|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15172 |
PRK15172 |
aldose-1-epimerase; |
1-288 |
0e+00 |
|
aldose-1-epimerase;
Pssm-ID: 237918 Cd Length: 300 Bit Score: 532.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 1 MHKSGTTIVLTAGEWQATIVTVGAGLASLTRRQRHVVIPHAPEEMPLAHLGKVLIPWPNRITGGRFTFEGQTLTPAINDR 80
Cdd:PRK15172 6 MHSSGQTISLAAGDYQATIVTVGAGLAELTFQGRHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQLPINEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 81 VGSTAIHGLLAWHNWAIREQSPTHVVLSAFLPPTYGYPFMLMADVTYQLDEAAGLRVRISGSNAGDTPAPYGVGIHPYLT 160
Cdd:PRK15172 86 VSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATGLSVEIASQNIGDVPAPYGVGIHPYLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 161 CNLHDISACELTLPAAQILEIDAAQ----LHPAGDEGLDFRTPRRIADTHIDHTFKAPSSArWEARLAHPT--MSVWLRA 234
Cdd:PRK15172 166 CNLTSVDEYLLQLPANQVLAVDEHAnpttLHHVDELDLDFSQAKKIAATKIDHTFKTANDL-WEVRITHPQqaLSVSLCS 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 495162776 235 EAPWIQVYTGEKLGRVGLAVEPMSCPPNAFNSGIDVVRLAPGETHTLNMDIGGE 288
Cdd:PRK15172 245 DQPWLQIYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLEPGKTHRLFFNIGGQ 298
|
|
| Aldose_epim_Ec_YihR |
cd09022 |
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ... |
15-285 |
1.84e-116 |
|
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: 336.08 E-value: 1.84e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 15 WQATIVTVGAGLASLTRRQRHVVIPHAPEEMPLAHLGKVLIPWPNRITGGRFTFEGQTLTPAINDRVGSTAIHGLLAWHN 94
Cdd:cd09022 1 YRAVVTEVGAGLRSLTVGGRDLVEPYPADEVPPGAAGQVLAPWPNRIADGRYTFDGVEHQLPITEPERGNAIHGLVRWAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 95 WAIREQSPTHVVLSAFLPPTYGYPFMLMADVTYQLDeAAGLRVRISGSNAGDTPAPYGVGIHPYLTCNLHDISACELTLP 174
Cdd:cd09022 81 WQLVEHTDSSVTLRTRIPPQPGYPFTLELTVTYELD-DDGLTVTLTATNVGDEPAPFGVGFHPYLSAGGAPLDECTLTLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 175 AAQILEIDaAQLHPAGDE-----GLDFRTPRRIADTHIDHTFKAP---SSARWEARLAHP---TMSVWLRAEAPWIQVYT 243
Cdd:cd09022 160 ADTWLPVD-ERLLPTGTEpvagtPYDFRTGRRLGGTALDTAFTDLtrdADGRARARLTGPdgrGVELWADESFPWVQVFT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495162776 244 GEKL----GRVGLAVEPMSCPPNAFNSGIDVVRLAPGETHTLNMDI 285
Cdd:cd09022 239 ADTLpppgRRRGLAVEPMTCPPNAFNSGTDLIVLAPGETHTASWGI 284
|
|
| GalM |
COG2017 |
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism]; |
4-285 |
3.85e-82 |
|
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
Pssm-ID: 441620 [Multi-domain] Cd Length: 309 Bit Score: 249.81 E-value: 3.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 4 SGTTIVLTAGEWQATIVTVGAGLASLT---RRQRHVVIPH--APEEMPLAHLGKVLIPWPNRITGGRFTFEGQTLTPAIN 78
Cdd:COG2017 6 DGELYTLENGGLRAVIPEYGATLTSLRvpdKDGRDVLLGFddLEDDPPWAYGGAILGPYANRIADGRFTLDGKTYQLPIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 79 DrvGSTAIHGLLAWHNWAIREQSPTHVVLSAFLPPTYGYPFMLMADVTYQLDEaAGLRVRISGSNAGDTPAPYGVGIHPY 158
Cdd:COG2017 86 E--GPNALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGNLELTVTYTLTD-NGLTITYTATNLGDKPTPFNLGNHPY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 159 LTCNLH---DISACELTLPAAQILEIDA-----AQLHPAGDEGLDFRTPRRIADTHIDHTFK-APSSARWEARLAHP--- 226
Cdd:COG2017 163 FNLPGEgggDIDDHRLQIPADEYLPVDEgliptGELAPVAGTPFDFREPRPLGDGGFDHAFVgLDSDGRPAARLTDPdsg 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495162776 227 -TMSVWLRaEAPWIQVYTGEKL--GRVGLAVEPMSCPPNAFNS--GIDVVRLAPGETHTLNMDI 285
Cdd:COG2017 243 rRLEVSTD-EFPGLQVYTGNFLdpGRDGVCLEPQTGPPDAPNHpgFEGLIVLAPGETYSATTRI 305
|
|
| Aldose_epim |
pfam01263 |
Aldose 1-epimerase; |
7-283 |
2.09e-48 |
|
Aldose 1-epimerase;
Pssm-ID: 396013 Cd Length: 300 Bit Score: 162.95 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 7 TIVLTAGEW-QATIVTVGAGLASLT--RRQRHVVIPHAPEEMPL---AHLGKVLIPWPNRITGGRFTFEGQTLTPAINDR 80
Cdd:pfam01263 2 LITLTNGNGlSATISLYGATLLSLKvpGKLREVLLGSDDAEGYLkdsNYFGATLGPYANRIANGRFELDGIPYCLPQNGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 81 vGSTAIHGLLAWHNWAIREQSPTH---VVLSAFLPPTYGYPFMLMADVTYQLDEAAGLRVRISGSNAGDtPAPYGVGIHP 157
Cdd:pfam01263 82 -GKNPLHGGARGRIWEVEEVKPDDgvtVTLVLDPDGEEGYPGDLEARVTYTLNEDNELTIEYEATNDGK-PTPFNLGNHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 158 YLTCNLhDISACELTLPAAQILEIDAAQLhPAG------DEGLDFRTPRRIADTH--IDHTFKAPsSARWEARLAHPTMS 229
Cdd:pfam01263 160 YFNLSG-DIDIHELQIEADEYLEVDDDLI-PTGelkdvkGTPFDFRQPTPIGEDIlgYDHVYLLD-PLKAVIIDPDPGSG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495162776 230 VWLRAE--APWIQVYTG-----EKLGRVGLAVEPMSCPPNAFNSGIDVVRLAPGETHTLNM 283
Cdd:pfam01263 237 IVLEVSttQPGLVVYTPnflkgKYLSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAET 297
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15172 |
PRK15172 |
aldose-1-epimerase; |
1-288 |
0e+00 |
|
aldose-1-epimerase;
Pssm-ID: 237918 Cd Length: 300 Bit Score: 532.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 1 MHKSGTTIVLTAGEWQATIVTVGAGLASLTRRQRHVVIPHAPEEMPLAHLGKVLIPWPNRITGGRFTFEGQTLTPAINDR 80
Cdd:PRK15172 6 MHSSGQTISLAAGDYQATIVTVGAGLAELTFQGRHLVIPHKPEEMPLAHLGKVLIPWPNRIANGCYRYQGQEYQLPINEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 81 VGSTAIHGLLAWHNWAIREQSPTHVVLSAFLPPTYGYPFMLMADVTYQLDEAAGLRVRISGSNAGDTPAPYGVGIHPYLT 160
Cdd:PRK15172 86 VSKAAIHGLLAWRDWQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATGLSVEIASQNIGDVPAPYGVGIHPYLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 161 CNLHDISACELTLPAAQILEIDAAQ----LHPAGDEGLDFRTPRRIADTHIDHTFKAPSSArWEARLAHPT--MSVWLRA 234
Cdd:PRK15172 166 CNLTSVDEYLLQLPANQVLAVDEHAnpttLHHVDELDLDFSQAKKIAATKIDHTFKTANDL-WEVRITHPQqaLSVSLCS 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 495162776 235 EAPWIQVYTGEKLGRVGLAVEPMSCPPNAFNSGIDVVRLAPGETHTLNMDIGGE 288
Cdd:PRK15172 245 DQPWLQIYSGEKLQRQGLAVEPMSCPPNAFNSGIDLLLLEPGKTHRLFFNIGGQ 298
|
|
| Aldose_epim_Ec_YihR |
cd09022 |
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ... |
15-285 |
1.84e-116 |
|
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: 336.08 E-value: 1.84e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 15 WQATIVTVGAGLASLTRRQRHVVIPHAPEEMPLAHLGKVLIPWPNRITGGRFTFEGQTLTPAINDRVGSTAIHGLLAWHN 94
Cdd:cd09022 1 YRAVVTEVGAGLRSLTVGGRDLVEPYPADEVPPGAAGQVLAPWPNRIADGRYTFDGVEHQLPITEPERGNAIHGLVRWAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 95 WAIREQSPTHVVLSAFLPPTYGYPFMLMADVTYQLDeAAGLRVRISGSNAGDTPAPYGVGIHPYLTCNLHDISACELTLP 174
Cdd:cd09022 81 WQLVEHTDSSVTLRTRIPPQPGYPFTLELTVTYELD-DDGLTVTLTATNVGDEPAPFGVGFHPYLSAGGAPLDECTLTLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 175 AAQILEIDaAQLHPAGDE-----GLDFRTPRRIADTHIDHTFKAP---SSARWEARLAHP---TMSVWLRAEAPWIQVYT 243
Cdd:cd09022 160 ADTWLPVD-ERLLPTGTEpvagtPYDFRTGRRLGGTALDTAFTDLtrdADGRARARLTGPdgrGVELWADESFPWVQVFT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495162776 244 GEKL----GRVGLAVEPMSCPPNAFNSGIDVVRLAPGETHTLNMDI 285
Cdd:cd09022 239 ADTLpppgRRRGLAVEPMTCPPNAFNSGTDLIVLAPGETHTASWGI 284
|
|
| GalM |
COG2017 |
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism]; |
4-285 |
3.85e-82 |
|
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
Pssm-ID: 441620 [Multi-domain] Cd Length: 309 Bit Score: 249.81 E-value: 3.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 4 SGTTIVLTAGEWQATIVTVGAGLASLT---RRQRHVVIPH--APEEMPLAHLGKVLIPWPNRITGGRFTFEGQTLTPAIN 78
Cdd:COG2017 6 DGELYTLENGGLRAVIPEYGATLTSLRvpdKDGRDVLLGFddLEDDPPWAYGGAILGPYANRIADGRFTLDGKTYQLPIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 79 DrvGSTAIHGLLAWHNWAIREQSPTHVVLSAFLPPTYGYPFMLMADVTYQLDEaAGLRVRISGSNAGDTPAPYGVGIHPY 158
Cdd:COG2017 86 E--GPNALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGNLELTVTYTLTD-NGLTITYTATNLGDKPTPFNLGNHPY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 159 LTCNLH---DISACELTLPAAQILEIDA-----AQLHPAGDEGLDFRTPRRIADTHIDHTFK-APSSARWEARLAHP--- 226
Cdd:COG2017 163 FNLPGEgggDIDDHRLQIPADEYLPVDEgliptGELAPVAGTPFDFREPRPLGDGGFDHAFVgLDSDGRPAARLTDPdsg 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495162776 227 -TMSVWLRaEAPWIQVYTGEKL--GRVGLAVEPMSCPPNAFNS--GIDVVRLAPGETHTLNMDI 285
Cdd:COG2017 243 rRLEVSTD-EFPGLQVYTGNFLdpGRDGVCLEPQTGPPDAPNHpgFEGLIVLAPGETYSATTRI 305
|
|
| Aldose_epim |
pfam01263 |
Aldose 1-epimerase; |
7-283 |
2.09e-48 |
|
Aldose 1-epimerase;
Pssm-ID: 396013 Cd Length: 300 Bit Score: 162.95 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 7 TIVLTAGEW-QATIVTVGAGLASLT--RRQRHVVIPHAPEEMPL---AHLGKVLIPWPNRITGGRFTFEGQTLTPAINDR 80
Cdd:pfam01263 2 LITLTNGNGlSATISLYGATLLSLKvpGKLREVLLGSDDAEGYLkdsNYFGATLGPYANRIANGRFELDGIPYCLPQNGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 81 vGSTAIHGLLAWHNWAIREQSPTH---VVLSAFLPPTYGYPFMLMADVTYQLDEAAGLRVRISGSNAGDtPAPYGVGIHP 157
Cdd:pfam01263 82 -GKNPLHGGARGRIWEVEEVKPDDgvtVTLVLDPDGEEGYPGDLEARVTYTLNEDNELTIEYEATNDGK-PTPFNLGNHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 158 YLTCNLhDISACELTLPAAQILEIDAAQLhPAG------DEGLDFRTPRRIADTH--IDHTFKAPsSARWEARLAHPTMS 229
Cdd:pfam01263 160 YFNLSG-DIDIHELQIEADEYLEVDDDLI-PTGelkdvkGTPFDFRQPTPIGEDIlgYDHVYLLD-PLKAVIIDPDPGSG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495162776 230 VWLRAE--APWIQVYTG-----EKLGRVGLAVEPMSCPPNAFNSGIDVVRLAPGETHTLNM 283
Cdd:pfam01263 237 IVLEVSttQPGLVVYTPnflkgKYLSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAET 297
|
|
| Aldose_epim |
cd01081 |
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ... |
16-283 |
8.74e-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: 155.70 E-value: 8.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 16 QATIVTVGAGLASLTRRQRHVVI--PHAPEEMPLAHL---GKVLIPWPNRITGGRFTFEGQTLTPAiNDRVGStAIHGLL 90
Cdd:cd01081 2 VAVIAPRGANIISLKVKGDVDLLwgYPDAEEYPLAPTgggGAILFPFANRISDGRYTFDGKQYPLN-EDEGGN-AIHGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 91 AWHNWAIREQSPTH--VVLSAFLP-PTYGYPFMLMADVTYQLDeAAGLRVRISGSNAGDTPAPYGVGIHPYLTCNLHDIS 167
Cdd:cd01081 80 RNLPWRVVATDEEEasVTLSYDLNdGPGGYPFPLELTVTYTLD-ADTLTITFTVTNLGDEPMPFGLGWHPYFGLPGVAIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 168 ACELTLPAAQILEIDAAQLHP---AGDEGLDFRTPRRIADTHIDHTF--KAPSSARWEARLAHPTM--SVWLRAEAPWIQ 240
Cdd:cd01081 159 DLRLRVPASKVLPLDDLLPPTgelEVPGEEDFRLGRPLGGGELDDCFllLGNDAGTAEARLEDPDSriSVEFETGWPFWQ 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495162776 241 VYTGEKLGRVGLAVEPMSCPPNAF-NSGIDVVRLA-PGETHTLNM 283
Cdd:cd01081 239 VYTGDGGRRGSVAIEPMTSAPDAFfNNNGGLITLKpPGETRTFSI 283
|
|
| Aldose_epim_Ec_YphB |
cd09021 |
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ... |
22-278 |
5.27e-31 |
|
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: 116.62 E-value: 5.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 22 VGAGLASLTRR--QRHVVIPHAPEEM-PLAHLGKVLIPWPNRITGGRFTFEGQTLTPAINDRVGSTAIHGlLAW-HNWAI 97
Cdd:cd09021 8 LGGSIAALTSRgdPTPLLRPADPDAAdALAMACFPLVPFSNRIRGGRFLFAGREVALPPNTADEPHPLHG-DGWrRPWQV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 98 REQSPTHVVLSAFLPPTYGyPFMLMADVTYQLDEaAGLRVRISGSNAGDTPAPYGVGIHPYLTCNLHDisacELTLPAAQ 177
Cdd:cd09021 87 VAASADSAELQLDHEADDP-PWAYRAEQRFHLAG-DGLSITLSVTNRGDRPMPAGLGFHPYFPRTPDT----RLQADADG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 178 ILEIDAAQL---HPAGDEGLDFRTPRRIADTHIDHTFKAPSSArweARLAHPTMSVWLRAEA----PWIQVYT--GEKLg 248
Cdd:cd09021 161 VWLEDEDHLptgLRPHPPDWDFSQPRPLPDRWIDNCFTGWDGA---ALIWPPERGLALTIEAdapfSHLVVYRppGEDF- 236
|
250 260 270
....*....|....*....|....*....|..
gi 495162776 249 rvgLAVEPMSCPPNAFNSGIDV--VRLAPGET 278
Cdd:cd09021 237 ---FCLEPVSHAPDAHHGPGDPglRVLAPGES 265
|
|
| galactose_mutarotase_like |
cd09019 |
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ... |
59-280 |
2.74e-24 |
|
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: 99.89 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 59 NRITGGRFTFEGQTLTPAINDrvGSTAIH-GLLAWH--NWAIREQSPTHVVLSAFLPPTY-GYPFMLMADVTYQLDEAAG 134
Cdd:cd09019 62 NRIANGRFTLDGKTYQLEANE--GPNHLHgGPKGFDkrVWDVEEVEENSVTFSLVSPDGEeGFPGNLTVTVTYTLTDDNE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 135 LRVRISGSNAGDTPapygVGI--HPYLtcNL-----HDISACELTLPAAQILEIDAAQLhPAG------DEGLDFRTPRR 201
Cdd:cd09019 140 LTIEYEATTDKPTP----VNLtnHSYF--NLagegsGDILDHELQINADRYLPVDEELI-PTGeilpvaGTPFDFRKPKP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 202 IADTHI-----------DHTF---KAPSSARWEARLAHP----TMSVWlrAEAPWIQVYTGEKLG------------RVG 251
Cdd:cd09019 213 IGRIDLddeqlklgggyDHNFvldKGGGKLRPAARLTSPesgrKLEVY--TTQPGVQFYTGNFLDgtpggggkvygkRSG 290
|
250 260 270
....*....|....*....|....*....|....
gi 495162776 252 LAVEPmSCPPNA-----FNSgidvVRLAPGETHT 280
Cdd:cd09019 291 FCLET-QHFPDApnhpnFPS----IILRPGETYR 319
|
|
| Aldose_epim_Slr1438 |
cd09025 |
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis ... |
116-281 |
3.45e-13 |
|
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: 68.04 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 116 GYPFMLMADVTYQLdEAAGLRVRISGSNAGDTPAPYGVGIHPYLTCNlhDISACELTLPAAQILEIDAAQLHPAGDEgLD 195
Cdd:cd09025 113 VYPFDFELELTYRL-AGNTLEIAQRVHNLGDQPMPFSFGFHPYFAVP--DKAKLSLDLPPTRCFDQKTDEEANTPGQ-FD 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 196 FRTPRriadthIDHTFKAPSSARweARLAHPTMSVWLRAEAPW--IQVYTgEKlGRVGLAVEPMSCPPNAFNSGIDVVRL 273
Cdd:cd09025 189 ETEEG------VDLLFRPLGPAS--LTDGARGLKITLDHDEPFsnLVVWT-DK-GKDFVCLEPWTGPRNALNTGERLLLL 258
|
....*...
gi 495162776 274 APGETHTL 281
Cdd:cd09025 259 PPGETEEA 266
|
|
| galM |
PRK11055 |
galactose-1-epimerase; Provisional |
48-278 |
3.23e-11 |
|
galactose-1-epimerase; Provisional
Pssm-ID: 182931 Cd Length: 342 Bit Score: 63.02 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 48 AHLGKVLIPWPNRITGGRFTFEGQTLTPAINDrvGSTAIH-GLLAWHN--WAIREQSPTHVVLSAFLPP-TYGYPFMLMA 123
Cdd:PRK11055 61 AYLGASVGRYANRIANSRFTLDGETYQLSPNQ--GGNQLHgGPEGFDKrrWQIVNQNDRQVTFSLSSPDgDQGFPGNLGA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 124 DVTYQLDEAAglRVRISGSNAGDTPAPYGVGIHPYLtcNL------HDISACELTLPAAQILEIDA-----AQLHPAGDE 192
Cdd:PRK11055 139 TVTYRLTDDN--RVSITYRATVDKPCPVNLTNHAYF--NLdgaeegSDVRNHKLQINADEYLPVDEggipnGGLKSVAGT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 193 GLDFRTPRRIADTHI-----------DHTFKAPSSARWEARLAHPT-------MSVwlRAEAPWIQVYTGEKLGRV---- 250
Cdd:PRK11055 215 SFDFRQPKTIAQDFLadddqqkvkgyDHAFLLQAKGDGKKPAAHLWspdeklqMKV--YTTAPALQFYSGNFLAGTpsrg 292
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 495162776 251 --------GLAVEPMSCP--PN----AFNSGIdvvrLAPGET 278
Cdd:PRK11055 293 ggpyadyaGLALESQFLPdsPNhpewPQPDCI----LKPGEE 330
|
|
| Aldose_epim_lacX |
cd09024 |
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ... |
17-157 |
8.57e-07 |
|
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: 49.47 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 17 ATIVTVGAGLASLTRRQRHVVI-----P-----HAPeemplahlgkVLIPWPNRITGGRFTFEGQTltpaindrvGSTAI 86
Cdd:cd09024 10 VTISEHGAELTSIKDKKTGREYlwqgdPaywgrHAP----------ILFPIVGRLKDDTYTIDGKT---------YPMPQ 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495162776 87 HGLLAWHNWAIREQSPTHVVLSafLPPT------YGYPFMLmaDVTYQLDEAaGLRVRISGSNAGDTPAPYGVGIHP 157
Cdd:cd09024 71 HGFARDMEFEVVEQSDDSVTFE--LTDNeetlkvYPFDFEL--RVTYTLEGN-TLKVTYEVKNPDDKTMPFSIGGHP 142
|
|
| PLN00194 |
PLN00194 |
aldose 1-epimerase; Provisional |
59-250 |
2.87e-06 |
|
aldose 1-epimerase; Provisional
Pssm-ID: 215098 [Multi-domain] Cd Length: 337 Bit Score: 47.75 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 59 NRITGGRFTFEGQTLTPAINDrvGSTAIHGLLAWHN---WAIREQSPTHVVLSAFlppTY-------GYPFMLMADVTYQ 128
Cdd:PLN00194 71 NRIKGAKFTLNGVTYKLPPNN--GPNSLHGGPKGFSkvvWEVAKYKKGEKPSITF---KYhsfdgeeGFPGDLSVTVTYT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495162776 129 LDEAAGLRVRISGSnAGDTPAPYGVGIHPYLTCNLH---DISACELTLPAAQILEIDaAQLHPAGD----EG--LDFRTP 199
Cdd:PLN00194 146 LLSSNTLRLDMEAK-PLNKATPVNLAQHTYWNLAGHnsgDILSHKIQIFGSHITPVD-ENLIPTGEilpvKGtpFDFTTP 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495162776 200 RRI--------------------ADTHIDHT--FKAPSSARwearlahpTMSVWlrAEAPWIQVYTGEKLGRV 250
Cdd:PLN00194 224 KKIgsrinelpkgydhnyvldgeEKEGLKKAakVKDPKSGR--------VLELW--TNAPGMQFYTSNYVNGV 286
|
|
| |
