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Conserved domains on  [gi|257796226|ref|NP_001158176|]
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N-acylglucosamine 2-epimerase isoform 2 [Mus musculus]

Protein Classification

AGE family epimerase/isomerase( domain architecture ID 10083298)

AGE (N-acylglucosamine 2-epimerase) family epimerase/isomerase with the common scaffold, alpha6/alpha6-barrel; similar to N-acylglucosamine 2-epimerase

CATH:  1.50.10.10
EC:  5.-.-.-
Gene Ontology:  GO:0016853
SCOP:  4001174

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AGE cd00249
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
15-394 2.59e-138

AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.


:

Pssm-ID: 238153  Cd Length: 384  Bit Score: 400.58  E-value: 2.59e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  15 ERETLQVWKKRVEQELDRVIAFWMEHSHDQEHGGFFTCLGRDGK--------------VWMYCRLYRsfeRFRRVELLDA 80
Cdd:cd00249    1 IAETLQELAQLAGWLLEDLLPFWLEAGLDREAGGFFECLDRDGQpfdtdrrlwlqarqVYCFAVAYL---LGWRPEWLEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  81 ARAGGEFLLRYARVAPPGKkCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWKVTGEVRYQSEAIEMMDQIIHWVREDPA 160
Cdd:cd00249   78 AEHGLEYLDRHGRDPDHGG-WYFALDQDGRPVDATKDLYSHAFALLAAAQAAKVGGDPEARALAEETIDLLERRFWEDHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 161 GLGRPQLSGALATEPMAVPMMLLSLVEQLGEEDEEltNMYAELGDWCVHRILQHVQRDGQVVLENVSEDGKE-LPGCLGR 239
Cdd:cd00249  157 GAFDEADPGTPPYRGSNPHMHLLEAMLAAYEATGE--QKYLDRADEIADLILDRFIDAESGVVREHFDEDWNpYNGDKGR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 240 HQNPGHTLEAGWFLLQYALRKGDPKLRmHIIDKFLLLPFHSGWDPEHGGLFY-FQDADGLcptqLEWNMKLWWPHSEAMI 318
Cdd:cd00249  235 HQEPGHQFEWAWLLLRIASRSGQAWLI-EKARRLFDLALALGWDPERGGLYYsFLDDGGL----LEDDDKRWWPQTEALK 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257796226 319 AFLMGYSDSGDPALLHLFYKVAEYTFRQFRDPEYGEWFGYLNQEGKVALTIKgGPFKGCFHVPRCLAMCEQILGAL 394
Cdd:cd00249  310 AALALAGITGDERYWQWYQRAWAYLWRHFIDPEYGLWFGYLDADGKVLLTPK-GPAKTFYHVVRALYEALDVLAAL 384
 
Name Accession Description Interval E-value
AGE cd00249
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
15-394 2.59e-138

AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.


Pssm-ID: 238153  Cd Length: 384  Bit Score: 400.58  E-value: 2.59e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  15 ERETLQVWKKRVEQELDRVIAFWMEHSHDQEHGGFFTCLGRDGK--------------VWMYCRLYRsfeRFRRVELLDA 80
Cdd:cd00249    1 IAETLQELAQLAGWLLEDLLPFWLEAGLDREAGGFFECLDRDGQpfdtdrrlwlqarqVYCFAVAYL---LGWRPEWLEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  81 ARAGGEFLLRYARVAPPGKkCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWKVTGEVRYQSEAIEMMDQIIHWVREDPA 160
Cdd:cd00249   78 AEHGLEYLDRHGRDPDHGG-WYFALDQDGRPVDATKDLYSHAFALLAAAQAAKVGGDPEARALAEETIDLLERRFWEDHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 161 GLGRPQLSGALATEPMAVPMMLLSLVEQLGEEDEEltNMYAELGDWCVHRILQHVQRDGQVVLENVSEDGKE-LPGCLGR 239
Cdd:cd00249  157 GAFDEADPGTPPYRGSNPHMHLLEAMLAAYEATGE--QKYLDRADEIADLILDRFIDAESGVVREHFDEDWNpYNGDKGR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 240 HQNPGHTLEAGWFLLQYALRKGDPKLRmHIIDKFLLLPFHSGWDPEHGGLFY-FQDADGLcptqLEWNMKLWWPHSEAMI 318
Cdd:cd00249  235 HQEPGHQFEWAWLLLRIASRSGQAWLI-EKARRLFDLALALGWDPERGGLYYsFLDDGGL----LEDDDKRWWPQTEALK 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257796226 319 AFLMGYSDSGDPALLHLFYKVAEYTFRQFRDPEYGEWFGYLNQEGKVALTIKgGPFKGCFHVPRCLAMCEQILGAL 394
Cdd:cd00249  310 AALALAGITGDERYWQWYQRAWAYLWRHFIDPEYGLWFGYLDADGKVLLTPK-GPAKTFYHVVRALYEALDVLAAL 384
YihS COG2942
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ...
23-391 8.46e-82

Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism];


Pssm-ID: 442185  Cd Length: 380  Bit Score: 255.96  E-value: 8.46e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  23 KKRVEQEL-DRVIAFWMEHSHDQEHGGFFTCLGRDGK---------------VWMYCRLYRsfeRFRRVELLDAARAGGE 86
Cdd:COG2942    1 ADWLRAELlDDLLPFWLPRSIDPEGGGFFGCLDDDGTpyddadkglvlqarqVWTFALAYL---LLGRPEYLELAEHGLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  87 FLLRYARvAPPGKKCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWKVTGEVRYQSEAIEMMDQIIHWVREDPAGLGRPQ 166
Cdd:COG2942   78 FLREHFR-DPEHGGWYWSLDADGKPLDDRKQAYGHAFALLALAEAYRATGDPEALELAKETFELLERRFWDPEHGGYAEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 167 LSGALATEP----MAVPM----MLLSLVEQLGEEDeeltnmYAELGDWCVHRILQH-VQRDGQVVLENVSEDGKELPGCL 237
Cdd:COG2942  157 FDRDWSPLRpyrgQNAHMhlleALLALYEATGDER------WLERAEEIADLILTRfADPEGGRLLEHFDPDWSPDPDYN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 238 -GRHQNPGHTLEAGWFLLQYALRKGDPKLRMHIIDKFLLLPFHsGWDPEHGGLFYFQDADGlcptQLEWNMKLWWPHSEA 316
Cdd:COG2942  231 rPRGVSPGHDIEWAWLLLELAALLGDAWLLELARKLFDAALEY-GWDDERGGLYYELDPDG----KPVDDDKLWWVQAEA 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257796226 317 MIAFLMGYSDSGDPALLHLFYKVAEYTFRQFRDPEYGEWFGYLNQEGKVALTIKGGPFKGCFHVPRCLAMCEQIL 391
Cdd:COG2942  306 LVAALLLYQLTGDERYLDWYRRLWDYIWAHFIDHEYGEWFGELDRDGEPLTDLKGGPWKGDYHNPRALLEVLRRL 380
GlcNAc_2-epim pfam07221
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
48-372 1.75e-37

N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of eukaryotic and bacterial N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase) enzymes (EC:5.1.3.8) approximately 500 residues long. This converts N-acyl-D-glucosamine to N-acyl-D-mannosamine.


Pssm-ID: 399891  Cd Length: 347  Bit Score: 139.07  E-value: 1.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226   48 GFFTCLGRDGK---------------VWMYCRLYRsferFRRVELLDAARAGGEFLLRYARVAPPGKKcaFVLTRDGRPV 112
Cdd:pfam07221   1 GFFGCLDADGKiddadrrhiwlqarqVYCFAMAAL----LGRPGWLDAADHGLAYLEGVYRDGEHGGW--YWALRDGGVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  113 KVQRTIFSECFYTMAMNELwKVTGEVRYQSEAIEMMDQIIHWVREDPAGLGRPQLSGA-LATEPMAVPMM-----LLSLV 186
Cdd:pfam07221  75 DASKDAYDHAFALLAAASA-LAAGNPEAKDLLDDTLAVLEKHFWEPLHGGAREEFDRPfSLPYRGQNPNMhlteaMLALY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  187 EQLGEedeeltNMYAELGDWCVHRILQHVQR--DGQVVlENVSEDGKELPGCLGRHQ------NPGHTLEAGWFLLQYAL 258
Cdd:pfam07221 154 EATGD------PRWLDRAERIADLAIHRFADanSGRVR-EHFDEDWNPDPDYNGDDCfrpygtTPGHQFEWAWLLLRLAL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  259 --RKGDPKLrmhiIDKFLLLPFHS---GWDPEHGGLFYFQDADGlCPTQLEwnmKLWWPHSEAMIAFLMGYSDSGDPALL 333
Cdd:pfam07221 227 laRRRPADW----IEKARDLFETAladGWDPDRGGLVYTLDWNG-KPVDDD---RLHWPQTEALAAAAALAQRTGEARYW 298
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 257796226  334 HLFYKVAEYTFRQFRDPEYGEWFGYLNQEGKVALTIKGG 372
Cdd:pfam07221 299 DWYRRAWDYLWRHFIDPEYGSWFDELDADGEVALPLPAG 337
 
Name Accession Description Interval E-value
AGE cd00249
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
15-394 2.59e-138

AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.


Pssm-ID: 238153  Cd Length: 384  Bit Score: 400.58  E-value: 2.59e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  15 ERETLQVWKKRVEQELDRVIAFWMEHSHDQEHGGFFTCLGRDGK--------------VWMYCRLYRsfeRFRRVELLDA 80
Cdd:cd00249    1 IAETLQELAQLAGWLLEDLLPFWLEAGLDREAGGFFECLDRDGQpfdtdrrlwlqarqVYCFAVAYL---LGWRPEWLEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  81 ARAGGEFLLRYARVAPPGKkCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWKVTGEVRYQSEAIEMMDQIIHWVREDPA 160
Cdd:cd00249   78 AEHGLEYLDRHGRDPDHGG-WYFALDQDGRPVDATKDLYSHAFALLAAAQAAKVGGDPEARALAEETIDLLERRFWEDHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 161 GLGRPQLSGALATEPMAVPMMLLSLVEQLGEEDEEltNMYAELGDWCVHRILQHVQRDGQVVLENVSEDGKE-LPGCLGR 239
Cdd:cd00249  157 GAFDEADPGTPPYRGSNPHMHLLEAMLAAYEATGE--QKYLDRADEIADLILDRFIDAESGVVREHFDEDWNpYNGDKGR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 240 HQNPGHTLEAGWFLLQYALRKGDPKLRmHIIDKFLLLPFHSGWDPEHGGLFY-FQDADGLcptqLEWNMKLWWPHSEAMI 318
Cdd:cd00249  235 HQEPGHQFEWAWLLLRIASRSGQAWLI-EKARRLFDLALALGWDPERGGLYYsFLDDGGL----LEDDDKRWWPQTEALK 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257796226 319 AFLMGYSDSGDPALLHLFYKVAEYTFRQFRDPEYGEWFGYLNQEGKVALTIKgGPFKGCFHVPRCLAMCEQILGAL 394
Cdd:cd00249  310 AALALAGITGDERYWQWYQRAWAYLWRHFIDPEYGLWFGYLDADGKVLLTPK-GPAKTFYHVVRALYEALDVLAAL 384
YihS COG2942
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ...
23-391 8.46e-82

Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism];


Pssm-ID: 442185  Cd Length: 380  Bit Score: 255.96  E-value: 8.46e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  23 KKRVEQEL-DRVIAFWMEHSHDQEHGGFFTCLGRDGK---------------VWMYCRLYRsfeRFRRVELLDAARAGGE 86
Cdd:COG2942    1 ADWLRAELlDDLLPFWLPRSIDPEGGGFFGCLDDDGTpyddadkglvlqarqVWTFALAYL---LLGRPEYLELAEHGLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  87 FLLRYARvAPPGKKCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWKVTGEVRYQSEAIEMMDQIIHWVREDPAGLGRPQ 166
Cdd:COG2942   78 FLREHFR-DPEHGGWYWSLDADGKPLDDRKQAYGHAFALLALAEAYRATGDPEALELAKETFELLERRFWDPEHGGYAEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 167 LSGALATEP----MAVPM----MLLSLVEQLGEEDeeltnmYAELGDWCVHRILQH-VQRDGQVVLENVSEDGKELPGCL 237
Cdd:COG2942  157 FDRDWSPLRpyrgQNAHMhlleALLALYEATGDER------WLERAEEIADLILTRfADPEGGRLLEHFDPDWSPDPDYN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226 238 -GRHQNPGHTLEAGWFLLQYALRKGDPKLRMHIIDKFLLLPFHsGWDPEHGGLFYFQDADGlcptQLEWNMKLWWPHSEA 316
Cdd:COG2942  231 rPRGVSPGHDIEWAWLLLELAALLGDAWLLELARKLFDAALEY-GWDDERGGLYYELDPDG----KPVDDDKLWWVQAEA 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257796226 317 MIAFLMGYSDSGDPALLHLFYKVAEYTFRQFRDPEYGEWFGYLNQEGKVALTIKGGPFKGCFHVPRCLAMCEQIL 391
Cdd:COG2942  306 LVAALLLYQLTGDERYLDWYRRLWDYIWAHFIDHEYGEWFGELDRDGEPLTDLKGGPWKGDYHNPRALLEVLRRL 380
GlcNAc_2-epim pfam07221
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
48-372 1.75e-37

N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of eukaryotic and bacterial N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase) enzymes (EC:5.1.3.8) approximately 500 residues long. This converts N-acyl-D-glucosamine to N-acyl-D-mannosamine.


Pssm-ID: 399891  Cd Length: 347  Bit Score: 139.07  E-value: 1.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226   48 GFFTCLGRDGK---------------VWMYCRLYRsferFRRVELLDAARAGGEFLLRYARVAPPGKKcaFVLTRDGRPV 112
Cdd:pfam07221   1 GFFGCLDADGKiddadrrhiwlqarqVYCFAMAAL----LGRPGWLDAADHGLAYLEGVYRDGEHGGW--YWALRDGGVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  113 KVQRTIFSECFYTMAMNELwKVTGEVRYQSEAIEMMDQIIHWVREDPAGLGRPQLSGA-LATEPMAVPMM-----LLSLV 186
Cdd:pfam07221  75 DASKDAYDHAFALLAAASA-LAAGNPEAKDLLDDTLAVLEKHFWEPLHGGAREEFDRPfSLPYRGQNPNMhlteaMLALY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  187 EQLGEedeeltNMYAELGDWCVHRILQHVQR--DGQVVlENVSEDGKELPGCLGRHQ------NPGHTLEAGWFLLQYAL 258
Cdd:pfam07221 154 EATGD------PRWLDRAERIADLAIHRFADanSGRVR-EHFDEDWNPDPDYNGDDCfrpygtTPGHQFEWAWLLLRLAL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257796226  259 --RKGDPKLrmhiIDKFLLLPFHS---GWDPEHGGLFYFQDADGlCPTQLEwnmKLWWPHSEAMIAFLMGYSDSGDPALL 333
Cdd:pfam07221 227 laRRRPADW----IEKARDLFETAladGWDPDRGGLVYTLDWNG-KPVDDD---RLHWPQTEALAAAAALAQRTGEARYW 298
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 257796226  334 HLFYKVAEYTFRQFRDPEYGEWFGYLNQEGKVALTIKGG 372
Cdd:pfam07221 299 DWYRRAWDYLWRHFIDPEYGSWFDELDADGEVALPLPAG 337
 
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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