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Conserved domains on  [gi|504788269|ref|WP_014975371|]
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MULTISPECIES: aldose epimerase family protein [Alteromonas]

Protein Classification

aldose epimerase family protein( domain architecture ID 10173257)

aldose epimerase family protein similar to Homo sapiens galactose mutarotase, which catalyzes the interconversion of beta-D-galactose and alpha-D-galactose during galactose metabolism

CATH:  2.70.98.10
EC:  5.1.3.-
Gene Ontology:  GO:0016857|GO:0030246|GO:0005975
PubMed:  12717027
SCOP:  4000040

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 19-337 9.86e-138

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: 393.79  E-value: 9.86e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  19 FTLTNDNGMSVTLLNYGGIIKEIHFPNAEGESVSCVQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLDKN 98
Cdd:cd09019    2 YTLTNGNGLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  99 GGEHNLHGGLAGFHKKVWAAsvqETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSLVITANTDKETPLSFTQ 178
Cdd:cd09019   82 EGPNHLHGGPKGFDKRVWDV---EEVEENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNELTIEYEATTDKPTPVNLTN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 179 HAYFTLSNDPQ--VGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERAEqsnSHPLFDRVGGYDHNYVL 256
Cdd:cd09019  159 HSYFNLAGEGSgdILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIGRIDL---DDEQLKLGGGYDHNFVL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 257 RDTPEH-TPQATVKALDTGIAMSLFTNLPGLQFYTG---------GLKTDDQLGALCLEPQHFPDAPNKPEFPNCFVKPG 326
Cdd:cd09019  236 DKGGGKlRPAARLTSPESGRKLEVYTTQPGVQFYTGnfldgtpggGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPG 315

                        330
                 ....*....|.
gi 504788269 327 ETFKASMRYKF 337
Cdd:cd09019  316 ETYRHTTVYRF 326
 
Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 19-337 9.86e-138

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: 393.79  E-value: 9.86e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  19 FTLTNDNGMSVTLLNYGGIIKEIHFPNAEGESVSCVQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLDKN 98
Cdd:cd09019    2 YTLTNGNGLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  99 GGEHNLHGGLAGFHKKVWAAsvqETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSLVITANTDKETPLSFTQ 178
Cdd:cd09019   82 EGPNHLHGGPKGFDKRVWDV---EEVEENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNELTIEYEATTDKPTPVNLTN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 179 HAYFTLSNDPQ--VGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERAEqsnSHPLFDRVGGYDHNYVL 256
Cdd:cd09019  159 HSYFNLAGEGSgdILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIGRIDL---DDEQLKLGGGYDHNFVL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 257 RDTPEH-TPQATVKALDTGIAMSLFTNLPGLQFYTG---------GLKTDDQLGALCLEPQHFPDAPNKPEFPNCFVKPG 326
Cdd:cd09019  236 DKGGGKlRPAARLTSPESGRKLEVYTTQPGVQFYTGnfldgtpggGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPG 315

                        330
                 ....*....|.
gi 504788269 327 ETFKASMRYKF 337
Cdd:cd09019  316 ETYRHTTVYRF 326
galM_Leloir TIGR02636
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ...
 13-338 5.15e-99

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: 295.81  E-value: 5.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   13 GEVINAFTLTNDNGMSVTLLNYGGIIKEIHFPnAEGESVSCVQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTE 92
Cdd:TIGR02636   1 GQPAQLITLTNKNGMTISFMDIGATWLSCQVP-LAGELREVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   93 YTLDKNGGEHNLHGGLAGFHKKVWAaSVQETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSLVITANTDKET 172
Cdd:TIGR02636  80 YQLSINQGPNCLHGGPEGFDKRRWT-IETLEQAEVQVKFSLESPDGDQGFPGNLTVSVTYTLTDDNELKIDYEATTDKAT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  173 PLSFTQHAYFTLSNDPQ---VGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERAEQSNSHPLfdrVGG 249
Cdd:TIGR02636 159 PFNLTNHVYFNLDGADAgsdVLNHELQLNADRYLPLDEEGIPLGQLKPVDGTSFDFRKEKAIGQDFLANDQQQL---AKG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  250 YDHNYVL-RDTPEHTPQATVKALDTGIAMSLFTNLPGLQFYTG---GLKTDDQ------LGALCLEPQHFPDAPNKPEF- 318
Cdd:TIGR02636 236 YDHAFLLnGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGnflAGTPNRGgkkyvdHAGIALETQFLPDSPNHPEWg 315

                         330       340
                  ....*....|....*....|.
gi 504788269  319 -PNCFVKPGETFKASMRYKFS 338
Cdd:TIGR02636 316 dISCILSPGQEYQHQTRYQFI 336
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
19-339 9.96e-99

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


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 294.11  E-value: 9.96e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  19 FTLTNDnGMSVTLLNYGGIIKEIHFPNAEGESVscVQTFETLQDyIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLDKN 98
Cdd:COG2017   10 YTLENG-GLRAVIPEYGATLTSLRVPDKDGRDV--LLGFDDLED-DPPWAYGGAILGPYANRIADGRFTLDGKTYQLPIN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  99 GGEHNLHGglaGFHKKVWaaSVQETTDSvAVTFTLTSPDgEGGFPGTVNVEACYSLDqNNELSLVITA--NTDKETPLSF 176
Cdd:COG2017   86 EGPNALHG---GARDRPW--EVEEQSED-SVTLSLTSPD-EEGYPGNLELTVTYTLT-DNGLTITYTAtnLGDKPTPFNL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 177 TQHAYFTLSNDPQ--VGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERaeqsnshplfdrvgGYDHNY 254
Cdd:COG2017  158 GNHPYFNLPGEGGgdIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFREPRPLGDG--------------GFDHAF 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 255 VLRDtPEHTPQATVKALDTGIAMSLFTN-LPGLQFYTGGLKTDDQlGALCLEPQHFP-DAPNKPEF-PNCFVKPGETFKA 331
Cdd:COG2017  224 VGLD-SDGRPAARLTDPDSGRRLEVSTDeFPGLQVYTGNFLDPGR-DGVCLEPQTGPpDAPNHPGFeGLIVLAPGETYSA 301


                 ....*...
gi 504788269 332 SMRYKFSA 339
Cdd:COG2017  302 TTRIRFSV 309
PLN00194 PLN00194
aldose 1-epimerase; Provisional
 8-339 8.22e-92

aldose 1-epimerase; Provisional


Pssm-ID: 215098 [Multi-domain]  Cd Length: 337  Bit Score: 277.33  E-value: 8.22e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   8 FGEVEGEVINAFTLTNDNgMSVTLLNYGGIIKEIHFPNAEGESVSCVQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFA 87
Cdd:PLN00194   1 MASAAEEKPGIYELKNGN-ISVKLTNYGATITSLILPDKNGKLADVVLGFDSVEPYKNDSPYFGAIVGRVANRIKGAKFT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  88 LNGTEYTLDKNGGEHNLHGGLAGFHKKVWAASVQETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSLVITA- 166
Cdd:PLN00194  80 LNGVTYKLPPNNGPNSLHGGPKGFSKVVWEVAKYKKGEKPSITFKYHSFDGEEGFPGDLSVTVTYTLLSSNTLRLDMEAk 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 167 NTDKETPLSFTQHAYFTLSNDPQvGNTLLH---IDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERaeqsnshpl 243
Cdd:PLN00194 160 PLNKATPVNLAQHTYWNLAGHNS-GDILSHkiqIFGSHITPVDENLIPTGEILPVKGTPFDFTTPKKIGSR--------- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 244 FDRV-GGYDHNYVLRDT-PEHTPQ-ATVKALDTGIAMSLFTNLPGLQFYTGGLKTD---------DQLGALCLEPQHFPD 311
Cdd:PLN00194 230 INELpKGYDHNYVLDGEeKEGLKKaAKVKDPKSGRVLELWTNAPGMQFYTSNYVNGvkgkggavyGKHAGLCLETQGFPD 309

                        330       340
                 ....*....|....*....|....*...
gi 504788269 312 APNKPEFPNCFVKPGETFKASMRYKFSA 339
Cdd:PLN00194 310 AVNQPNFPSVVVNPGEKYKHTMLFEFSA 337
Aldose_epim pfam01263
Aldose 1-epimerase;
19-336 6.71e-84

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 255.78  E-value: 6.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   19 FTLTNDNGMSVTLLNYGGIIKEIHFPNAEGESVscvQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLDKN 98
Cdd:pfam01263   3 ITLTNGNGLSATISLYGATLLSLKVPGKLREVL---LGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   99 G-GEHNLHGGLAGfhkKVWAASVQETTDSVAVTFTLtSPDGEGGFPGTVNVEACYSLDQNNELSLVITA-NTDKETPLSF 176
Cdd:pfam01263  80 GpGKNPLHGGARG---RIWEVEEVKPDDGVTVTLVL-DPDGEEGYPGDLEARVTYTLNEDNELTIEYEAtNDGKPTPFNL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  177 TQHAYFTLSNDpqVGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKeraeqsnshplfDRVGGYDHNYVL 256
Cdd:pfam01263 156 GNHPYFNLSGD--IDIHELQIEADEYLEVDDDLIPTGELKDVKGTPFDFRQPTPIG------------EDILGYDHVYLL 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  257 rdtPEHTPQATVKALDTGIAMSLFTNLPGLQFYTGGLKTDD--QLGALCLEPQHFPDAPNKPEFPNCFVKPGETFKASMR 334
Cdd:pfam01263 222 ---DPLKAVIIDPDPGSGIVLEVSTTQPGLVVYTPNFLKGKylSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAETS 298


                  ..
gi 504788269  335 YK 336
Cdd:pfam01263 299 YS 300
 
Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 19-337 9.86e-138

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: 393.79  E-value: 9.86e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  19 FTLTNDNGMSVTLLNYGGIIKEIHFPNAEGESVSCVQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLDKN 98
Cdd:cd09019    2 YTLTNGNGLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  99 GGEHNLHGGLAGFHKKVWAAsvqETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSLVITANTDKETPLSFTQ 178
Cdd:cd09019   82 EGPNHLHGGPKGFDKRVWDV---EEVEENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNELTIEYEATTDKPTPVNLTN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 179 HAYFTLSNDPQ--VGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERAEqsnSHPLFDRVGGYDHNYVL 256
Cdd:cd09019  159 HSYFNLAGEGSgdILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIGRIDL---DDEQLKLGGGYDHNFVL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 257 RDTPEH-TPQATVKALDTGIAMSLFTNLPGLQFYTG---------GLKTDDQLGALCLEPQHFPDAPNKPEFPNCFVKPG 326
Cdd:cd09019  236 DKGGGKlRPAARLTSPESGRKLEVYTTQPGVQFYTGnfldgtpggGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPG 315

                        330
                 ....*....|.
gi 504788269 327 ETFKASMRYKF 337
Cdd:cd09019  316 ETYRHTTVYRF 326
galM_Leloir TIGR02636
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ...
 13-338 5.15e-99

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: 295.81  E-value: 5.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   13 GEVINAFTLTNDNGMSVTLLNYGGIIKEIHFPnAEGESVSCVQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTE 92
Cdd:TIGR02636   1 GQPAQLITLTNKNGMTISFMDIGATWLSCQVP-LAGELREVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   93 YTLDKNGGEHNLHGGLAGFHKKVWAaSVQETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSLVITANTDKET 172
Cdd:TIGR02636  80 YQLSINQGPNCLHGGPEGFDKRRWT-IETLEQAEVQVKFSLESPDGDQGFPGNLTVSVTYTLTDDNELKIDYEATTDKAT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  173 PLSFTQHAYFTLSNDPQ---VGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERAEQSNSHPLfdrVGG 249
Cdd:TIGR02636 159 PFNLTNHVYFNLDGADAgsdVLNHELQLNADRYLPLDEEGIPLGQLKPVDGTSFDFRKEKAIGQDFLANDQQQL---AKG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  250 YDHNYVL-RDTPEHTPQATVKALDTGIAMSLFTNLPGLQFYTG---GLKTDDQ------LGALCLEPQHFPDAPNKPEF- 318
Cdd:TIGR02636 236 YDHAFLLnGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGnflAGTPNRGgkkyvdHAGIALETQFLPDSPNHPEWg 315

                         330       340
                  ....*....|....*....|.
gi 504788269  319 -PNCFVKPGETFKASMRYKFS 338
Cdd:TIGR02636 316 dISCILSPGQEYQHQTRYQFI 336
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
19-339 9.96e-99

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


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 294.11  E-value: 9.96e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  19 FTLTNDnGMSVTLLNYGGIIKEIHFPNAEGESVscVQTFETLQDyIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLDKN 98
Cdd:COG2017   10 YTLENG-GLRAVIPEYGATLTSLRVPDKDGRDV--LLGFDDLED-DPPWAYGGAILGPYANRIADGRFTLDGKTYQLPIN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  99 GGEHNLHGglaGFHKKVWaaSVQETTDSvAVTFTLTSPDgEGGFPGTVNVEACYSLDqNNELSLVITA--NTDKETPLSF 176
Cdd:COG2017   86 EGPNALHG---GARDRPW--EVEEQSED-SVTLSLTSPD-EEGYPGNLELTVTYTLT-DNGLTITYTAtnLGDKPTPFNL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 177 TQHAYFTLSNDPQ--VGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERaeqsnshplfdrvgGYDHNY 254
Cdd:COG2017  158 GNHPYFNLPGEGGgdIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFREPRPLGDG--------------GFDHAF 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 255 VLRDtPEHTPQATVKALDTGIAMSLFTN-LPGLQFYTGGLKTDDQlGALCLEPQHFP-DAPNKPEF-PNCFVKPGETFKA 331
Cdd:COG2017  224 VGLD-SDGRPAARLTDPDSGRRLEVSTDeFPGLQVYTGNFLDPGR-DGVCLEPQTGPpDAPNHPGFeGLIVLAPGETYSA 301


                 ....*...
gi 504788269 332 SMRYKFSA 339
Cdd:COG2017  302 TTRIRFSV 309
PLN00194 PLN00194
aldose 1-epimerase; Provisional
 8-339 8.22e-92

aldose 1-epimerase; Provisional


Pssm-ID: 215098 [Multi-domain]  Cd Length: 337  Bit Score: 277.33  E-value: 8.22e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   8 FGEVEGEVINAFTLTNDNgMSVTLLNYGGIIKEIHFPNAEGESVSCVQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFA 87
Cdd:PLN00194   1 MASAAEEKPGIYELKNGN-ISVKLTNYGATITSLILPDKNGKLADVVLGFDSVEPYKNDSPYFGAIVGRVANRIKGAKFT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  88 LNGTEYTLDKNGGEHNLHGGLAGFHKKVWAASVQETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSLVITA- 166
Cdd:PLN00194  80 LNGVTYKLPPNNGPNSLHGGPKGFSKVVWEVAKYKKGEKPSITFKYHSFDGEEGFPGDLSVTVTYTLLSSNTLRLDMEAk 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 167 NTDKETPLSFTQHAYFTLSNDPQvGNTLLH---IDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERaeqsnshpl 243
Cdd:PLN00194 160 PLNKATPVNLAQHTYWNLAGHNS-GDILSHkiqIFGSHITPVDENLIPTGEILPVKGTPFDFTTPKKIGSR--------- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 244 FDRV-GGYDHNYVLRDT-PEHTPQ-ATVKALDTGIAMSLFTNLPGLQFYTGGLKTD---------DQLGALCLEPQHFPD 311
Cdd:PLN00194 230 INELpKGYDHNYVLDGEeKEGLKKaAKVKDPKSGRVLELWTNAPGMQFYTSNYVNGvkgkggavyGKHAGLCLETQGFPD 309

                        330       340
                 ....*....|....*....|....*...
gi 504788269 312 APNKPEFPNCFVKPGETFKASMRYKFSA 339
Cdd:PLN00194 310 AVNQPNFPSVVVNPGEKYKHTMLFEFSA 337
galM PRK11055
galactose-1-epimerase; Provisional
 17-339 2.22e-85

galactose-1-epimerase; Provisional


Pssm-ID: 182931  Cd Length: 342  Bit Score: 261.01  E-value: 2.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  17 NAFTLTNDNGMSVTLLNYGGIIKEIHFPNAEGESVSCVQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLD 96
Cdd:PRK11055  10 RLLTLRNNAGMVVTLMDWGATWLSCRVPLSDGSVREVLLGCASPEDYPDQAAYLGASVGRYANRIANSRFTLDGETYQLS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  97 KNGGEHNLHGGLAGFHKKVWaasVQETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSLVITANTDKETPLSF 176
Cdd:PRK11055  90 PNQGGNQLHGGPEGFDKRRW---QIVNQNDRQVTFSLSSPDGDQGFPGNLGATVTYRLTDDNRVSITYRATVDKPCPVNL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 177 TQHAYFTLSNDPQVGNTLLH---IDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKEraeqsnsHPLFDR----VGG 249
Cdd:PRK11055 167 TNHAYFNLDGAEEGSDVRNHklqINADEYLPVDEGGIPNGGLKSVAGTSFDFRQPKTIAQ-------DFLADDdqqkVKG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 250 YDHNYVLRDTPE-HTPQATVKALDTGIAMSLFTNLPGLQFYTG----GLKTDDQ-----LGALCLEPQHFPDAPNKPEF- 318
Cdd:PRK11055 240 YDHAFLLQAKGDgKKPAAHLWSPDEKLQMKVYTTAPALQFYSGnflaGTPSRGGgpyadYAGLALESQFLPDSPNHPEWp 319

                        330       340
                 ....*....|....*....|..
gi 504788269 319 -PNCFVKPGETFKASMRYKFSA 339
Cdd:PRK11055 320 qPDCILKPGEEYRSLTEYQFIA 341
Aldose_epim pfam01263
Aldose 1-epimerase;
19-336 6.71e-84

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 255.78  E-value: 6.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   19 FTLTNDNGMSVTLLNYGGIIKEIHFPNAEGESVscvQTFETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLDKN 98
Cdd:pfam01263   3 ITLTNGNGLSATISLYGATLLSLKVPGKLREVL---LGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269   99 G-GEHNLHGGLAGfhkKVWAASVQETTDSVAVTFTLtSPDGEGGFPGTVNVEACYSLDQNNELSLVITA-NTDKETPLSF 176
Cdd:pfam01263  80 GpGKNPLHGGARG---RIWEVEEVKPDDGVTVTLVL-DPDGEEGYPGDLEARVTYTLNEDNELTIEYEAtNDGKPTPFNL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  177 TQHAYFTLSNDpqVGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKeraeqsnshplfDRVGGYDHNYVL 256
Cdd:pfam01263 156 GNHPYFNLSGD--IDIHELQIEADEYLEVDDDLIPTGELKDVKGTPFDFRQPTPIG------------EDILGYDHVYLL 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  257 rdtPEHTPQATVKALDTGIAMSLFTNLPGLQFYTGGLKTDD--QLGALCLEPQHFPDAPNKPEFPNCFVKPGETFKASMR 334
Cdd:pfam01263 222 ---DPLKAVIIDPDPGSGIVLEVSTTQPGLVVYTPNFLKGKylSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAETS 298


                  ..
gi 504788269  335 YK 336
Cdd:pfam01263 299 YS 300
PTZ00485 PTZ00485
aldolase 1-epimerase; Provisional
 27-328 2.08e-48

aldolase 1-epimerase; Provisional


Pssm-ID: 240435  Cd Length: 376  Bit Score: 166.72  E-value: 2.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  27 MSVTLLNYGGIIKEI---HFPNAEGESVSCVQTfETLQDYIDDPSYRGAIVGRYANRIGHGSFALNGTEYTLDKNGGEHN 103
Cdd:PTZ00485  23 LKVGLTNYAASVASIqvyHPADNKWIEVNCGYP-KNPEEAYADPDYMGATVGRCAGRVAGGVFTLDGVKYYTQKNRGENT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 104 LHGGLAGFHKKVWAASVQETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDQNNELSL------VITANTDKE-TPLSF 176
Cdd:PTZ00485 102 CHCGDDAYHKKHWGMKLIETANVIGVRFNYTSPHMENGFPGELVSKVTYSIERSKPNVLktiydsYIPETSPADaTPVNI 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 177 TQHAYFTLSNDPQ--------------VGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFTKPTAIKERAEQSnshP 242
Cdd:PTZ00485 182 FNHAYWNLNGIPErngkknavwvqpesVRNHWLRVPASRVAEADRMAIPTGEFLSVEGTGLDFRQGRVIGDCIDDV---A 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 243 LFDR-VGGYDHNYVLrDTPEHTP---QATVKALDTGIAMSLFTNLPGLQFYTGGLKTDDQLG----------ALCLEPQH 308
Cdd:PTZ00485 259 LLDRdPCGYDHPLAI-DGWEKGKlmlHAEAKSPVTNICMKVYSTFPCMWVYTANNKPLPASGgpgqryarwtGMGLEPQY 337

                        330       340
                 ....*....|....*....|.
gi 504788269 309 FPDAPNK-PEFPNCFVKPGET 328
Cdd:PTZ00485 338 FPDVANHyPKYPSCIVRRGER 358
Aldose_epim cd01081
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
 29-334 1.01e-34

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: 128.35  E-value: 1.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  29 VTLLNYGGIIKEIHFPNAegesVSCVQTFETLQDYIDDPS-YRGAIVGRYANRIGHGSFALNGTEYTLDKNGGEHNLHGG 107
Cdd:cd01081    3 AVIAPRGANIISLKVKGD----VDLLWGYPDAEEYPLAPTgGGGAILFPFANRISDGRYTFDGKQYPLNEDEGGNAIHGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 108 LagfHKKVWAAsVQETTDSVAVTFTLTSPDGEGGFPGTVNVEACYSLDqNNELSLVITA-NT-DKETPLSFTQHAYFTLs 185
Cdd:cd01081   79 V---RNLPWRV-VATDEEEASVTLSYDLNDGPGGYPFPLELTVTYTLD-ADTLTITFTVtNLgDEPMPFGLGWHPYFGL- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 186 NDPQVGNTLLHIDADKVTDADSTLLPTGKLVEVANTPFDFtkptaikeraeqsnshPLFDRVGGYDHNYVLRDTPEHTPQ 265
Cdd:cd01081  153 PGVAIEDLRLRVPASKVLPLDDLLPPTGELEVPGEEDFRL----------------GRPLGGGELDDCFLLLGNDAGTAE 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504788269 266 ATVKALDTGIAMSLFTNLPGLQFYTGGLKTDDqlgALCLEPQ-HFPDAPNKPEFP-NCFVKPGETFKASMR 334
Cdd:cd01081  217 ARLEDPDSRISVEFETGWPFWQVYTGDGGRRG---SVAIEPMtSAPDAFFNNNGGlITLKPPGETRTFSIT 284
Aldose_epim_Ec_YihR cd09022
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ...
 67-335 4.64e-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: 4.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  67 PSYRGAIVGRYANRIGHGSFALNGTEYTLDKNGGE-HN-LHgGLAGFHkkVWAASvqETTDSvAVTFTLTSPDGEgGFPG 144
Cdd:cd09022   33 PGAAGQVLAPWPNRIADGRYTFDGVEHQLPITEPErGNaIH-GLVRWA--DWQLV--EHTDS-SVTLRTRIPPQP-GYPF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 145 TVNVEACYSLDQnNELSLVITA-NTDKET-PLSFTQHAYFTLsNDPQVGNTLLHIDADKVTDADSTLLPTGkLVEVANTP 222
Cdd:cd09022  106 TLELTVTYELDD-DGLTVTLTAtNVGDEPaPFGVGFHPYLSA-GGAPLDECTLTLPADTWLPVDERLLPTG-TEPVAGTP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 223 FDFTKPTAIKERAeqsnshplfdrvggYDHNYV-LRDTPEHTPQATVKALD-TGIAMSLFTNLPGLQFYTG-GLKTDDQL 299
Cdd:cd09022  183 YDFRTGRRLGGTA--------------LDTAFTdLTRDADGRARARLTGPDgRGVELWADESFPWVQVFTAdTLPPPGRR 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 504788269 300 GALCLEPQHFPdapnkpefPNCFV--------KPGETFKASMRY 335
Cdd:cd09022  249 RGLAVEPMTCP--------PNAFNsgtdlivlAPGETHTASWGI 284
Aldose_epim_Ec_YphB cd09021
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ...
 77-334 5.02e-14

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: 71.17  E-value: 5.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  77 YANRIGHGSFALNGTEYTLDKN-GGE-HNLHGglagfhkKVWAA--SVQETTDSvAVTFTLTSPDGEGGFPGTVNVEacY 152
Cdd:cd09021   46 FSNRIRGGRFLFAGREVALPPNtADEpHPLHG-------DGWRRpwQVVAASAD-SAELQLDHEADDPPWAYRAEQR--F 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 153 SLDqNNELSLVITA-NTDKET-PLSFTQHAYFtlsndPQVGNTLLHIDADKVTDADSTLLPTGkLVEVANtPFDFTKPTA 230
Cdd:cd09021  116 HLA-GDGLSITLSVtNRGDRPmPAGLGFHPYF-----PRTPDTRLQADADGVWLEDEDHLPTG-LRPHPP-DWDFSQPRP 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 231 IKERaeqsnshplfdrvgGYDHNYVLRD--TPEHTPQAtvkaldtGIAMSLFTNlPGLQFYTggLKTDDQLGALCLEPQ- 307
Cdd:cd09021  188 LPDR--------------WIDNCFTGWDgaALIWPPER-------GLALTIEAD-APFSHLV--VYRPPGEDFFCLEPVs 243

                        250       260
                 ....*....|....*....|....*...
gi 504788269 308 HFPDAPNKPEFPN-CFVKPGETFKASMR 334
Cdd:cd09021  244 HAPDAHHGPGDPGlRVLAPGESLSLSMR 271
PRK15172 PRK15172
aldose-1-epimerase;
79-328 2.11e-10

aldose-1-epimerase;


Pssm-ID: 237918  Cd Length: 300  Bit Score: 60.60  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  79 NRIGHGSFALNGTEYTLDKN--GGEHNLHGGLAGfhkKVWAASVQETTDsvaVTFTLTSPDGEgGFPGTVNVEACYSLDQ 156
Cdd:PRK15172  64 NRIANGCYRYQGQEYQLPINehVSKAAIHGLLAW---RDWQISELTATS---VTLTAFLPPSY-GYPFMLASQVIYSLDA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 157 NNELSLVITANT--DKETPLSFTQHAYFTlSNDPQVGNTLLHIDADKVTDADSTLLPTgKLVEVANTPFDFTKPTAIKER 234
Cdd:PRK15172 137 ATGLSVEIASQNigDVPAPYGVGIHPYLT-CNLTSVDEYLLQLPANQVLAVDEHANPT-TLHHVDELDLDFSQAKKIAAT 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 235 AeqsnshplfdrvggYDHNYvlrDTPEHTPQATVKALDTGIAMSLFTNLPGLQFYTGglktdDQLG--ALCLEPQHFPda 312
Cdd:PRK15172 215 K--------------IDHTF---KTANDLWEVRITHPQQALSVSLCSDQPWLQIYSG-----EKLQrqGLAVEPMSCP-- 270

                        250       260
                 ....*....|....*....|....
gi 504788269 313 pnkpefPNCF--------VKPGET 328
Cdd:PRK15172 271 ------PNAFnsgidlllLEPGKT 288
Aldose_epim_Slr1438 cd09025
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis ...
 84-335 1.24e-04

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: 43.01  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269  84 GSFALNGTEYTLDKNGGEHNLhgglagfhkkvwAASVQETTDSVAVTFTLTS-PDGEGGFPGTVNVEACYSLDQNN-ELS 161
Cdd:cd09025   67 DGYPLAGQEYTLKQHGFARDL------------PWEVELLGDGAGLTLTLRDnEATRAVYPFDFELELTYRLAGNTlEIA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 162 LVITANTDKETPLSFTQHAYFTLsndPQVGNTLLHIDADKVTDADSTllptgklvEVANTP--FDFTKPTaIKERAEQSN 239
Cdd:cd09025  135 QRVHNLGDQPMPFSFGFHPYFAV---PDKAKLSLDLPPTRCFDQKTD--------EEANTPgqFDETEEG-VDLLFRPLG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504788269 240 SHPLFDRVGGYdhnyvlrdtpehtpQATVKALDTGIAMSLFTnLPGLQFYtgglktddqlgalCLEP-QHFPDAPN---- 314
Cdd:cd09025  203 PASLTDGARGL--------------KITLDHDEPFSNLVVWT-DKGKDFV-------------CLEPwTGPRNALNtger 254

                        250       260
                 ....*....|....*....|.
gi 504788269 315 KPefpncFVKPGETFKASMRY 335
Cdd:cd09025  255 LL-----LLPPGETEEASVRI 270
 
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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