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Conserved domains on  [gi|517395683|ref|WP_018569008|]
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aldose 1-epimerase [Streptomyces sp. PsTaAH-124]

Protein Classification

aldose epimerase family protein( domain architecture ID 52393)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aldose_epim super family cl14648
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
 14-258 2.39e-66

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


The actual alignment was detected with superfamily member cd09021:

Pssm-ID: 449342  Cd Length: 273  Bit Score: 207.15  E-value: 2.39e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  14 EATVRPGHGARIGGLRVGG--LELLRQGD-------RFGCFPMVPWCGRIREGRFRDGATVHQMPLNS--PPHAIHGTAR 82
Cdd:cd09021    1 RLVLAPELGGSIAALTSRGdpTPLLRPADpdaadalAMACFPLVPFSNRIRGGRFLFAGREVALPPNTadEPHPLHGDGW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  83 DGVWKMARVSENEAVLTYDLGEP-WPYPGRITQVVALSEDALTLSMAVETYDSS-FPAQIGWHPWFNRTLDGQdVRLDFT 160
Cdd:cd09021   81 RRPWQVVAASADSAELQLDHEADdPPWAYRAEQRFHLAGDGLSITLSVTNRGDRpMPAGLGFHPYFPRTPDTR-LQADAD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 161 PAWQEERggDHLPTGRRIDP-----------LPGPWDDCFGMPGgvGVTLTWPE----RLELEVTSPEEWVVVYDEQEA- 224
Cdd:cd09021  160 GVWLEDE--DHLPTGLRPHPpdwdfsqprplPDRWIDNCFTGWD--GAALIWPPerglALTIEADAPFSHLVVYRPPGEd 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 517395683 225 AVCVEPQTGPPDGLN----TCPRLVTPLEPLEATTTWS 258
Cdd:cd09021  236 FFCLEPVSHAPDAHHgpgdPGLRVLAPGESLSLSMRIT 273
 
Name Accession Description Interval E-value
Aldose_epim_Ec_YphB cd09021
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ...
 14-258 2.39e-66

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: 207.15  E-value: 2.39e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  14 EATVRPGHGARIGGLRVGG--LELLRQGD-------RFGCFPMVPWCGRIREGRFRDGATVHQMPLNS--PPHAIHGTAR 82
Cdd:cd09021    1 RLVLAPELGGSIAALTSRGdpTPLLRPADpdaadalAMACFPLVPFSNRIRGGRFLFAGREVALPPNTadEPHPLHGDGW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  83 DGVWKMARVSENEAVLTYDLGEP-WPYPGRITQVVALSEDALTLSMAVETYDSS-FPAQIGWHPWFNRTLDGQdVRLDFT 160
Cdd:cd09021   81 RRPWQVVAASADSAELQLDHEADdPPWAYRAEQRFHLAGDGLSITLSVTNRGDRpMPAGLGFHPYFPRTPDTR-LQADAD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 161 PAWQEERggDHLPTGRRIDP-----------LPGPWDDCFGMPGgvGVTLTWPE----RLELEVTSPEEWVVVYDEQEA- 224
Cdd:cd09021  160 GVWLEDE--DHLPTGLRPHPpdwdfsqprplPDRWIDNCFTGWD--GAALIWPPerglALTIEADAPFSHLVVYRPPGEd 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 517395683 225 AVCVEPQTGPPDGLN----TCPRLVTPLEPLEATTTWS 258
Cdd:cd09021  236 FFCLEPVSHAPDAHHgpgdPGLRVLAPGESLSLSMRIT 273
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
6-258 2.36e-49

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


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 164.68  E-value: 2.36e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683   6 ITLTAGDAEATVrPGHGARIGGLRV---GGLELLRQGD--------RFGCFPMVPWCGRIREGRFRDGATVHQMPLNSPP 74
Cdd:COG2017   10 YTLENGGLRAVI-PEYGATLTSLRVpdkDGRDVLLGFDdleddppwAYGGAILGPYANRIADGRFTLDGKTYQLPINEGP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  75 HAIHGTARDGVWKMARVSENEAVLTYDLGEPWPYPG--RITQVVALSEDALTLSMAVETY-DSSFPAQIGWHPWFNRTLD 151
Cdd:COG2017   89 NALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGnlELTVTYTLTDNGLTITYTATNLgDKPTPFNLGNHPYFNLPGE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 152 GQ----DVRLDFTPAWQEERGGDHLPTGRRIDPLPGPW-------------DDCF---GMPGGVGVTLTWPER-LELEV- 209
Cdd:COG2017  169 GGgdidDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFdfreprplgdggfDHAFvglDSDGRPAARLTDPDSgRRLEVs 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517395683 210 TSPEEWVVVY-----DEQEAAVCVEPQTGPPDGLNTCP----RLVTPLEPLEATTTWS 258
Cdd:COG2017  249 TDEFPGLQVYtgnflDPGRDGVCLEPQTGPPDAPNHPGfeglIVLAPGETYSATTRIR 306
Aldose_epim pfam01263
Aldose 1-epimerase;
4-239 7.67e-19

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 83.99  E-value: 7.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683    4 DDITLTAGDAEATVRPGHGARIGGLRVGG--LELLRQGD---------RFGCFPMVPWCGRIREGRFRDGATVHQMPLNS 72
Cdd:pfam01263   1 DLITLTNGNGLSATISLYGATLLSLKVPGklREVLLGSDdaegylkdsNYFGATLGPYANRIANGRFELDGIPYCLPQNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683   73 P-PHAIHGTARDGVWKMARVSENEAV-----LTYDLGEPWPYPGRITQVVALSED-ALTLSMAVETYDSSFPAQIGWHPW 145
Cdd:pfam01263  81 PgKNPLHGGARGRIWEVEEVKPDDGVtvtlvLDPDGEEGYPGDLEARVTYTLNEDnELTIEYEATNDGKPTPFNLGNHPY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  146 FN--RTLDGQDVRLDFTPAWqeERGGDHLPTGRRIDPLPGPW---------------DDCFGMPGGVGVTL--TWPERLE 206
Cdd:pfam01263 161 FNlsGDIDIHELQIEADEYL--EVDDDLIPTGELKDVKGTPFdfrqptpigedilgyDHVYLLDPLKAVIIdpDPGSGIV 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 517395683  207 LEVTSPEEWVVVY---DEQEAAVCVEPQTGPPDGLN 239
Cdd:pfam01263 239 LEVSTTQPGLVVYtpnFLKGKYLSDEGFALETQFLP 274
PRK15172 PRK15172
aldose-1-epimerase;
6-250 1.25e-08

aldose-1-epimerase;


Pssm-ID: 237918  Cd Length: 300  Bit Score: 54.43  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683   6 ITLTAGDAEATVrpghgariggLRVG-GL-ELLRQGdRFGCFP--------------MVPWCGRIREGRFRDGATVHQMP 69
Cdd:PRK15172  13 ISLAAGDYQATI----------VTVGaGLaELTFQG-RHLVIPhkpeemplahlgkvLIPWPNRIANGCYRYQGQEYQLP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  70 LNSPPH--AIHG--TARDgvWKMARVSENEAVLTYDLGEPWPYPGRITQVVALSEDALT-LSMAVETY---DSSFPAQIG 141
Cdd:PRK15172  82 INEHVSkaAIHGllAWRD--WQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATgLSVEIASQnigDVPAPYGVG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 142 WHPWFNRTLDGQDVRLDFTPAWQEERGGDHLPTGRRIDPLPGPWDdcFGMPGGVGVTL------TWPERLELEVTSPEE- 214
Cdd:PRK15172 160 IHPYLTCNLTSVDEYLLQLPANQVLAVDEHANPTTLHHVDELDLD--FSQAKKIAATKidhtfkTANDLWEVRITHPQQa 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 517395683 215 ----------WVVVYDE---QEAAVCVEPQTGPPDGLNTCPRLVTpLEP 250
Cdd:PRK15172 238 lsvslcsdqpWLQIYSGeklQRQGLAVEPMSCPPNAFNSGIDLLL-LEP 285
 
Name Accession Description Interval E-value
Aldose_epim_Ec_YphB cd09021
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ...
 14-258 2.39e-66

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: 207.15  E-value: 2.39e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  14 EATVRPGHGARIGGLRVGG--LELLRQGD-------RFGCFPMVPWCGRIREGRFRDGATVHQMPLNS--PPHAIHGTAR 82
Cdd:cd09021    1 RLVLAPELGGSIAALTSRGdpTPLLRPADpdaadalAMACFPLVPFSNRIRGGRFLFAGREVALPPNTadEPHPLHGDGW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  83 DGVWKMARVSENEAVLTYDLGEP-WPYPGRITQVVALSEDALTLSMAVETYDSS-FPAQIGWHPWFNRTLDGQdVRLDFT 160
Cdd:cd09021   81 RRPWQVVAASADSAELQLDHEADdPPWAYRAEQRFHLAGDGLSITLSVTNRGDRpMPAGLGFHPYFPRTPDTR-LQADAD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 161 PAWQEERggDHLPTGRRIDP-----------LPGPWDDCFGMPGgvGVTLTWPE----RLELEVTSPEEWVVVYDEQEA- 224
Cdd:cd09021  160 GVWLEDE--DHLPTGLRPHPpdwdfsqprplPDRWIDNCFTGWD--GAALIWPPerglALTIEADAPFSHLVVYRPPGEd 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 517395683 225 AVCVEPQTGPPDGLN----TCPRLVTPLEPLEATTTWS 258
Cdd:cd09021  236 FFCLEPVSHAPDAHHgpgdPGLRVLAPGESLSLSMRIT 273
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
6-258 2.36e-49

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


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 164.68  E-value: 2.36e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683   6 ITLTAGDAEATVrPGHGARIGGLRV---GGLELLRQGD--------RFGCFPMVPWCGRIREGRFRDGATVHQMPLNSPP 74
Cdd:COG2017   10 YTLENGGLRAVI-PEYGATLTSLRVpdkDGRDVLLGFDdleddppwAYGGAILGPYANRIADGRFTLDGKTYQLPINEGP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  75 HAIHGTARDGVWKMARVSENEAVLTYDLGEPWPYPG--RITQVVALSEDALTLSMAVETY-DSSFPAQIGWHPWFNRTLD 151
Cdd:COG2017   89 NALHGGARDRPWEVEEQSEDSVTLSLTSPDEEGYPGnlELTVTYTLTDNGLTITYTATNLgDKPTPFNLGNHPYFNLPGE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 152 GQ----DVRLDFTPAWQEERGGDHLPTGRRIDPLPGPW-------------DDCF---GMPGGVGVTLTWPER-LELEV- 209
Cdd:COG2017  169 GGgdidDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFdfreprplgdggfDHAFvglDSDGRPAARLTDPDSgRRLEVs 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517395683 210 TSPEEWVVVY-----DEQEAAVCVEPQTGPPDGLNTCP----RLVTPLEPLEATTTWS 258
Cdd:COG2017  249 TDEFPGLQVYtgnflDPGRDGVCLEPQTGPPDAPNHPGfeglIVLAPGETYSATTRIR 306
Aldose_epim cd01081
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
 13-260 4.24e-32

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: 119.11  E-value: 4.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  13 AEATVrPGHGARIGGLRV-GGLELLRQG----------DRFGCFPMVPWCGRIREGRFRDGATVHQMPLNSPPHAIHGTA 81
Cdd:cd01081    1 AVAVI-APRGANIISLKVkGDVDLLWGYpdaeeyplapTGGGGAILFPFANRISDGRYTFDGKQYPLNEDEGGNAIHGFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  82 RDGVWKMARVSENEA--VLTYDLGEP---WPYPGRITQVVALSEDALTLSMAVE-TYDSSFPAQIGWHPWFN-RTLDGQD 154
Cdd:cd01081   80 RNLPWRVVATDEEEAsvTLSYDLNDGpggYPFPLELTVTYTLDADTLTITFTVTnLGDEPMPFGLGWHPYFGlPGVAIED 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 155 VRLDFTPAWQEERGGDHLPTGRRIDP-----------LPGPWDDCF----GMPGGVGVTLTWPE-RLELEVTSPEEWVVV 218
Cdd:cd01081  160 LRLRVPASKVLPLDDLLPPTGELEVPgeedfrlgrplGGGELDDCFlllgNDAGTAEARLEDPDsRISVEFETGWPFWQV 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517395683 219 Y---DEQEAAVCVEPQTGPPD-------GLNTcprlvtpLEPLEATTTWSWC 260
Cdd:cd01081  240 YtgdGGRRGSVAIEPMTSAPDaffnnngGLIT-------LKPPGETRTFSIT 284
Aldose_epim_Ec_YihR cd09022
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ...
 22-257 1.32e-22

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: 93.79  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  22 GARIGGLRVGGLELLRQGDRFGCFPM------VPWCGRIREGRFRDGATVHQMPLNSP--PHAIHGTARDGVWKMARVSE 93
Cdd:cd09022    9 GAGLRSLTVGGRDLVEPYPADEVPPGaagqvlAPWPNRIADGRYTFDGVEHQLPITEPerGNAIHGLVRWADWQLVEHTD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  94 NEAVLTYDLG--EPWPYPGRITQVVALSEDALTLSMAVE-TYDSSFPAQIGWHPWF---NRTLDGQDVRLDFTpAWQE-- 165
Cdd:cd09022   89 SSVTLRTRIPpqPGYPFTLELTVTYELDDDGLTVTLTATnVGDEPAPFGVGFHPYLsagGAPLDECTLTLPAD-TWLPvd 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 166 ERG---GDHLPTGRRID-----PLPG-PWDDCFG-----MPGGVGVTLTWPERLELEVTSPEE--WVVVY-------DEQ 222
Cdd:cd09022  168 ERLlptGTEPVAGTPYDfrtgrRLGGtALDTAFTdltrdADGRARARLTGPDGRGVELWADESfpWVQVFtadtlppPGR 247

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 517395683 223 EAAVCVEPQTGPPDGLNTCPRLVTpLEPLEA-TTTW 257
Cdd:cd09022  248 RRGLAVEPMTCPPNAFNSGTDLIV-LAPGEThTASW 282
Aldose_epim pfam01263
Aldose 1-epimerase;
4-239 7.67e-19

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 83.99  E-value: 7.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683    4 DDITLTAGDAEATVRPGHGARIGGLRVGG--LELLRQGD---------RFGCFPMVPWCGRIREGRFRDGATVHQMPLNS 72
Cdd:pfam01263   1 DLITLTNGNGLSATISLYGATLLSLKVPGklREVLLGSDdaegylkdsNYFGATLGPYANRIANGRFELDGIPYCLPQNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683   73 P-PHAIHGTARDGVWKMARVSENEAV-----LTYDLGEPWPYPGRITQVVALSED-ALTLSMAVETYDSSFPAQIGWHPW 145
Cdd:pfam01263  81 PgKNPLHGGARGRIWEVEEVKPDDGVtvtlvLDPDGEEGYPGDLEARVTYTLNEDnELTIEYEATNDGKPTPFNLGNHPY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  146 FN--RTLDGQDVRLDFTPAWqeERGGDHLPTGRRIDPLPGPW---------------DDCFGMPGGVGVTL--TWPERLE 206
Cdd:pfam01263 161 FNlsGDIDIHELQIEADEYL--EVDDDLIPTGELKDVKGTPFdfrqptpigedilgyDHVYLLDPLKAVIIdpDPGSGIV 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 517395683  207 LEVTSPEEWVVVY---DEQEAAVCVEPQTGPPDGLN 239
Cdd:pfam01263 239 LEVSTTQPGLVVYtpnFLKGKYLSDEGFALETQFLP 274
Aldose_epim_Slr1438 cd09025
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis ...
 6-262 9.26e-14

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: 69.20  E-value: 9.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683   6 ITLTAGDAEATVR--PGHGARIGGLRVGGLELL-----RQGD-----RFG---CFPMvpwCGRIREGRFRDGATVHQMPl 70
Cdd:cd09025    4 YELSDEEAGSRLRvvPERGGLITRWTVQGRELLyldeeRFADpaksvRGGipiLFPI---CGNLPDDGYPLAGQEYTLK- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  71 nspphaIHGTARDGVWKM------ARV----SENEAVLTYdlgepWPYPGRITQVVALSEDALTLSMAVE-TYDSSFPAQ 139
Cdd:cd09025   80 ------QHGFARDLPWEVellgdgAGLtltlRDNEATRAV-----YPFDFELELTYRLAGNTLEIAQRVHnLGDQPMPFS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 140 IGWHPWFNRTlDGQDVRLDFTPA--WQEERGGDHLPTGRRIDPLPGpWDDCFGMPGGVGVTLTwPERLELEVTSPEEW-- 215
Cdd:cd09025  149 FGFHPYFAVP-DKAKLSLDLPPTrcFDQKTDEEANTPGQFDETEEG-VDLLFRPLGPASLTDG-ARGLKITLDHDEPFsn 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 517395683 216 VVVYDEQ-EAAVCVEPQTGPPDGLNTCPRLVtpLEPLEATTTWsWCRL 262
Cdd:cd09025  226 LVVWTDKgKDFVCLEPWTGPRNALNTGERLL--LLPPGETEEA-SVRI 270
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 49-239 4.39e-09

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: 55.97  E-value: 4.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  49 PWCGRIREGRFR-DGATvHQMPLNSPPHAIHGtARDG----VWKMARVSENEAVLTY-----DLGepwpYPGRITQVV-- 116
Cdd:cd09019   59 RVANRIANGRFTlDGKT-YQLEANEGPNHLHG-GPKGfdkrVWDVEEVEENSVTFSLvspdgEEG----FPGNLTVTVty 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 117 ALSED-ALTLSMAVETyDSSFPAQIGWHPWFN------RTLDGQDVRLD---FTPAWQEerggdHLPTGR---------- 176
Cdd:cd09019  133 TLTDDnELTIEYEATT-DKPTPVNLTNHSYFNlagegsGDILDHELQINadrYLPVDEE-----LIPTGEilpvagtpfd 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 177 --------------RIDPLPGPWDDCFGMPGGVG-----VTLTWPE-RLELEVTSPEEWVVVYD---------------E 221
Cdd:cd09019  207 frkpkpigridlddEQLKLGGGYDHNFVLDKGGGklrpaARLTSPEsGRKLEVYTTQPGVQFYTgnfldgtpggggkvyG 286

                        250
                 ....*....|....*...
gi 517395683 222 QEAAVCVEPQtGPPDGLN 239
Cdd:cd09019  287 KRSGFCLETQ-HFPDAPN 303
PRK15172 PRK15172
aldose-1-epimerase;
6-250 1.25e-08

aldose-1-epimerase;


Pssm-ID: 237918  Cd Length: 300  Bit Score: 54.43  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683   6 ITLTAGDAEATVrpghgariggLRVG-GL-ELLRQGdRFGCFP--------------MVPWCGRIREGRFRDGATVHQMP 69
Cdd:PRK15172  13 ISLAAGDYQATI----------VTVGaGLaELTFQG-RHLVIPhkpeemplahlgkvLIPWPNRIANGCYRYQGQEYQLP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  70 LNSPPH--AIHG--TARDgvWKMARVSENEAVLTYDLGEPWPYPGRITQVVALSEDALT-LSMAVETY---DSSFPAQIG 141
Cdd:PRK15172  82 INEHVSkaAIHGllAWRD--WQISELTATSVTLTAFLPPSYGYPFMLASQVIYSLDAATgLSVEIASQnigDVPAPYGVG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683 142 WHPWFNRTLDGQDVRLDFTPAWQEERGGDHLPTGRRIDPLPGPWDdcFGMPGGVGVTL------TWPERLELEVTSPEE- 214
Cdd:PRK15172 160 IHPYLTCNLTSVDEYLLQLPANQVLAVDEHANPTTLHHVDELDLD--FSQAKKIAATKidhtfkTANDLWEVRITHPQQa 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 517395683 215 ----------WVVVYDE---QEAAVCVEPQTGPPDGLNTCPRLVTpLEP 250
Cdd:PRK15172 238 lsvslcsdqpWLQIYSGeklQRQGLAVEPMSCPPNAFNSGIDLLL-LEP 285
Aldose_epim_lacX cd09024
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ...
 6-167 1.32e-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: 51.39  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683   6 ITLTAGDAEATVRPgHGARIGGLRVG--GLELLRQGDR----------FgcfpmvPWCGRIREGRFRDGATVHQMPlnsp 73
Cdd:cd09024    1 ITLENEFLTVTISE-HGAELTSIKDKktGREYLWQGDPaywgrhapilF------PIVGRLKDDTYTIDGKTYPMP---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  74 phaIHGTARDGVWKMARVSENEAVLTY----DLGEPWPYPGRITQVVALSEDALTLSMAVE-TYDSSFPAQIGWHPWFNR 148
Cdd:cd09024   70 ---QHGFARDMEFEVVEQSDDSVTFELtdneETLKVYPFDFELRVTYTLEGNTLKVTYEVKnPDDKTMPFSIGGHPAFNC 146

                        170       180
                 ....*....|....*....|...
gi 517395683 149 TLDGQ----DVRLDFTPAWQEER 167
Cdd:cd09024  147 PLDEGekfeDYYLEFEPKEELER 169
D-hex-6-P-epi_like cd09020
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces ...
 78-179 1.09e-04

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


Pssm-ID: 185697  Cd Length: 269  Bit Score: 42.60  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  78 HGTARDGVWKMARVSENE--AVLTYDLGEP------WPYPGRITQVVALSEDALTLSMAVETYDS-SFPAQIGWHPWFN- 147
Cdd:cd09020   69 HGFARTRLWELLEVSEDEdgVTVSLELDDTdetraiWPHAFELRLTVTLGFDTLELELTVTNTGDkPFSFTAALHTYFRv 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 517395683 148 --------RTLDGQDVrLDFTPAWQEERGGDHLPTGRRID 179
Cdd:cd09020  149 sdieqvrvEGLEGATY-LDKLTDQREKVQGGAVTFDGEVD 187
PLN00194 PLN00194
aldose 1-epimerase; Provisional
 53-154 1.95e-04

aldose 1-epimerase; Provisional


Pssm-ID: 215098 [Multi-domain]  Cd Length: 337  Bit Score: 41.97  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517395683  53 RIREGRFRDGATVHQMPLNSPPHAIHGTAR---DGVWKMARVSENEA---VLTY---DlGEPwPYPGRITQVVA---LSE 120
Cdd:PLN00194  72 RIKGAKFTLNGVTYKLPPNNGPNSLHGGPKgfsKVVWEVAKYKKGEKpsiTFKYhsfD-GEE-GFPGDLSVTVTytlLSS 149

                         90       100       110
                 ....*....|....*....|....*....|....
gi 517395683 121 DALTLSMAVETYDSSFPAQIGWHPWFNrtLDGQD 154
Cdd:PLN00194 150 NTLRLDMEAKPLNKATPVNLAQHTYWN--LAGHN 181
 
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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