|
Name |
Accession |
Description |
Interval |
E-value |
| galM |
PRK11055 |
galactose-1-epimerase; Provisional |
7-345 |
0e+00 |
|
galactose-1-epimerase; Provisional
Pssm-ID: 182931 Cd Length: 342 Bit Score: 702.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 7 ALAPDGQPYRLLTLRNNAGMVVTLMDWGATLLSARIPLSDGSVREALLGCASPECYQDQAAFLGASIGRYANRIANSRYT 86
Cdd:PRK11055 1 ALAPDGQPYRLLTLRNNAGMVVTLMDWGATWLSCRVPLSDGSVREVLLGCASPEDYPDQAAYLGASVGRYANRIANSRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 87 FDGETVTLSPSQGVNQLHGGPEGFDKRRWQIVNQNDRQVLFALSSDDGDQGFPGNLGATVQYRLTDDNRISITYRATVDK 166
Cdd:PRK11055 81 LDGETYQLSPNQGGNQLHGGPEGFDKRRWQIVNQNDRQVTFSLSSPDGDQGFPGNLGATVTYRLTDDNRVSITYRATVDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 167 PCPVNMTNHVYFNLDG--EQSDVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFLADDDQRKVKGY 244
Cdd:PRK11055 161 PCPVNLTNHAYFNLDGaeEGSDVRNHKLQINADEYLPVDEGGIPNGGLKSVAGTSFDFRQPKTIAQDFLADDDQQKVKGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 245 DHAFLLQAKGDGKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGTPSRGTEPYADWQGLALESEFLPDSPNHPEWPQ 324
Cdd:PRK11055 241 DHAFLLQAKGDGKKPAAHLWSPDEKLQMKVYTTAPALQFYSGNFLAGTPSRGGGPYADYAGLALESQFLPDSPNHPEWPQ 320
|
330 340
....*....|....*....|.
gi 1230355636 325 PDCFLRPGEEYSSLTEYQFIA 345
Cdd:PRK11055 321 PDCILKPGEEYRSLTEYQFIA 341
|
|
| galM_Leloir |
TIGR02636 |
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ... |
12-344 |
0e+00 |
|
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose 1-epimerase) and participate in the Leloir pathway for galactose/glucose interconversion. All members of the seed alignment for this model are found in gene clusters with other enzymes of the Leloir pathway. This enzyme family belongs to the aldose 1-epimerase family, described by pfam01263. However, the enzyme described as aldose 1-epimerase itself (EC 5.1.3.3) is called broadly specific for D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. The restricted genome context for genes in this family suggests members should act primarily on D-galactose.
Pssm-ID: 274240 Cd Length: 336 Bit Score: 568.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 12 GQPYRLLTLRNNAGMVVTLMDWGATLLSARIPLSDGSvREALLGCASPECYQDQAAFLGASIGRYANRIANSRYTFDGET 91
Cdd:TIGR02636 1 GQPAQLITLTNKNGMTISFMDIGATWLSCQVPLAGEL-REVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 92 VTLSPSQGVNQLHGGPEGFDKRRWQIV--NQNDRQVLFALSSDDGDQGFPGNLGATVQYRLTDDNRISITYRATVDKPCP 169
Cdd:TIGR02636 80 YQLSINQGPNCLHGGPEGFDKRRWTIEtlEQAEVQVKFSLESPDGDQGFPGNLTVSVTYTLTDDNELKIDYEATTDKATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 170 VNMTNHVYFNLDGE--QSDVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFLADDDQRKVKGYDHA 247
Cdd:TIGR02636 160 FNLTNHVYFNLDGAdaGSDVLNHELQLNADRYLPLDEEGIPLGQLKPVDGTSFDFRKEKAIGQDFLANDQQQLAKGYDHA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 248 FLLQAKGDGKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGTPSRGTEPYADWQGLALESEFLPDSPNHPEWPQPDC 327
Cdd:TIGR02636 240 FLLNGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGNFLAGTPNRGGKKYVDHAGIALETQFLPDSPNHPEWGDISC 319
|
330
....*....|....*..
gi 1230355636 328 FLRPGEEYSSLTEYQFI 344
Cdd:TIGR02636 320 ILSPGQEYQHQTRYQFI 336
|
|
| galactose_mutarotase_like |
cd09019 |
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ... |
17-343 |
4.93e-160 |
|
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: 450.42 E-value: 4.93e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 17 LLTLRNNAGMVVTLMDWGATLLSARIPLSDGSVREALLGCASPECYQDQAAFLGASIGRYANRIANSRYTFDGETVTLSP 96
Cdd:cd09019 1 LYTLTNGNGLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 97 SQGVNQLHGGPEGFDKRRWQIVNQNDRQVLFALSSDDGDQGFPGNLGATVQYRLTDDNRISITYRATVDKPCPVNMTNHV 176
Cdd:cd09019 81 NEGPNHLHGGPKGFDKRVWDVEEVEENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNELTIEYEATTDKPTPVNLTNHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 177 YFNLDGEQS-DVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFLADDDQRKVKGYDHAFLLQAKGD 255
Cdd:cd09019 161 YFNLAGEGSgDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIGRIDLDDEQLKLGGGYDHNFVLDKGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 256 GKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGTPSRGTEPYADWQGLALESEFLPDSPNHPEWpqPDCFLRPGEEY 335
Cdd:cd09019 241 KLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTPGGGGKVYGKRSGFCLETQHFPDAPNHPNF--PSIILRPGETY 318
|
....*...
gi 1230355636 336 SSLTEYQF 343
Cdd:cd09019 319 RHTTVYRF 326
|
|
| GalM |
COG2017 |
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism]; |
10-345 |
1.36e-104 |
|
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
Pssm-ID: 441620 [Multi-domain] Cd Length: 309 Bit Score: 309.13 E-value: 1.36e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 10 PDGQPYRLltlrNNAGMVVTLMDWGATLLSARIPLSDGsvREALLGCASPECyQDQAAFLGASIGRYANRIANSRYTFDG 89
Cdd:COG2017 5 PDGELYTL----ENGGLRAVIPEYGATLTSLRVPDKDG--RDVLLGFDDLED-DPPWAYGGAILGPYANRIADGRFTLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 90 ETVTLSPSQGVNQLHGgpeGFDKRRWQIVNQNDRQVLFALSSDDgDQGFPGNLGATVQYRLTdDNRISITYRATV--DKP 167
Cdd:COG2017 78 KTYQLPINEGPNALHG---GARDRPWEVEEQSEDSVTLSLTSPD-EEGYPGNLELTVTYTLT-DNGLTITYTATNlgDKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 168 CPVNMTNHVYFNLDGEQS-DVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASefladddqrkvKGYDH 246
Cdd:COG2017 153 TPFNLGNHPYFNLPGEGGgDIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFREPRPLGD-----------GGFDH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 247 AFL-LQAKGdgkKVAAHVWSADEKLQLKVYTTA-PALQFYSGNFLGGTPSrgtepyadwqGLALESEFLP-DSPNHPEWP 323
Cdd:COG2017 222 AFVgLDSDG---RPAARLTDPDSGRRLEVSTDEfPGLQVYTGNFLDPGRD----------GVCLEPQTGPpDAPNHPGFE 288
|
330 340
....*....|....*....|..
gi 1230355636 324 qPDCFLRPGEEYSSLTEYQFIA 345
Cdd:COG2017 289 -GLIVLAPGETYSATTRIRFSV 309
|
|
| Aldose_epim |
pfam01263 |
Aldose 1-epimerase; |
16-342 |
1.25e-102 |
|
Aldose 1-epimerase;
Pssm-ID: 396013 Cd Length: 300 Bit Score: 303.93 E-value: 1.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 16 RLLTLRNNAGMVVTLMDWGATLLSARIPlsdGSVREALLGCASPECYQDQAAFLGASIGRYANRIANSRYTFDGETVTLS 95
Cdd:pfam01263 1 DLITLTNGNGLSATISLYGATLLSLKVP---GKLREVLLGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 96 PSQ-GVNQLHGGPEGfdkRRWQIV-NQNDRQVLFALSSD-DGDQGFPGNLGATVQYRLTDDNRISITYRAT-VDKPCPVN 171
Cdd:pfam01263 78 QNGpGKNPLHGGARG---RIWEVEeVKPDDGVTVTLVLDpDGEEGYPGDLEARVTYTLNEDNELTIEYEATnDGKPTPFN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 172 MTNHVYFNLDGeqsDVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIAsefladddqRKVKGYDHAFLLq 251
Cdd:pfam01263 155 LGNHPYFNLSG---DIDIHELQIEADEYLEVDDDLIPTGELKDVKGTPFDFRQPTPIG---------EDILGYDHVYLL- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 252 akgDGKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGtpsrgtePYADWQGLALESEFLPDSPNHPEWpqPDCFLRP 331
Cdd:pfam01263 222 ---DPLKAVIIDPDPGSGIVLEVSTTQPGLVVYTPNFLKG-------KYLSDEGFALETQFLPDEPNHPEF--PSIILKP 289
|
330
....*....|.
gi 1230355636 332 GEEYSSLTEYQ 342
Cdd:pfam01263 290 GESYTAETSYS 300
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| galM |
PRK11055 |
galactose-1-epimerase; Provisional |
7-345 |
0e+00 |
|
galactose-1-epimerase; Provisional
Pssm-ID: 182931 Cd Length: 342 Bit Score: 702.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 7 ALAPDGQPYRLLTLRNNAGMVVTLMDWGATLLSARIPLSDGSVREALLGCASPECYQDQAAFLGASIGRYANRIANSRYT 86
Cdd:PRK11055 1 ALAPDGQPYRLLTLRNNAGMVVTLMDWGATWLSCRVPLSDGSVREVLLGCASPEDYPDQAAYLGASVGRYANRIANSRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 87 FDGETVTLSPSQGVNQLHGGPEGFDKRRWQIVNQNDRQVLFALSSDDGDQGFPGNLGATVQYRLTDDNRISITYRATVDK 166
Cdd:PRK11055 81 LDGETYQLSPNQGGNQLHGGPEGFDKRRWQIVNQNDRQVTFSLSSPDGDQGFPGNLGATVTYRLTDDNRVSITYRATVDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 167 PCPVNMTNHVYFNLDG--EQSDVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFLADDDQRKVKGY 244
Cdd:PRK11055 161 PCPVNLTNHAYFNLDGaeEGSDVRNHKLQINADEYLPVDEGGIPNGGLKSVAGTSFDFRQPKTIAQDFLADDDQQKVKGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 245 DHAFLLQAKGDGKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGTPSRGTEPYADWQGLALESEFLPDSPNHPEWPQ 324
Cdd:PRK11055 241 DHAFLLQAKGDGKKPAAHLWSPDEKLQMKVYTTAPALQFYSGNFLAGTPSRGGGPYADYAGLALESQFLPDSPNHPEWPQ 320
|
330 340
....*....|....*....|.
gi 1230355636 325 PDCFLRPGEEYSSLTEYQFIA 345
Cdd:PRK11055 321 PDCILKPGEEYRSLTEYQFIA 341
|
|
| galM_Leloir |
TIGR02636 |
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ... |
12-344 |
0e+00 |
|
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose 1-epimerase) and participate in the Leloir pathway for galactose/glucose interconversion. All members of the seed alignment for this model are found in gene clusters with other enzymes of the Leloir pathway. This enzyme family belongs to the aldose 1-epimerase family, described by pfam01263. However, the enzyme described as aldose 1-epimerase itself (EC 5.1.3.3) is called broadly specific for D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. The restricted genome context for genes in this family suggests members should act primarily on D-galactose.
Pssm-ID: 274240 Cd Length: 336 Bit Score: 568.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 12 GQPYRLLTLRNNAGMVVTLMDWGATLLSARIPLSDGSvREALLGCASPECYQDQAAFLGASIGRYANRIANSRYTFDGET 91
Cdd:TIGR02636 1 GQPAQLITLTNKNGMTISFMDIGATWLSCQVPLAGEL-REVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 92 VTLSPSQGVNQLHGGPEGFDKRRWQIV--NQNDRQVLFALSSDDGDQGFPGNLGATVQYRLTDDNRISITYRATVDKPCP 169
Cdd:TIGR02636 80 YQLSINQGPNCLHGGPEGFDKRRWTIEtlEQAEVQVKFSLESPDGDQGFPGNLTVSVTYTLTDDNELKIDYEATTDKATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 170 VNMTNHVYFNLDGE--QSDVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFLADDDQRKVKGYDHA 247
Cdd:TIGR02636 160 FNLTNHVYFNLDGAdaGSDVLNHELQLNADRYLPLDEEGIPLGQLKPVDGTSFDFRKEKAIGQDFLANDQQQLAKGYDHA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 248 FLLQAKGDGKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGTPSRGTEPYADWQGLALESEFLPDSPNHPEWPQPDC 327
Cdd:TIGR02636 240 FLLNGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGNFLAGTPNRGGKKYVDHAGIALETQFLPDSPNHPEWGDISC 319
|
330
....*....|....*..
gi 1230355636 328 FLRPGEEYSSLTEYQFI 344
Cdd:TIGR02636 320 ILSPGQEYQHQTRYQFI 336
|
|
| galactose_mutarotase_like |
cd09019 |
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ... |
17-343 |
4.93e-160 |
|
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: 450.42 E-value: 4.93e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 17 LLTLRNNAGMVVTLMDWGATLLSARIPLSDGSVREALLGCASPECYQDQAAFLGASIGRYANRIANSRYTFDGETVTLSP 96
Cdd:cd09019 1 LYTLTNGNGLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 97 SQGVNQLHGGPEGFDKRRWQIVNQNDRQVLFALSSDDGDQGFPGNLGATVQYRLTDDNRISITYRATVDKPCPVNMTNHV 176
Cdd:cd09019 81 NEGPNHLHGGPKGFDKRVWDVEEVEENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNELTIEYEATTDKPTPVNLTNHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 177 YFNLDGEQS-DVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFLADDDQRKVKGYDHAFLLQAKGD 255
Cdd:cd09019 161 YFNLAGEGSgDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIGRIDLDDEQLKLGGGYDHNFVLDKGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 256 GKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGTPSRGTEPYADWQGLALESEFLPDSPNHPEWpqPDCFLRPGEEY 335
Cdd:cd09019 241 KLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTPGGGGKVYGKRSGFCLETQHFPDAPNHPNF--PSIILRPGETY 318
|
....*...
gi 1230355636 336 SSLTEYQF 343
Cdd:cd09019 319 RHTTVYRF 326
|
|
| GalM |
COG2017 |
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism]; |
10-345 |
1.36e-104 |
|
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
Pssm-ID: 441620 [Multi-domain] Cd Length: 309 Bit Score: 309.13 E-value: 1.36e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 10 PDGQPYRLltlrNNAGMVVTLMDWGATLLSARIPLSDGsvREALLGCASPECyQDQAAFLGASIGRYANRIANSRYTFDG 89
Cdd:COG2017 5 PDGELYTL----ENGGLRAVIPEYGATLTSLRVPDKDG--RDVLLGFDDLED-DPPWAYGGAILGPYANRIADGRFTLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 90 ETVTLSPSQGVNQLHGgpeGFDKRRWQIVNQNDRQVLFALSSDDgDQGFPGNLGATVQYRLTdDNRISITYRATV--DKP 167
Cdd:COG2017 78 KTYQLPINEGPNALHG---GARDRPWEVEEQSEDSVTLSLTSPD-EEGYPGNLELTVTYTLT-DNGLTITYTATNlgDKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 168 CPVNMTNHVYFNLDGEQS-DVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASefladddqrkvKGYDH 246
Cdd:COG2017 153 TPFNLGNHPYFNLPGEGGgDIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFREPRPLGD-----------GGFDH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 247 AFL-LQAKGdgkKVAAHVWSADEKLQLKVYTTA-PALQFYSGNFLGGTPSrgtepyadwqGLALESEFLP-DSPNHPEWP 323
Cdd:COG2017 222 AFVgLDSDG---RPAARLTDPDSGRRLEVSTDEfPGLQVYTGNFLDPGRD----------GVCLEPQTGPpDAPNHPGFE 288
|
330 340
....*....|....*....|..
gi 1230355636 324 qPDCFLRPGEEYSSLTEYQFIA 345
Cdd:COG2017 289 -GLIVLAPGETYSATTRIRFSV 309
|
|
| Aldose_epim |
pfam01263 |
Aldose 1-epimerase; |
16-342 |
1.25e-102 |
|
Aldose 1-epimerase;
Pssm-ID: 396013 Cd Length: 300 Bit Score: 303.93 E-value: 1.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 16 RLLTLRNNAGMVVTLMDWGATLLSARIPlsdGSVREALLGCASPECYQDQAAFLGASIGRYANRIANSRYTFDGETVTLS 95
Cdd:pfam01263 1 DLITLTNGNGLSATISLYGATLLSLKVP---GKLREVLLGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 96 PSQ-GVNQLHGGPEGfdkRRWQIV-NQNDRQVLFALSSD-DGDQGFPGNLGATVQYRLTDDNRISITYRAT-VDKPCPVN 171
Cdd:pfam01263 78 QNGpGKNPLHGGARG---RIWEVEeVKPDDGVTVTLVLDpDGEEGYPGDLEARVTYTLNEDNELTIEYEATnDGKPTPFN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 172 MTNHVYFNLDGeqsDVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIAsefladddqRKVKGYDHAFLLq 251
Cdd:pfam01263 155 LGNHPYFNLSG---DIDIHELQIEADEYLEVDDDLIPTGELKDVKGTPFDFRQPTPIG---------EDILGYDHVYLL- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 252 akgDGKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGtpsrgtePYADWQGLALESEFLPDSPNHPEWpqPDCFLRP 331
Cdd:pfam01263 222 ---DPLKAVIIDPDPGSGIVLEVSTTQPGLVVYTPNFLKG-------KYLSDEGFALETQFLPDEPNHPEF--PSIILKP 289
|
330
....*....|.
gi 1230355636 332 GEEYSSLTEYQ 342
Cdd:pfam01263 290 GESYTAETSYS 300
|
|
| PLN00194 |
PLN00194 |
aldose 1-epimerase; Provisional |
22-343 |
3.35e-84 |
|
aldose 1-epimerase; Provisional
Pssm-ID: 215098 [Multi-domain] Cd Length: 337 Bit Score: 258.07 E-value: 3.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 22 NNAGMVVTLMDWGATLLSARIPLSDGSVREALLGCASPECYQDQAAFLGASIGRYANRIANSRYTFDGETVTLSPSQGVN 101
Cdd:PLN00194 15 KNGNISVKLTNYGATITSLILPDKNGKLADVVLGFDSVEPYKNDSPYFGAIVGRVANRIKGAKFTLNGVTYKLPPNNGPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 102 QLHGGPEGFDKRRWQIVNQNDRQ---VLFALSSDDGDQGFPGNLGATVQYRLTDDNRISITYRAT-VDKPCPVNMTNHVY 177
Cdd:PLN00194 95 SLHGGPKGFSKVVWEVAKYKKGEkpsITFKYHSFDGEEGFPGDLSVTVTYTLLSSNTLRLDMEAKpLNKATPVNLAQHTY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 178 FNLDGEQS-DVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFladddqRKV-KGYDHAFLLQAKGD 255
Cdd:PLN00194 175 WNLAGHNSgDILSHKIQIFGSHITPVDENLIPTGEILPVKGTPFDFTTPKKIGSRI------NELpKGYDHNYVLDGEEK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 256 GK-KVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGTPSRGTEPYADWQGLALESEFLPDSPNHPEWPQpdCFLRPGEE 334
Cdd:PLN00194 249 EGlKKAAKVKDPKSGRVLELWTNAPGMQFYTSNYVNGVKGKGGAVYGKHAGLCLETQGFPDAVNQPNFPS--VVVNPGEK 326
|
....*....
gi 1230355636 335 YSSLTEYQF 343
Cdd:PLN00194 327 YKHTMLFEF 335
|
|
| PTZ00485 |
PTZ00485 |
aldolase 1-epimerase; Provisional |
28-346 |
3.86e-40 |
|
aldolase 1-epimerase; Provisional
Pssm-ID: 240435 Cd Length: 376 Bit Score: 145.14 E-value: 3.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 28 VTLMDWGATLLSARI--PLSDGSVRealLGCASPECYQDQAA---FLGASIGRYANRIANSRYTFDGETVTLSPSQGVNQ 102
Cdd:PTZ00485 25 VGLTNYAASVASIQVyhPADNKWIE---VNCGYPKNPEEAYAdpdYMGATVGRCAGRVAGGVFTLDGVKYYTQKNRGENT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 103 LHGGPEGFDKRRWQ---IVNQNDRQVLFALSSDDGDQGFPGNLGATVQYRL--TDDNRISITYRATV--DKPC---PVNM 172
Cdd:PTZ00485 102 CHCGDDAYHKKHWGmklIETANVIGVRFNYTSPHMENGFPGELVSKVTYSIerSKPNVLKTIYDSYIpeTSPAdatPVNI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 173 TNHVYFNLDG-------------EQSDVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFladDD-- 237
Cdd:PTZ00485 182 FNHAYWNLNGiperngkknavwvQPESVRNHWLRVPASRVAEADRMAIPTGEFLSVEGTGLDFRQGRVIGDCI---DDva 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 238 --QRKVKGYDHAFLLQAKGDGK-KVAAHVWSADEKLQLKVYTTAPALQFYSGN-----FLGGTPSRgtepYADWQGLALE 309
Cdd:PTZ00485 259 llDRDPCGYDHPLAIDGWEKGKlMLHAEAKSPVTNICMKVYSTFPCMWVYTANnkplpASGGPGQR----YARWTGMGLE 334
|
330 340 350
....*....|....*....|....*....|....*....
gi 1230355636 310 SEFLPDSPNHpeWPQ-PDCFLRPGE-EYSSLTEYQFIAE 346
Cdd:PTZ00485 335 PQYFPDVANH--YPKyPSCIVRRGErRFTETILNEFTVE 371
|
|
| Aldose_epim |
cd01081 |
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ... |
27-322 |
4.06e-28 |
|
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: 110.63 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 27 VVTLMDWGATLLSaripLSDGSVREALLGCASPECYQDQA-AFLGASIGRYANRIANSRYTFDGETVTLSPSQGVNQLHG 105
Cdd:cd01081 2 VAVIAPRGANIIS----LKVKGDVDLLWGYPDAEEYPLAPtGGGGAILFPFANRISDGRYTFDGKQYPLNEDEGGNAIHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 106 gpeGFDKRRWQIVNQ--NDRQVLFALSSDDGDQGFPGNLGATVQYRLtDDNRISITYRAT--VDKPCPVNMTNHVYFNLD 181
Cdd:cd01081 78 ---FVRNLPWRVVATdeEEASVTLSYDLNDGPGGYPFPLELTVTYTL-DADTLTITFTVTnlGDEPMPFGLGWHPYFGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 182 GEQSDvrNHKLQILADEYLPVDEGGIPhdGLKSVAGTSFDFRsakiiASEFLADDDqrkvkgYDHAFLLQAKGDGKKVAA 261
Cdd:cd01081 154 GVAIE--DLRLRVPASKVLPLDDLLPP--TGELEVPGEEDFR-----LGRPLGGGE------LDDCFLLLGNDAGTAEAR 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1230355636 262 hVWSADEKLQLKVYTTAPALQFYSGNFlGGTPSRGTEPYADWqglaleseflPDSPNHPEW 322
Cdd:cd01081 219 -LEDPDSRISVEFETGWPFWQVYTGDG-GRRGSVAIEPMTSA----------PDAFFNNNG 267
|
|
| Aldose_epim_Ec_YihR |
cd09022 |
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ... |
78-309 |
6.65e-21 |
|
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: 91.09 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 78 NRIANSRYTFDGETVTLS---PSQGvNQLHGgpEGFDkRRWQIVNQNDRQVlfALSSDDGDQ-GFPGNLGATVQYRLTDD 153
Cdd:cd09022 45 NRIADGRYTFDGVEHQLPitePERG-NAIHG--LVRW-ADWQLVEHTDSSV--TLRTRIPPQpGYPFTLELTVTYELDDD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 154 N-RISITYRATVDKPCPVNMTNHVYFNLDGEQSDvrNHKLQILADEYLPVDEGGIPHdGLKSVAGTSFDFRSAKIIASEF 232
Cdd:cd09022 119 GlTVTLTATNVGDEPAPFGVGFHPYLSAGGAPLD--ECTLTLPADTWLPVDERLLPT-GTEPVAGTPYDFRTGRRLGGTA 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1230355636 233 LadddqrkvkgyDHAFLLQAKGDGKKVAAHVWSAD-EKLQLKVYTTAPALQFYSGNFLGGTPSRgtepyadwQGLALE 309
Cdd:cd09022 196 L-----------DTAFTDLTRDADGRARARLTGPDgRGVELWADESFPWVQVFTADTLPPPGRR--------RGLAVE 254
|
|
| PRK15172 |
PRK15172 |
aldose-1-epimerase; |
67-309 |
1.53e-12 |
|
aldose-1-epimerase;
Pssm-ID: 237918 Cd Length: 300 Bit Score: 67.14 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 67 AFLGASIGRYANRIANSRYTFDGETVTLSPSQGVNQ--LHGgpeGFDKRRWQIVNQNDRQV---LFALSSddgdQGFPGN 141
Cdd:PRK15172 53 AHLGKVLIPWPNRIANGCYRYQGQEYQLPINEHVSKaaIHG---LLAWRDWQISELTATSVtltAFLPPS----YGYPFM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 142 LGATVQYRLTDDN--RISITYRATVDKPCPVNMTNHVYF--NLdgeqSDVRNHKLQILADEYLPVDEGGiPHDGLKSVAG 217
Cdd:PRK15172 126 LASQVIYSLDAATglSVEIASQNIGDVPAPYGVGIHPYLtcNL----TSVDEYLLQLPANQVLAVDEHA-NPTTLHHVDE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 218 TSFDFRSAKIIASEFLadddqrkvkgyDHAFllqakgdgkKVAAHVW-----SADEKLQLKVYTTAPALQFYSGNFLGGt 292
Cdd:PRK15172 201 LDLDFSQAKKIAATKI-----------DHTF---------KTANDLWevritHPQQALSVSLCSDQPWLQIYSGEKLQR- 259
|
250
....*....|....*..
gi 1230355636 293 psrgtepyadwQGLALE 309
Cdd:PRK15172 260 -----------QGLAVE 265
|
|
| Aldose_epim_Ec_YphB |
cd09021 |
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ... |
76-280 |
4.47e-11 |
|
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: 62.70 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 76 YANRIANSRYTFDGETVTLSPSQG--VNQLHGgpEGFDkRRWQIVNQNDRQVLFALSSDDGDQGFPGnlGATVQYRLTDD 153
Cdd:cd09021 46 FSNRIRGGRFLFAGREVALPPNTAdePHPLHG--DGWR-RPWQVVAASADSAELQLDHEADDPPWAY--RAEQRFHLAGD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1230355636 154 N-RISITYRATVDKPCPVNMTNHVYFNLDGEQsdvrnhKLQILADEYLPVDEGGIPhdGLKSVAGTSFDFRSAKIIASEf 232
Cdd:cd09021 121 GlSITLSVTNRGDRPMPAGLGFHPYFPRTPDT------RLQADADGVWLEDEDHLP--TGLRPHPPDWDFSQPRPLPDR- 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1230355636 233 ladddqrkvkGYDHAFllqakgDGKKVAAHVWSADEKLQLKVYTTAPA 280
Cdd:cd09021 192 ----------WIDNCF------TGWDGAALIWPPERGLALTIEADAPF 223
|
|
| |
