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Conserved domains on  [gi|545559846|ref|XP_855355|]
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N-acylglucosamine 2-epimerase [Canis lupus familiaris]

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 ...
14-407 2.72e-142

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: 411.37  E-value: 2.72e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  14 EREALQAWKERVEQELDRVVAFWMEHSHDQEHGGFFTCLGRDGQVYDDLKYVWLQGRQVWMYCRLYRKFERfrsPELLDS 93
Cdd:cd00249    1 IAETLQELAQLAGWLLEDLLPFWLEAGLDREAGGFFECLDRDGQPFDTDRRLWLQARQVYCFAVAYLLGWR---PEWLEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  94 AKAGGEFLLRFARVAPPGKkCAFVLTRDGQPIKVQRTIFSECFYTMAMNELWRVTGEARYQNEAVEMMDQIAYWVREDPS 173
Cdd:cd00249   78 AEHGLEYLDRHGRDPDHGG-WYFALDQDGRPVDATKDLYSHAFALLAAAQAAKVGGDPEARALAEETIDLLERRFWEDHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 174 GLGRPCLPGAPASESMAVPMMLLNLVDQLGEADEElaGTYAELGDWCAQRILQHVQRDGQAVLENVSEDGGE-LSGCLGR 252
Cdd:cd00249  157 GAFDEADPGTPPYRGSNPHMHLLEAMLAAYEATGE--QKYLDRADEIADLILDRFIDAESGVVREHFDEDWNpYNGDKGR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 253 HQNPGHALEAGWFLLRHAIRKGDPELRArVIDKFLLLPFRSGWDPDHGGLFY-FQDADGLcptqLEWAMKLWWPHSEAMI 331
Cdd:cd00249  235 HQEPGHQFEWAWLLLRIASRSGQAWLIE-KARRLFDLALALGWDPERGGLYYsFLDDGGL----LEDDDKRWWPQTEALK 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545559846 332 AFLMGYSDSGDPTLLHLFYQVAEYTFRQFRDPEHGEWFGYLTREGKVALTIKgGPFKGCFHVPRCLAMCEEMLGAL 407
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 ...
14-407 2.72e-142

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: 411.37  E-value: 2.72e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  14 EREALQAWKERVEQELDRVVAFWMEHSHDQEHGGFFTCLGRDGQVYDDLKYVWLQGRQVWMYCRLYRKFERfrsPELLDS 93
Cdd:cd00249    1 IAETLQELAQLAGWLLEDLLPFWLEAGLDREAGGFFECLDRDGQPFDTDRRLWLQARQVYCFAVAYLLGWR---PEWLEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  94 AKAGGEFLLRFARVAPPGKkCAFVLTRDGQPIKVQRTIFSECFYTMAMNELWRVTGEARYQNEAVEMMDQIAYWVREDPS 173
Cdd:cd00249   78 AEHGLEYLDRHGRDPDHGG-WYFALDQDGRPVDATKDLYSHAFALLAAAQAAKVGGDPEARALAEETIDLLERRFWEDHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 174 GLGRPCLPGAPASESMAVPMMLLNLVDQLGEADEElaGTYAELGDWCAQRILQHVQRDGQAVLENVSEDGGE-LSGCLGR 252
Cdd:cd00249  157 GAFDEADPGTPPYRGSNPHMHLLEAMLAAYEATGE--QKYLDRADEIADLILDRFIDAESGVVREHFDEDWNpYNGDKGR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 253 HQNPGHALEAGWFLLRHAIRKGDPELRArVIDKFLLLPFRSGWDPDHGGLFY-FQDADGLcptqLEWAMKLWWPHSEAMI 331
Cdd:cd00249  235 HQEPGHQFEWAWLLLRIASRSGQAWLIE-KARRLFDLALALGWDPERGGLYYsFLDDGGL----LEDDDKRWWPQTEALK 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545559846 332 AFLMGYSDSGDPTLLHLFYQVAEYTFRQFRDPEHGEWFGYLTREGKVALTIKgGPFKGCFHVPRCLAMCEEMLGAL 407
Cdd:cd00249  310 AALALAGITGDERYWQWYQRAWAYLWRHFIDPEYGLWFGYLDADGKVLLTPK-GPAKTFYHVVRALYEALDVLAAL 384
YihS COG2942
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ...
22-404 2.07e-88

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


Pssm-ID: 442185  Cd Length: 380  Bit Score: 273.67  E-value: 2.07e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  22 KERVEQEL-DRVVAFWMEHSHDQEHGGFFTCLGRDGQVYDD-LKYVWLQGRQVWMYCRLYRKFERfrsPELLDSAKAGGE 99
Cdd:COG2942    1 ADWLRAELlDDLLPFWLPRSIDPEGGGFFGCLDDDGTPYDDaDKGLVLQARQVWTFALAYLLLGR---PEYLELAEHGLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 100 FLLRFARvAPPGKKCAFVLTRDGQPIKVQRTIFSECFYTMAMNELWRVTGEARYQNEAVEMMDQI--AYW------VRED 171
Cdd:COG2942   78 FLREHFR-DPEHGGWYWSLDADGKPLDDRKQAYGHAFALLALAEAYRATGDPEALELAKETFELLerRFWdpehggYAEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 172 PSGLGRPClpgaPASESMAVPMMLLNLVDQLGEADEElaGTYAELGDWCAQRILQH-VQRDGQAVLENVSEDGGELSGCL 250
Cdd:COG2942  157 FDRDWSPL----RPYRGQNAHMHLLEALLALYEATGD--ERWLERAEEIADLILTRfADPEGGRLLEHFDPDWSPDPDYN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 251 -GRHQNPGHALEAGWFLLRHAIRKGDPELRARVIDKFLLLpFRSGWDPDHGGLFYFQDADGlcptQLEWAMKLWWPHSEA 329
Cdd:COG2942  231 rPRGVSPGHDIEWAWLLLELAALLGDAWLLELARKLFDAA-LEYGWDDERGGLYYELDPDG----KPVDDDKLWWVQAEA 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545559846 330 MIAFLMGYSDSGDPTLLHLFYQVAEYTFRQFRDPEHGEWFGYLTREGKVALTIKGGPFKGCFHVPRCLAMCEEML 404
Cdd:COG2942  306 LVAALLLYQLTGDERYLDWYRRLWDYIWAHFIDHEYGEWFGELDRDGEPLTDLKGGPWKGDYHNPRALLEVLRRL 380
GlcNAc_2-epim pfam07221
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
47-385 2.21e-38

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: 141.77  E-value: 2.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846   47 GFFTCLGRDGQVYD-DLKYVWLQGRQVWMYCRLYRkFERfrsPELLDSAKAGGEFLLRFARVAPPGKKcaFVLTRDGQPI 125
Cdd:pfam07221   1 GFFGCLDADGKIDDaDRRHIWLQARQVYCFAMAAL-LGR---PGWLDAADHGLAYLEGVYRDGEHGGW--YWALRDGGVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  126 KVQRTIFSECFYTMAMNELWrVTGEARYQNEAVEMMDQIAYWVREDPSGLGRPCLPGAPASESMAV--PMMLLNLVDQLG 203
Cdd:pfam07221  75 DASKDAYDHAFALLAAASAL-AAGNPEAKDLLDDTLAVLEKHFWEPLHGGAREEFDRPFSLPYRGQnpNMHLTEAMLALY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  204 EADEElaGTYAELGDWCAQRILQHVQRDGQAVL-------ENVSEDGGELSGCLGRHQNPGHALEAGWFLLRHAIRKGdp 276
Cdd:pfam07221 154 EATGD--PRWLDRAERIADLAIHRFADANSGRVrehfdedWNPDPDYNGDDCFRPYGTTPGHQFEWAWLLLRLALLAR-- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  277 ELRARVIDKFLLLPFRS---GWDPDHGGLFYFQDADGlCPTQLEwamKLWWPHSEAMIAFLMGYSDSGDPTLLHLFYQVA 353
Cdd:pfam07221 230 RRPADWIEKARDLFETAladGWDPDRGGLVYTLDWNG-KPVDDD---RLHWPQTEALAAAAALAQRTGEARYWDWYRRAW 305
                         330       340       350
                  ....*....|....*....|....*....|..
gi 545559846  354 EYTFRQFRDPEHGEWFGYLTREGKVALTIKGG 385
Cdd:pfam07221 306 DYLWRHFIDPEYGSWFDELDADGEVALPLPAG 337
 
Name Accession Description Interval E-value
AGE cd00249
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
14-407 2.72e-142

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: 411.37  E-value: 2.72e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  14 EREALQAWKERVEQELDRVVAFWMEHSHDQEHGGFFTCLGRDGQVYDDLKYVWLQGRQVWMYCRLYRKFERfrsPELLDS 93
Cdd:cd00249    1 IAETLQELAQLAGWLLEDLLPFWLEAGLDREAGGFFECLDRDGQPFDTDRRLWLQARQVYCFAVAYLLGWR---PEWLEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  94 AKAGGEFLLRFARVAPPGKkCAFVLTRDGQPIKVQRTIFSECFYTMAMNELWRVTGEARYQNEAVEMMDQIAYWVREDPS 173
Cdd:cd00249   78 AEHGLEYLDRHGRDPDHGG-WYFALDQDGRPVDATKDLYSHAFALLAAAQAAKVGGDPEARALAEETIDLLERRFWEDHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 174 GLGRPCLPGAPASESMAVPMMLLNLVDQLGEADEElaGTYAELGDWCAQRILQHVQRDGQAVLENVSEDGGE-LSGCLGR 252
Cdd:cd00249  157 GAFDEADPGTPPYRGSNPHMHLLEAMLAAYEATGE--QKYLDRADEIADLILDRFIDAESGVVREHFDEDWNpYNGDKGR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 253 HQNPGHALEAGWFLLRHAIRKGDPELRArVIDKFLLLPFRSGWDPDHGGLFY-FQDADGLcptqLEWAMKLWWPHSEAMI 331
Cdd:cd00249  235 HQEPGHQFEWAWLLLRIASRSGQAWLIE-KARRLFDLALALGWDPERGGLYYsFLDDGGL----LEDDDKRWWPQTEALK 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545559846 332 AFLMGYSDSGDPTLLHLFYQVAEYTFRQFRDPEHGEWFGYLTREGKVALTIKgGPFKGCFHVPRCLAMCEEMLGAL 407
Cdd:cd00249  310 AALALAGITGDERYWQWYQRAWAYLWRHFIDPEYGLWFGYLDADGKVLLTPK-GPAKTFYHVVRALYEALDVLAAL 384
YihS COG2942
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ...
22-404 2.07e-88

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


Pssm-ID: 442185  Cd Length: 380  Bit Score: 273.67  E-value: 2.07e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  22 KERVEQEL-DRVVAFWMEHSHDQEHGGFFTCLGRDGQVYDD-LKYVWLQGRQVWMYCRLYRKFERfrsPELLDSAKAGGE 99
Cdd:COG2942    1 ADWLRAELlDDLLPFWLPRSIDPEGGGFFGCLDDDGTPYDDaDKGLVLQARQVWTFALAYLLLGR---PEYLELAEHGLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 100 FLLRFARvAPPGKKCAFVLTRDGQPIKVQRTIFSECFYTMAMNELWRVTGEARYQNEAVEMMDQI--AYW------VRED 171
Cdd:COG2942   78 FLREHFR-DPEHGGWYWSLDADGKPLDDRKQAYGHAFALLALAEAYRATGDPEALELAKETFELLerRFWdpehggYAEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 172 PSGLGRPClpgaPASESMAVPMMLLNLVDQLGEADEElaGTYAELGDWCAQRILQH-VQRDGQAVLENVSEDGGELSGCL 250
Cdd:COG2942  157 FDRDWSPL----RPYRGQNAHMHLLEALLALYEATGD--ERWLERAEEIADLILTRfADPEGGRLLEHFDPDWSPDPDYN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846 251 -GRHQNPGHALEAGWFLLRHAIRKGDPELRARVIDKFLLLpFRSGWDPDHGGLFYFQDADGlcptQLEWAMKLWWPHSEA 329
Cdd:COG2942  231 rPRGVSPGHDIEWAWLLLELAALLGDAWLLELARKLFDAA-LEYGWDDERGGLYYELDPDG----KPVDDDKLWWVQAEA 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545559846 330 MIAFLMGYSDSGDPTLLHLFYQVAEYTFRQFRDPEHGEWFGYLTREGKVALTIKGGPFKGCFHVPRCLAMCEEML 404
Cdd:COG2942  306 LVAALLLYQLTGDERYLDWYRRLWDYIWAHFIDHEYGEWFGELDRDGEPLTDLKGGPWKGDYHNPRALLEVLRRL 380
GlcNAc_2-epim pfam07221
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
47-385 2.21e-38

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: 141.77  E-value: 2.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846   47 GFFTCLGRDGQVYD-DLKYVWLQGRQVWMYCRLYRkFERfrsPELLDSAKAGGEFLLRFARVAPPGKKcaFVLTRDGQPI 125
Cdd:pfam07221   1 GFFGCLDADGKIDDaDRRHIWLQARQVYCFAMAAL-LGR---PGWLDAADHGLAYLEGVYRDGEHGGW--YWALRDGGVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  126 KVQRTIFSECFYTMAMNELWrVTGEARYQNEAVEMMDQIAYWVREDPSGLGRPCLPGAPASESMAV--PMMLLNLVDQLG 203
Cdd:pfam07221  75 DASKDAYDHAFALLAAASAL-AAGNPEAKDLLDDTLAVLEKHFWEPLHGGAREEFDRPFSLPYRGQnpNMHLTEAMLALY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  204 EADEElaGTYAELGDWCAQRILQHVQRDGQAVL-------ENVSEDGGELSGCLGRHQNPGHALEAGWFLLRHAIRKGdp 276
Cdd:pfam07221 154 EATGD--PRWLDRAERIADLAIHRFADANSGRVrehfdedWNPDPDYNGDDCFRPYGTTPGHQFEWAWLLLRLALLAR-- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545559846  277 ELRARVIDKFLLLPFRS---GWDPDHGGLFYFQDADGlCPTQLEwamKLWWPHSEAMIAFLMGYSDSGDPTLLHLFYQVA 353
Cdd:pfam07221 230 RRPADWIEKARDLFETAladGWDPDRGGLVYTLDWNG-KPVDDD---RLHWPQTEALAAAAALAQRTGEARYWDWYRRAW 305
                         330       340       350
                  ....*....|....*....|....*....|..
gi 545559846  354 EYTFRQFRDPEHGEWFGYLTREGKVALTIKGG 385
Cdd:pfam07221 306 DYLWRHFIDPEYGSWFDELDADGEVALPLPAG 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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