDVPAPYGVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 169 HPYLTCNLTSVDEYLFQLPANQVYAVDEHANPTTLHHVDELDLNFTQAKKIAATKIDHTFKTANDLWEMTITHPQQALSV 248
Cdd:PRK15172 161 HPYLTCNLTSVDEYLLQLPANQVLAVDEHANPTTLHHVDELDLDFSQAKKIAATKIDHTFKTANDLWEVRITHPQQALSV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 249 SLCSDQLWVQVYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLESGKPHRLFFNIYGQRK 308
Cdd:PRK15172 241 SLCSDQPWLQIYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLEPGKTHRLFFNIGGQRK 300
|
|
| Aldose_epim_Ec_YihR |
cd09022 |
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ... |
28-303 |
4.65e-130 |
|
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: 371.52 E-value: 4.65e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 28 YHATIVTVGAGLAELTFQGCHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQLPINEHSSKAAIHGLLAWRD 107
Cdd:cd09022 1 YRAVVTEVGAGLRSLTVGGRDLVEPYPADEVPPGAAGQVLAPWPNRIADGRYTFDGVEHQLPITEPERGNAIHGLVRWAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 108 WQISELTATSVTLTAFLPPSYGYPFMLASQVVYSLNAHtGLSVEIASQNIGTVAAPYGVGIHPYLTCNLTSVDEYLFQLP 187
Cdd:cd09022 81 WQLVEHTDSSVTLRTRIPPQPGYPFTLELTVTYELDDD-GLTVTLTATNVGDEPAPFGVGFHPYLSAGGAPLDECTLTLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 188 ANQVYAVDEHANPTTLHHVDELDLNFTQAKKIAATKIDHTFKT----ANDLWEMTITHPQQaLSVSLCSDQL--WVQVYS 261
Cdd:cd09022 160 ADTWLPVDERLLPTGTEPVAGTPYDFRTGRRLGGTALDTAFTDltrdADGRARARLTGPDG-RGVELWADESfpWVQVFT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 49176437 262 GEKL----QRQGLAVEPMSCPPNAFNSGIDLLLLESGKPHRLFFNI 303
Cdd:cd09022 239 ADTLpppgRRRGLAVEPMTCPPNAFNSGTDLIVLAPGETHTASWGI 284
|
|
| GalM |
COG2017 |
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism]; |
17-303 |
2.33e-79 |
|
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
Pssm-ID: 441620 [Multi-domain] Cd Length: 309 Bit Score: 243.26 E-value: 2.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 17 SGQTVSLAAGDYHATIVTVGAGLAELTF---QGCHLVIPHK--PEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQLPIN 91
Cdd:COG2017 6 DGELYTLENGGLRAVIPEYGATLTSLRVpdkDGRDVLLGFDdlEDDPPWAYGGAILGPYANRIADGRFTLDGKTYQLPIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 92 EHssKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVVYSLNAHtGLSVEIASQNIGTVAAPYGVGIHPY 171
Cdd:COG2017 86 EG--PNALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGNLELTVTYTLTDN-GLTITYTATNLGDKPTPFNLGNHPY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 172 LTCNL---TSVDEYLFQLPANQVYAVDEHANPT-TLHHVDELDLNFTQAKKIAATKIDHTFKTAN--DLWEMTITHPQQA 245
Cdd:COG2017 163 FNLPGeggGDIDDHRLQIPADEYLPVDEGLIPTgELAPVAGTPFDFREPRPLGDGGFDHAFVGLDsdGRPAARLTDPDSG 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49176437 246 LSVSLCSDQL-WVQVYSGEKLQ--RQGLAVEPMSCPPNAFNS--GIDLLLLESGKPHRLFFNI 303
Cdd:COG2017 243 RRLEVSTDEFpGLQVYTGNFLDpgRDGVCLEPQTGPPDAPNHpgFEGLIVLAPGETYSATTRI 305
|
|
| Aldose_epim |
pfam01263 |
Aldose 1-epimerase; |
19-304 |
1.66e-59 |
|
Aldose 1-epimerase;
Pssm-ID: 396013 Cd Length: 300 Bit Score: 192.23 E-value: 1.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 19 QTVSLAAGD-YHATIVTVGAGLAELTFQGC--HLVIPHKPEEMPL---AHLGKVLIPWPNRIANGCYRYQGQEYQLPINE 92
Cdd:pfam01263 1 DLITLTNGNgLSATISLYGATLLSLKVPGKlrEVLLGSDDAEGYLkdsNYFGATLGPYANRIANGRFELDGIPYCLPQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 93 HsSKAAIHGLLAWRDWQISELTA---TSVTLTAFLPPSYGYPFMLASQVVYSLNAHTGLSVEIASQNIGTvAAPYGVGIH 169
Cdd:pfam01263 81 P-GKNPLHGGARGRIWEVEEVKPddgVTVTLVLDPDGEEGYPGDLEARVTYTLNEDNELTIEYEATNDGK-PTPFNLGNH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 170 PYLTCNLTsVDEYLFQLPANQVYAVDEHANPTTLH-HVDELDLNFTQAKKIAAT--KIDHTFKTANDLWEMTITHPQQAL 246
Cdd:pfam01263 159 PYFNLSGD-IDIHELQIEADEYLEVDDDLIPTGELkDVKGTPFDFRQPTPIGEDilGYDHVYLLDPLKAVIIDPDPGSGI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49176437 247 SVSLCSDQLWVQVYSG-----EKLQRQGLAVEPMSCPPNAFNSGIDLLLLESGKPHRLFFNIY 304
Cdd:pfam01263 238 VLEVSTTQPGLVVYTPnflkgKYLSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAETSYS 300
|
|
| Aldose_epim |
cd01081 |
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ... |
30-292 |
4.33e-45 |
|
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: 154.54 E-value: 4.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 30 ATIVTVGAGLAELTFQGCHLVI--PHKPEEMPLAHL---GKVLIPWPNRIANGCYRYQGQEYQLPINEHssKAAIHGLLA 104
Cdd:cd01081 3 AVIAPRGANIISLKVKGDVDLLwgYPDAEEYPLAPTgggGAILFPFANRISDGRYTFDGKQYPLNEDEG--GNAIHGFVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 105 WRDWQISELTATSVTLTAFL---PPSYGYPFMLASQVVYSLNAHTgLSVEIASQNIGTVAAPYGVGIHPYLTCNLTSVDE 181
Cdd:cd01081 81 NLPWRVVATDEEEASVTLSYdlnDGPGGYPFPLELTVTYTLDADT-LTITFTVTNLGDEPMPFGLGWHPYFGLPGVAIED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 182 YLFQLPANQVYAVDEHANPTTLHHVDELDLNFTQAkKIAATKIDHTF---KTANDLWEMTITHPQQALSVSLCSDQLWVQ 258
Cdd:cd01081 160 LRLRVPASKVLPLDDLLPPTGELEVPGEEDFRLGR-PLGGGELDDCFlllGNDAGTAEARLEDPDSRISVEFETGWPFWQ 238
|
250 260 270
....*....|....*....|....*....|....*
gi 49176437 259 VYSGEKLQRQGLAVEPMSCPPNAF-NSGIDLLLLE 292
Cdd:cd01081 239 VYTGDGGRRGSVAIEPMTSAPDAFfNNNGGLITLK 273
|
|
| Aldose_epim_Ec_YphB |
cd09021 |
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ... |
29-296 |
1.55e-30 |
|
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: 115.85 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 29 HATIV-TVGAGLAELTFQG--CHLVIPHKPEEM-PLAHLGKVLIPWPNRIANGCYRYQGQEYQLPINEHSSKAAIHGlLA 104
Cdd:cd09021 1 RLVLApELGGSIAALTSRGdpTPLLRPADPDAAdALAMACFPLVPFSNRIRGGRFLFAGREVALPPNTADEPHPLHG-DG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 105 WRD-WQISELTATSVTLTAFLPPSYGyPFMLASQVVYSLNAHtGLSVEIASQNIGTVAAPYGVGIHPYLTCNLTSvdeyL 183
Cdd:cd09021 80 WRRpWQVVAASADSAELQLDHEADDP-PWAYRAEQRFHLAGD-GLSITLSVTNRGDRPMPAGLGFHPYFPRTPDT----R 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 184 FQLPANQVYAVDEHANPTTLHHVDElDLNFTQAKKIAATKIDHTF----KTANDLWemtithPQQALSVSLCSDQL--WV 257
Cdd:cd09021 154 LQADADGVWLEDEDHLPTGLRPHPP-DWDFSQPRPLPDRWIDNCFtgwdGAALIWP------PERGLALTIEADAPfsHL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 49176437 258 QVYSgekLQRQG-LAVEPMSCPPNAFNSGID--LLLLESGKP 296
Cdd:cd09021 227 VVYR---PPGEDfFCLEPVSHAPDAHHGPGDpgLRVLAPGES 265
|
|
| galactose_mutarotase_like |
cd09019 |
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ... |
72-298 |
9.90e-21 |
|
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: 90.26 E-value: 9.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 72 NRIANGCYRYQGQEYQLPINEHssKAAIH-GLLAW--RDWQISELTATSVTLTAFLPPSY-GYPFMLASQVVYSLNAHTG 147
Cdd:cd09019 62 NRIANGRFTLDGKTYQLEANEG--PNHLHgGPKGFdkRVWDVEEVEENSVTFSLVSPDGEeGFPGNLTVTVTYTLTDDNE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 148 LSVEIasqnIGTVAAPYGVGI--HPYLtcNLT-----SVDEYLFQLPANQVYAVDEHANPT-TLHHVDELDLNFTQAKKI 219
Cdd:cd09019 140 LTIEY----EATTDKPTPVNLtnHSYF--NLAgegsgDILDHELQINADRYLPVDEELIPTgEILPVAGTPFDFRKPKPI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 220 AATKI-----------DHTFKTANDLWEM----TITHPQQALSVSLCSDQLWVQVYSGEKL------------QRQGLAV 272
Cdd:cd09019 214 GRIDLddeqlklgggyDHNFVLDKGGGKLrpaaRLTSPESGRKLEVYTTQPGVQFYTGNFLdgtpggggkvygKRSGFCL 293
|
250 260 270
....*....|....*....|....*....|.
gi 49176437 273 EPmSCPPNA-----FNSGIdlllLESGKPHR 298
Cdd:cd09019 294 ET-QHFPDApnhpnFPSII----LRPGETYR 319
|
|
| Aldose_epim_Slr1438 |
cd09025 |
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis ... |
66-303 |
6.20e-17 |
|
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: 78.83 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 66 VLIPWPNRIANGCYRYQGQEYQLPInehsskaaiHGLlAwRD--WQISELTATS-VTLT--------AFlppsygYPFML 134
Cdd:cd09025 56 ILFPICGNLPDDGYPLAGQEYTLKQ---------HGF-A-RDlpWEVELLGDGAgLTLTlrdneatrAV------YPFDF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 135 ASQVVYSLNAHTgLSVEIASQNIGTVAAPYGVGIHPYLTCnlTSVDEYLFQLPAN--QVYAVDEHANPT--TLHHVDELD 210
Cdd:cd09025 119 ELELTYRLAGNT-LEIAQRVHNLGDQPMPFSFGFHPYFAV--PDKAKLSLDLPPTrcFDQKTDEEANTPgqFDETEEGVD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 211 LNFTQAKkiaatkidhtfktandlwEMTITHPQQALSVSLCSDQLW--VQVYSgEKlQRQGLAVEPMSCPPNAFNSGIDL 288
Cdd:cd09025 196 LLFRPLG------------------PASLTDGARGLKITLDHDEPFsnLVVWT-DK-GKDFVCLEPWTGPRNALNTGERL 255
|
250
....*....|....*
gi 49176437 289 LLLESGKPHRLFFNI 303
Cdd:cd09025 256 LLLPPGETEEASVRI 270
|
|
| galM |
PRK11055 |
galactose-1-epimerase; Provisional |
54-280 |
1.90e-09 |
|
galactose-1-epimerase; Provisional
Pssm-ID: 182931 Cd Length: 342 Bit Score: 58.01 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 54 KPEEMP--LAHLGKVLIPWPNRIANGCYRYQGQEYQLPIN--EHSSKAAIHGLLAwRDWQISELTATSVTLTAFLPP-SY 128
Cdd:PRK11055 52 SPEDYPdqAAYLGASVGRYANRIANSRFTLDGETYQLSPNqgGNQLHGGPEGFDK-RRWQIVNQNDRQVTFSLSSPDgDQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 129 GYPFMLASQVVYSLNAHTGLSVEIAsqniGTVAAPYGVGI--HPYLtcNL------TSVDEYLFQLPANQVYAVDEHANP 200
Cdd:PRK11055 131 GFPGNLGATVTYRLTDDNRVSITYR----ATVDKPCPVNLtnHAYF--NLdgaeegSDVRNHKLQINADEYLPVDEGGIP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 201 TT-LHHVDELDLNFTQAKKIA----------ATK-IDHTF---------KTANDLWEmtithPQQALSVSLCSDQLWVQV 259
Cdd:PRK11055 205 NGgLKSVAGTSFDFRQPKTIAqdfladddqqKVKgYDHAFllqakgdgkKPAAHLWS-----PDEKLQMKVYTTAPALQF 279
|
250 260 270
....*....|....*....|....*....|....*
gi 49176437 260 YSGEKL------------QRQGLAVEPMSCP--PN 280
Cdd:PRK11055 280 YSGNFLagtpsrgggpyaDYAGLALESQFLPdsPN 314
|
|
| Aldose_epim_lacX |
cd09024 |
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ... |
66-170 |
5.11e-09 |
|
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: 56.01 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 66 VLIPWPNRIANGCYRYQGQEYQLPinehsskaaIHGLLAWRDWQISELTATSVTLTafLPPS------YGYPFMLasQVV 139
Cdd:cd09024 46 ILFPIVGRLKDDTYTIDGKTYPMP---------QHGFARDMEFEVVEQSDDSVTFE--LTDNeetlkvYPFDFEL--RVT 112
|
90 100 110
....*....|....*....|....*....|.
gi 49176437 140 YSLNAHTgLSVEIASQNIGTVAAPYGVGIHP 170
Cdd:cd09024 113 YTLEGNT-LKVTYEVKNPDDKTMPFSIGGHP 142
|
|
| PLN00194 |
PLN00194 |
aldose 1-epimerase; Provisional |
72-221 |
1.88e-04 |
|
aldose 1-epimerase; Provisional
Pssm-ID: 215098 [Multi-domain] Cd Length: 337 Bit Score: 42.36 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 72 NRIANGCYRYQGQEYQLPINEhsSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSY-------GYPFMLASQVVYSLNA 144
Cdd:PLN00194 71 NRIKGAKFTLNGVTYKLPPNN--GPNSLHGGPKGFSKVVWEVAKYKKGEKPSITFKYhsfdgeeGFPGDLSVTVTYTLLS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176437 145 HTGLSVEIASQNIGTvAAPYGVGIHPYLtcNLT-----SVDEYLFQLPANQVYAVDEHANPT-TLHHVDELDLNFTQAKK 218
Cdd:PLN00194 149 SNTLRLDMEAKPLNK-ATPVNLAQHTYW--NLAghnsgDILSHKIQIFGSHITPVDENLIPTgEILPVKGTPFDFTTPKK 225
|
...
gi 49176437 219 IAA 221
Cdd:PLN00194 226 IGS 228
|
|
| |
