NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488215647|ref|WP_002286855|]
View 

MULTISPECIES: aldose epimerase family protein [Enterococcus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 14-338 4.60e-131

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: 376.85  E-value: 4.60e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  14 LITLENKNKLALSISDLGARIVSLKSNDR-----ELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKTYQLAT 88
Cdd:cd09019    1 LYTLTNGNGLRVSILNYGATIQSLKVPDKngklrDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  89 DPKtGHNLHGGAPGFELKKWSYVILNgenEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSDQDTLFNP 168
Cdd:cd09019   81 NEG-PNHLHGGPKGFDKRVWDVEEVE---ENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNELTIEYEATTDKPTPVNL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 169 TNHVYFNLTGDASQSIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLAsVFASDLDQKNLVDGIDHPFFL 248
Cdd:cd09019  157 TNHSYFNLAGEGSGDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIG-RIDLDDEQLKLGGGYDHNFVL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 249 -KETGLGKEAARLTSPDKRIQVDIATDASSVVIFTANFGTETPEMRNRKLAHHGGITFETQTAPGAERFSAFGSIHLKAG 327
Cdd:cd09019  236 dKGGGKLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTPGGGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPG 315

                        330
                 ....*....|.
gi 488215647 328 SVFETVTEFKI 338
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 ...
 14-338 4.60e-131

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: 376.85  E-value: 4.60e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  14 LITLENKNKLALSISDLGARIVSLKSNDR-----ELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKTYQLAT 88
Cdd:cd09019    1 LYTLTNGNGLRVSILNYGATIQSLKVPDKngklrDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  89 DPKtGHNLHGGAPGFELKKWSYVILNgenEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSDQDTLFNP 168
Cdd:cd09019   81 NEG-PNHLHGGPKGFDKRVWDVEEVE---ENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNELTIEYEATTDKPTPVNL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 169 TNHVYFNLTGDASQSIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLAsVFASDLDQKNLVDGIDHPFFL 248
Cdd:cd09019  157 TNHSYFNLAGEGSGDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIG-RIDLDDEQLKLGGGYDHNFVL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 249 -KETGLGKEAARLTSPDKRIQVDIATDASSVVIFTANFGTETPEMRNRKLAHHGGITFETQTAPGAERFSAFGSIHLKAG 327
Cdd:cd09019  236 dKGGGKLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTPGGGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPG 315

                        330
                 ....*....|.
gi 488215647 328 SVFETVTEFKI 338
Cdd:cd09019  316 ETYRHTTVYRF 326
galM_Leloir TIGR02636
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ...
 9-337 6.92e-124

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: 359.37  E-value: 6.92e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647    9 GQGYHLITLENKNKLALSISDLGARIVSLK----SNDRELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKTY 84
Cdd:TIGR02636   1 GQPAQLITLTNKNGMTISFMDIGATWLSCQvplaGELREVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   85 QLATDpKTGHNLHGGAPGFELKKWSYVILNGEnEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSDQDT 164
Cdd:TIGR02636  81 QLSIN-QGPNCLHGGPEGFDKRRWTIETLEQA-EVQVKFSLESPDGDQGFPGNLTVSVTYTLTDDNELKIDYEATTDKAT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  165 LFNPTNHVYFNLTG-DASQSIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVFASDLDQKnLVDGID 243
Cdd:TIGR02636 159 PFNLTNHVYFNLDGaDAGSDVLNHELQLNADRYLPLDEEGIPLGQLKPVDGTSFDFRKEKAIGQDFLANDQQQ-LAKGYD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  244 HPFFL-KETGLGKEAARLTSPDKRIQVDIATDASSVVIFTANFGTETPEMRNRKLAHHGGITFETQTAPGAERFSAFGSI 322
Cdd:TIGR02636 238 HAFLLnGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGNFLAGTPNRGGKKYVDHAGIALETQFLPDSPNHPEWGDI 317

                         330
                  ....*....|....*..
gi 488215647  323 --HLKAGSVFETVTEFK 337
Cdd:TIGR02636 318 scILSPGQEYQHQTRYQ 334
galM PRK11055
galactose-1-epimerase; Provisional
 9-311 1.40e-87

galactose-1-epimerase; Provisional


Pssm-ID: 182931  Cd Length: 342  Bit Score: 266.79  E-value: 1.40e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   9 GQGYHLITLENKNKLALSISDLGAR----IVSLKSND-RELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKT 83
Cdd:PRK11055   6 GQPYRLLTLRNNAGMVVTLMDWGATwlscRVPLSDGSvREVLLGCASPEDYPDQAAYLGASVGRYANRIANSRFTLDGET 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  84 YQLATDpKTGHNLHGGAPGFELKKWsyVILNgENEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSDQD 163
Cdd:PRK11055  86 YQLSPN-QGGNQLHGGPEGFDKRRW--QIVN-QNDRQVTFSLSSPDGDQGFPGNLGATVTYRLTDDNRVSITYRATVDKP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 164 TLFNPTNHVYFNLTGDASQS-IDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVFASDLDQKnLVDGI 242
Cdd:PRK11055 162 CPVNLTNHAYFNLDGAEEGSdVRNHKLQINADEYLPVDEGGIPNGGLKSVAGTSFDFRQPKTIAQDFLADDDQQ-KVKGY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 243 DHPFFLKETGLGKE-AARLTSPDKRIQVDIATDASSVVIFTANFGTETPEMRNRKLAHHGGITFETQTAP 311
Cdd:PRK11055 241 DHAFLLQAKGDGKKpAAHLWSPDEKLQMKVYTTAPALQFYSGNFLAGTPSRGGGPYADYAGLALESQFLP 310
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
13-340 2.23e-78

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


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 242.11  E-value: 2.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  13 HLITLENKNkLALSISDLGARIVSLK---SNDRELVLGFDTAEEyIEKDPYIGASIGRTAGRIENGRFSLNGKTYQLATD 89
Cdd:COG2017    8 ELYTLENGG-LRAVIPEYGATLTSLRvpdKDGRDVLLGFDDLED-DPPWAYGGAILGPYANRIADGRFTLDGKTYQLPIN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  90 PkTGHNLHGGapgFELKKWSYVIlngENEASVIFTTTSPDgEHGFPGTMDVEIRYTLTkDNIWRVTSRGT--SDQDTLFN 167
Cdd:COG2017   86 E-GPNALHGG---ARDRPWEVEE---QSEDSVTLSLTSPD-EEGYPGNLELTVTYTLT-DNGLTITYTATnlGDKPTPFN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 168 PTNHVYFNLTGDASQSIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVfasdldqknlvdGIDHPFf 247
Cdd:COG2017  157 LGNHPYFNLPGEGGGDIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFREPRPLGDG------------GFDHAF- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 248 lkeTGL---GKEAARLTSPDKRIQVDIATDASS-VVIFTANFGTEtpemrnrklaHHGGITFETQTAP-GAERFSAF-GS 321
Cdd:COG2017  224 ---VGLdsdGRPAARLTDPDSGRRLEVSTDEFPgLQVYTGNFLDP----------GRDGVCLEPQTGPpDAPNHPGFeGL 290

                        330
                 ....*....|....*....
gi 488215647 322 IHLKAGSVFETVTEFKIKT 340
Cdd:COG2017  291 IVLAPGETYSATTRIRFSV 309
Aldose_epim pfam01263
Aldose 1-epimerase;
13-337 7.76e-76

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 235.37  E-value: 7.76e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   13 HLITLENKNKLALSISDLGARIVSLKSND--RELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKTYQLATDP 90
Cdd:pfam01263   1 DLITLTNGNGLSATISLYGATLLSLKVPGklREVLLGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLPQNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   91 KTGHNLHGGAPGfelKKWSYVILngENEASVIFTTTS-PDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSD-QDTLFNP 168
Cdd:pfam01263  81 PGKNPLHGGARG---RIWEVEEV--KPDDGVTVTLVLdPDGEEGYPGDLEARVTYTLNEDNELTIEYEATNDgKPTPFNL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  169 TNHVYFNLTGDasqsIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVfasdldqknlVDGIDHPFFL 248
Cdd:pfam01263 156 GNHPYFNLSGD----IDIHELQIEADEYLEVDDDLIPTGELKDVKGTPFDFRQPTPIGED----------ILGYDHVYLL 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  249 KEtglGKEAARLTSPDKRIQVDIATDASSVVIFTANFgtetpemRNRKLAHHGGITFETQTAPGAERFSAFGSIHLKAGS 328
Cdd:pfam01263 222 DP---LKAVIIDPDPGSGIVLEVSTTQPGLVVYTPNF-------LKGKYLSDEGFALETQFLPDEPNHPEFPSIILKPGE 291


                  ....*....
gi 488215647  329 VFETVTEFK 337
Cdd:pfam01263 292 SYTAETSYS 300
 
Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 14-338 4.60e-131

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: 376.85  E-value: 4.60e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  14 LITLENKNKLALSISDLGARIVSLKSNDR-----ELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKTYQLAT 88
Cdd:cd09019    1 LYTLTNGNGLRVSILNYGATIQSLKVPDKngklrDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  89 DPKtGHNLHGGAPGFELKKWSYVILNgenEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSDQDTLFNP 168
Cdd:cd09019   81 NEG-PNHLHGGPKGFDKRVWDVEEVE---ENSVTFSLVSPDGEEGFPGNLTVTVTYTLTDDNELTIEYEATTDKPTPVNL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 169 TNHVYFNLTGDASQSIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLAsVFASDLDQKNLVDGIDHPFFL 248
Cdd:cd09019  157 TNHSYFNLAGEGSGDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIG-RIDLDDEQLKLGGGYDHNFVL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 249 -KETGLGKEAARLTSPDKRIQVDIATDASSVVIFTANFGTETPEMRNRKLAHHGGITFETQTAPGAERFSAFGSIHLKAG 327
Cdd:cd09019  236 dKGGGKLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTPGGGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPG 315

                        330
                 ....*....|.
gi 488215647 328 SVFETVTEFKI 338
Cdd:cd09019  316 ETYRHTTVYRF 326
galM_Leloir TIGR02636
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ...
 9-337 6.92e-124

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: 359.37  E-value: 6.92e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647    9 GQGYHLITLENKNKLALSISDLGARIVSLK----SNDRELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKTY 84
Cdd:TIGR02636   1 GQPAQLITLTNKNGMTISFMDIGATWLSCQvplaGELREVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   85 QLATDpKTGHNLHGGAPGFELKKWSYVILNGEnEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSDQDT 164
Cdd:TIGR02636  81 QLSIN-QGPNCLHGGPEGFDKRRWTIETLEQA-EVQVKFSLESPDGDQGFPGNLTVSVTYTLTDDNELKIDYEATTDKAT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  165 LFNPTNHVYFNLTG-DASQSIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVFASDLDQKnLVDGID 243
Cdd:TIGR02636 159 PFNLTNHVYFNLDGaDAGSDVLNHELQLNADRYLPLDEEGIPLGQLKPVDGTSFDFRKEKAIGQDFLANDQQQ-LAKGYD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  244 HPFFL-KETGLGKEAARLTSPDKRIQVDIATDASSVVIFTANFGTETPEMRNRKLAHHGGITFETQTAPGAERFSAFGSI 322
Cdd:TIGR02636 238 HAFLLnGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGNFLAGTPNRGGKKYVDHAGIALETQFLPDSPNHPEWGDI 317

                         330
                  ....*....|....*..
gi 488215647  323 --HLKAGSVFETVTEFK 337
Cdd:TIGR02636 318 scILSPGQEYQHQTRYQ 334
galM PRK11055
galactose-1-epimerase; Provisional
 9-311 1.40e-87

galactose-1-epimerase; Provisional


Pssm-ID: 182931  Cd Length: 342  Bit Score: 266.79  E-value: 1.40e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   9 GQGYHLITLENKNKLALSISDLGAR----IVSLKSND-RELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKT 83
Cdd:PRK11055   6 GQPYRLLTLRNNAGMVVTLMDWGATwlscRVPLSDGSvREVLLGCASPEDYPDQAAYLGASVGRYANRIANSRFTLDGET 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  84 YQLATDpKTGHNLHGGAPGFELKKWsyVILNgENEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSDQD 163
Cdd:PRK11055  86 YQLSPN-QGGNQLHGGPEGFDKRRW--QIVN-QNDRQVTFSLSSPDGDQGFPGNLGATVTYRLTDDNRVSITYRATVDKP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 164 TLFNPTNHVYFNLTGDASQS-IDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVFASDLDQKnLVDGI 242
Cdd:PRK11055 162 CPVNLTNHAYFNLDGAEEGSdVRNHKLQINADEYLPVDEGGIPNGGLKSVAGTSFDFRQPKTIAQDFLADDDQQ-KVKGY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 243 DHPFFLKETGLGKE-AARLTSPDKRIQVDIATDASSVVIFTANFGTETPEMRNRKLAHHGGITFETQTAP 311
Cdd:PRK11055 241 DHAFLLQAKGDGKKpAAHLWSPDEKLQMKVYTTAPALQFYSGNFLAGTPSRGGGPYADYAGLALESQFLP 310
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
13-340 2.23e-78

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


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 242.11  E-value: 2.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  13 HLITLENKNkLALSISDLGARIVSLK---SNDRELVLGFDTAEEyIEKDPYIGASIGRTAGRIENGRFSLNGKTYQLATD 89
Cdd:COG2017    8 ELYTLENGG-LRAVIPEYGATLTSLRvpdKDGRDVLLGFDDLED-DPPWAYGGAILGPYANRIADGRFTLDGKTYQLPIN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  90 PkTGHNLHGGapgFELKKWSYVIlngENEASVIFTTTSPDgEHGFPGTMDVEIRYTLTkDNIWRVTSRGT--SDQDTLFN 167
Cdd:COG2017   86 E-GPNALHGG---ARDRPWEVEE---QSEDSVTLSLTSPD-EEGYPGNLELTVTYTLT-DNGLTITYTATnlGDKPTPFN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 168 PTNHVYFNLTGDASQSIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVfasdldqknlvdGIDHPFf 247
Cdd:COG2017  157 LGNHPYFNLPGEGGGDIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFREPRPLGDG------------GFDHAF- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 248 lkeTGL---GKEAARLTSPDKRIQVDIATDASS-VVIFTANFGTEtpemrnrklaHHGGITFETQTAP-GAERFSAF-GS 321
Cdd:COG2017  224 ---VGLdsdGRPAARLTDPDSGRRLEVSTDEFPgLQVYTGNFLDP----------GRDGVCLEPQTGPpDAPNHPGFeGL 290

                        330
                 ....*....|....*....
gi 488215647 322 IHLKAGSVFETVTEFKIKT 340
Cdd:COG2017  291 IVLAPGETYSATTRIRFSV 309
Aldose_epim pfam01263
Aldose 1-epimerase;
13-337 7.76e-76

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 235.37  E-value: 7.76e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   13 HLITLENKNKLALSISDLGARIVSLKSND--RELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKTYQLATDP 90
Cdd:pfam01263   1 DLITLTNGNGLSATISLYGATLLSLKVPGklREVLLGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLPQNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   91 KTGHNLHGGAPGfelKKWSYVILngENEASVIFTTTS-PDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTSD-QDTLFNP 168
Cdd:pfam01263  81 PGKNPLHGGARG---RIWEVEEV--KPDDGVTVTLVLdPDGEEGYPGDLEARVTYTLNEDNELTIEYEATNDgKPTPFNL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  169 TNHVYFNLTGDasqsIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVfasdldqknlVDGIDHPFFL 248
Cdd:pfam01263 156 GNHPYFNLSGD----IDIHELQIEADEYLEVDDDLIPTGELKDVKGTPFDFRQPTPIGED----------ILGYDHVYLL 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  249 KEtglGKEAARLTSPDKRIQVDIATDASSVVIFTANFgtetpemRNRKLAHHGGITFETQTAPGAERFSAFGSIHLKAGS 328
Cdd:pfam01263 222 DP---LKAVIIDPDPGSGIVLEVSTTQPGLVVYTPNF-------LKGKYLSDEGFALETQFLPDEPNHPEFPSIILKPGE 291


                  ....*....
gi 488215647  329 VFETVTEFK 337
Cdd:pfam01263 292 SYTAETSYS 300
PLN00194 PLN00194
aldose 1-epimerase; Provisional
 19-340 7.47e-56

aldose 1-epimerase; Provisional


Pssm-ID: 215098 [Multi-domain]  Cd Length: 337  Bit Score: 185.27  E-value: 7.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  19 NKNKLALSISDLGARIVSLKSNDR-----ELVLGFDTAEEYIEKDPYIGASIGRTAGRIENGRFSLNGKTYQLAtdPKTG 93
Cdd:PLN00194  15 KNGNISVKLTNYGATITSLILPDKngklaDVVLGFDSVEPYKNDSPYFGAIVGRVANRIKGAKFTLNGVTYKLP--PNNG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  94 HN-LHGGAPGFELKKWSYVILNGENEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNIWRVTSRGTS-DQDTLFNPTNH 171
Cdd:PLN00194  93 PNsLHGGPKGFSKVVWEVAKYKKGEKPSITFKYHSFDGEEGFPGDLSVTVTYTLLSSNTLRLDMEAKPlNKATPVNLAQH 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 172 VYFNLTGDASQSIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLASVFasdldqKNLVDGIDHPFFLKET 251
Cdd:PLN00194 173 TYWNLAGHNSGDILSHKIQIFGSHITPVDENLIPTGEILPVKGTPFDFTTPKKIGSRI------NELPKGYDHNYVLDGE 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 252 GLG--KEAARLTSPDKRIQVDIATDASSVVIFTANFGTETPEMRNRKLAHHGGITFETQTAPGAERFSAFGSIHLKAGSV 329
Cdd:PLN00194 247 EKEglKKAAKVKDPKSGRVLELWTNAPGMQFYTSNYVNGVKGKGGAVYGKHAGLCLETQGFPDAVNQPNFPSVVVNPGEK 326

                        330
                 ....*....|.
gi 488215647 330 FETVTEFKIKT 340
Cdd:PLN00194 327 YKHTMLFEFSA 337
Aldose_epim cd01081
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
 25-335 4.51e-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: 126.42  E-value: 4.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  25 LSISDLGARIVSLKSN-DRELVLGFDTAEEYI-EKDPYIGASIGRTAGRIENGRFSLNGKTYQLATDPKtGHNLHGGAPg 102
Cdd:cd01081    3 AVIAPRGANIISLKVKgDVDLLWGYPDAEEYPlAPTGGGGAILFPFANRISDGRYTFDGKQYPLNEDEG-GNAIHGFVR- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 103 feLKKWSYVILnGENEASVIFTTTSPDGEHGFPGTMDVEIRYTLTKDNiWRVTSRGT--SDQDTLFNPTNHVYFNLTGDA 180
Cdd:cd01081   81 --NLPWRVVAT-DEEEASVTLSYDLNDGPGGYPFPLELTVTYTLDADT-LTITFTVTnlGDEPMPFGLGWHPYFGLPGVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 181 sqsIDQHELWLNSEAYAPLRTDSIPIGVKENAAGSAFDFQIPKKLasvfasdldqknlvDGIDHPFFLKETGLGKEAARL 260
Cdd:cd01081  157 ---IEDLRLRVPASKVLPLDDLLPPTGELEVPGEEDFRLGRPLGG--------------GELDDCFLLLGNDAGTAEARL 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488215647 261 TSPDKRIQVDIATDASSVVIFTANFGtetpemrnrklaHHGGITFETQT-APGAERFSAFGSIHLKAGSvfETVTE 335
Cdd:cd01081  220 EDPDSRISVEFETGWPFWQVYTGDGG------------RRGSVAIEPMTsAPDAFFNNNGGLITLKPPG--ETRTF 281
Aldose_epim_Ec_YihR cd09022
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ...
 27-333 3.35e-25

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: 102.65  E-value: 3.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  27 ISDLGARIVSLKSNDRELVLGFDtaeeyieKDPYIGASIGRT----AGRIENGRFSLNGKTYQLA-TDPKTGHNLHGgap 101
Cdd:cd09022    5 VTEVGAGLRSLTVGGRDLVEPYP-------ADEVPPGAAGQVlapwPNRIADGRYTFDGVEHQLPiTEPERGNAIHG--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 102 gfeLKKWSYVILNGENEASVIFTTTSPDgEHGFPGTMDVEIRYTLTKDNI-WRVTSRGTSDQDTLFNPTNHVYFnLTGDA 180
Cdd:cd09022   75 ---LVRWADWQLVEHTDSSVTLRTRIPP-QPGYPFTLELTVTYELDDDGLtVTLTATNVGDEPAPFGVGFHPYL-SAGGA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 181 sqSIDQHELWLNSEAYapLRTDS--IPIGVkENAAGSAFDFQIPKKLASVFasdldqknlvdgIDHPFF-LKETGLGKEA 257
Cdd:cd09022  150 --PLDECTLTLPADTW--LPVDErlLPTGT-EPVAGTPYDFRTGRRLGGTA------------LDTAFTdLTRDADGRAR 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 258 ARLTSPDKRiQVDIATDAS--SVVIFTANfgTETPEMRNRKLAhhggitFETQTAPGaerfSAFGS----IHLKAGSVFE 331
Cdd:cd09022  213 ARLTGPDGR-GVELWADESfpWVQVFTAD--TLPPPGRRRGLA------VEPMTCPP----NAFNSgtdlIVLAPGETHT 279


                 ..
gi 488215647 332 TV 333
Cdd:cd09022  280 AS 281
PTZ00485 PTZ00485
aldolase 1-epimerase; Provisional
 8-302 1.06e-24

aldolase 1-epimerase; Provisional


Pssm-ID: 240435  Cd Length: 376  Bit Score: 103.16  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647   8 FGQGyHLITLENkNKLALSISDLGARIVSLK----SNDR--ELVLGFDTAEEYIEKDP-YIGASIGRTAGRIENGRFSLN 80
Cdd:PTZ00485  10 YGYD-KLVWLET-DRLKVGLTNYAASVASIQvyhpADNKwiEVNCGYPKNPEEAYADPdYMGATVGRCAGRVAGGVFTLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  81 GKTYQlaTDPKTG-HNLHGGAPGFELKKWSYVILNGENEASVIFTTTSPDGEHGFPGTMDVEIRYTL--TKDNIWRVTSR 157
Cdd:PTZ00485  88 GVKYY--TQKNRGeNTCHCGDDAYHKKHWGMKLIETANVIGVRFNYTSPHMENGFPGELVSKVTYSIerSKPNVLKTIYD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 158 G----TSDQD-TLFNPTNHVYFNLTG------------DASQSIDQHelWLNSEAYAPLRTD--SIPIGVKENAAGSAFD 218
Cdd:PTZ00485 166 SyipeTSPADaTPVNIFNHAYWNLNGiperngkknavwVQPESVRNH--WLRVPASRVAEADrmAIPTGEFLSVEGTGLD 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 219 FqipkKLASVFASDLDQKNLVD----GIDHPFFLK--ETGLGKEAARLTSPDKRIQVDIATDASSVVIFTANfgtetpem 292
Cdd:PTZ00485 244 F----RQGRVIGDCIDDVALLDrdpcGYDHPLAIDgwEKGKLMLHAEAKSPVTNICMKVYSTFPCMWVYTAN-------- 311

                        330
                 ....*....|
gi 488215647 293 rNRKLAHHGG 302
Cdd:PTZ00485 312 -NKPLPASGG 320
PRK15172 PRK15172
aldose-1-epimerase;
71-327 2.25e-06

aldose-1-epimerase;


Pssm-ID: 237918  Cd Length: 300  Bit Score: 48.66  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  71 RIENGRFSLNGKTYQLATDPKTGHN-LHGgapgfeLKKWSYVILNGENEASVIFTTTSPDgEHGFPGTMDVEIRYTLTKD 149
Cdd:PRK15172  65 RIANGCYRYQGQEYQLPINEHVSKAaIHG------LLAWRDWQISELTATSVTLTAFLPP-SYGYPFMLASQVIYSLDAA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 150 NIWRVTSRGTS--DQDTLFNPTNHVYfnLTGDAsQSIDQHELWLNSEAYAPLRTDSIPiGVKENAAGSAFDFQIPKKLAS 227
Cdd:PRK15172 138 TGLSVEIASQNigDVPAPYGVGIHPY--LTCNL-TSVDEYLLQLPANQVLAVDEHANP-TTLHHVDELDLDFSQAKKIAA 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 228 VfasdldqknlvdGIDHPFflkETGLGKEAARLTSPDKRIQVDIATDASSVVIFTAnfgtetpEMRNRKlahhgGITFET 307
Cdd:PRK15172 214 T------------KIDHTF---KTANDLWEVRITHPQQALSVSLCSDQPWLQIYSG-------EKLQRQ-----GLAVEP 266

                        250       260
                 ....*....|....*....|
gi 488215647 308 QTAPGAERFSAFGSIHLKAG 327
Cdd:PRK15172 267 MSCPPNAFNSGIDLLLLEPG 286
Aldose_epim_Ec_YphB cd09021
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ...
 23-282 8.43e-06

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: 46.52  E-value: 8.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  23 LALSISDLGARIVSLKSNDRELVLGFDTAEEyiekdpyiGASIGRTA--------GRIENGRFSLNGKTYQLATDP-KTG 93
Cdd:cd09021    1 RLVLAPELGGSIAALTSRGDPTPLLRPADPD--------AADALAMAcfplvpfsNRIRGGRFLFAGREVALPPNTaDEP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  94 HNLHGgaPGFeLKKWSyVILNGENEASVIFtttspDGEHGFPG-TMDVEIRYTLTKDNI---WRVTSRGTSDqdtlfNPT 169
Cdd:cd09021   73 HPLHG--DGW-RRPWQ-VVAASADSAELQL-----DHEADDPPwAYRAEQRFHLAGDGLsitLSVTNRGDRP-----MPA 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647 170 N---HVYFNLTGDASQSIDQHELWLNSEAYAPLRTDSIPigvkenaagSAFDFQIPKKLASVfasdldqknlvdGIDHPF 246
Cdd:cd09021  139 GlgfHPYFPRTPDTRLQADADGVWLEDEDHLPTGLRPHP---------PDWDFSQPRPLPDR------------WIDNCF 197

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488215647 247 flkeTGLGKeAARLTSPDKRIQVDIATDA--SSVVIFT 282
Cdd:cd09021  198 ----TGWDG-AALIWPPERGLALTIEADApfSHLVVYR 230
Aldose_epim_lacX cd09024
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ...
 15-161 4.61e-05

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: 44.46  E-value: 4.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488215647  15 ITLENkNKLALSISDLGARIVSLKSNDRELvlgfdtaeEYI-EKDPyigASIGRTA-------GRIENGRFSLNGKTYQL 86
Cdd:cd09024    1 ITLEN-EFLTVTISEHGAELTSIKDKKTGR--------EYLwQGDP---AYWGRHApilfpivGRLKDDTYTIDGKTYPM 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488215647  87 atdPKtghnlHGGAPGFELKkwsyVILNGENeaSVIFTTTS-PDGEHGFPGTMDVEIRYTLTKDNI---WRVTSRGTSD 161
Cdd:cd09024   69 ---PQ-----HGFARDMEFE----VVEQSDD--SVTFELTDnEETLKVYPFDFELRVTYTLEGNTLkvtYEVKNPDDKT 133
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH