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Conserved domains on  [gi|755545286|ref|XP_011242790|]
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fructose-1,6-bisphosphatase 1 isoform X1 [Mus musculus]

Protein Classification

fructose-1,6-bisphosphatase (domain architecture ID 10086071)

class 1 fructose-1,6-bisphosphatase I catalyzes the conversion of D-fructose 1,6-bisphosphate to D-fructose 6-phosphate in gluconeogenesis and the Calvin cycle, which are both anabolic pathways

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
1-248 2.31e-155

Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway. The alignment model also includes chloroplastic FBPases and sedoheptulose-1,7-biphosphatases that play a role in pentose phosphate pathway (Calvin cycle).


:

Pssm-ID: 238214  Cd Length: 315  Bit Score: 434.29  E-value: 2.31e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   1 MLKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAG 80
Cdd:cd00354   68 ALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  81 YALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGAR 160
Cdd:cd00354  148 YALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLR 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 161 YVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSED 240
Cdd:cd00354  228 YIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEE 307

                 ....*...
gi 755545286 241 VQEFLEIY 248
Cdd:cd00354  308 VERVEEYL 315
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
1-248 2.31e-155

Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway. The alignment model also includes chloroplastic FBPases and sedoheptulose-1,7-biphosphatases that play a role in pentose phosphate pathway (Calvin cycle).


Pssm-ID: 238214  Cd Length: 315  Bit Score: 434.29  E-value: 2.31e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   1 MLKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAG 80
Cdd:cd00354   68 ALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  81 YALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGAR 160
Cdd:cd00354  148 YALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLR 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 161 YVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSED 240
Cdd:cd00354  228 YIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEE 307

                 ....*...
gi 755545286 241 VQEFLEIY 248
Cdd:cd00354  308 VERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
1-254 1.69e-130

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 372.22  E-value: 1.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   1 MLKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAG 80
Cdd:PLN02262  87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  81 YALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGAR 160
Cdd:PLN02262 167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 161 YVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSED 240
Cdd:PLN02262 247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326
                        250
                 ....*....|....
gi 755545286 241 VQEFLEIYRKHKAK 254
Cdd:PLN02262 327 VEEIKALYAAEAAK 340
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
2-252 2.19e-114

Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 223236  Cd Length: 326  Bit Score: 330.81  E-value: 2.19e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   2 LKSSYATCVLVSEENTNAIIIEPEKrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDePSEKDALQPGRDLVAAGY 81
Cdd:COG0158   77 LKARGNVAGIASEEEDEPVTFPENN-GSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  82 ALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLqRKKFPPDGSA--PYGA 159
Cdd:COG0158  155 VVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYI-KDCFAEDKGTrrPYNM 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 160 RYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSE 239
Cdd:COG0158  234 RYIGSMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKE 313
                        250
                 ....*....|...
gi 755545286 240 DVQEFLEIYRKHK 252
Cdd:COG0158  314 EVEKLERFIKEFP 326
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
1-114 1.28e-65

Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this protein family.


Pssm-ID: 395249  Cd Length: 189  Bit Score: 202.25  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286    1 MLKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAG 80
Cdd:pfam00316  75 ALKASGIVAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAG 154
                          90       100       110
                  ....*....|....*....|....*....|....
gi 755545286   81 YALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVD 114
Cdd:pfam00316 155 YVVYGSSTMLVLTTGCGVHGFTLDPSLGEFILTH 188
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
1-248 2.31e-155

Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway. The alignment model also includes chloroplastic FBPases and sedoheptulose-1,7-biphosphatases that play a role in pentose phosphate pathway (Calvin cycle).


Pssm-ID: 238214  Cd Length: 315  Bit Score: 434.29  E-value: 2.31e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   1 MLKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAG 80
Cdd:cd00354   68 ALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  81 YALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGAR 160
Cdd:cd00354  148 YALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLR 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 161 YVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSED 240
Cdd:cd00354  228 YIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEE 307

                 ....*...
gi 755545286 241 VQEFLEIY 248
Cdd:cd00354  308 VERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
1-254 1.69e-130

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 372.22  E-value: 1.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   1 MLKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAG 80
Cdd:PLN02262  87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  81 YALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGAR 160
Cdd:PLN02262 167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 161 YVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSED 240
Cdd:PLN02262 247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326
                        250
                 ....*....|....
gi 755545286 241 VQEFLEIYRKHKAK 254
Cdd:PLN02262 327 VEEIKALYAAEAAK 340
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
2-252 2.17e-124

class 1 fructose-bisphosphatase;


Pssm-ID: 236458  Cd Length: 327  Bit Score: 356.47  E-value: 2.17e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   2 LKSSYATCVLVSEENTNAIIIePEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKStDEPSEKDALQPGRDLVAAGY 81
Cdd:PRK09293  78 LKARGHVAGLASEEEDEIVPI-PENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGY 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  82 ALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAIN---EYLQRKKFPpdGSAPYG 158
Cdd:PRK09293 156 VLYGPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKkyiELLAGKDGP--RGRPYN 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 159 ARYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSS 238
Cdd:PRK09293 234 MRYIGSMVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSK 313
                        250
                 ....*....|....
gi 755545286 239 EDVQEFLEIYRKHK 252
Cdd:PRK09293 314 EEVERVEEYHAEAP 327
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
2-252 2.19e-114

Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 223236  Cd Length: 326  Bit Score: 330.81  E-value: 2.19e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   2 LKSSYATCVLVSEENTNAIIIEPEKrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDePSEKDALQPGRDLVAAGY 81
Cdd:COG0158   77 LKARGNVAGIASEEEDEPVTFPENN-GSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  82 ALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLqRKKFPPDGSA--PYGA 159
Cdd:COG0158  155 VVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYI-KDCFAEDKGTrrPYNM 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 160 RYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSE 239
Cdd:COG0158  234 RYIGSMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKE 313
                        250
                 ....*....|...
gi 755545286 240 DVQEFLEIYRKHK 252
Cdd:COG0158  314 EVEKLERFIKEFP 326
PLN02542 PLN02542
fructose-1,6-bisphosphatase
2-248 6.65e-80

fructose-1,6-bisphosphatase


Pssm-ID: 215298  Cd Length: 412  Bit Score: 245.94  E-value: 6.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   2 LKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYR-----------KKSTDEPSEK--- 67
Cdd:PLN02542 151 LRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSpndecladigdDSTLDSVEQRciv 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  68 DALQPGRDLVAAGYALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRK 147
Cdd:PLN02542 231 NVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDL 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 148 KFPPDGSAPYGARYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEI 227
Cdd:PLN02542 311 KDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEI 390
                        250       260
                 ....*....|....*....|.
gi 755545286 228 HQKAPVVMGSSEDVqEFLEIY 248
Cdd:PLN02542 391 HQRVPLYIGSVEEV-EKLEKY 410
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
2-248 2.21e-75

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337  Cd Length: 351  Bit Score: 232.38  E-value: 2.21e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   2 LKSSYATCVLVSEENTNAIIIEPEkrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKS------TDEPSEKDALQPGRD 75
Cdd:PLN02628  94 LRNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVeadhlpVEEKAQLNVLQRGSR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  76 LVAAGYALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYL----QRKkfpp 151
Cdd:PLN02628 172 LVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIdtvrQGK---- 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 152 dGSAP--YGARYVGSMVADIHRTLVYGGIFLypankkSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQ 229
Cdd:PLN02628 248 -GQYPkkYSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQ 320
                        250
                 ....*....|....*....
gi 755545286 230 KAPVVMGSSEDVQEfLEIY 248
Cdd:PLN02628 321 RLPLFLGSSEDVLE-LESY 338
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
1-114 1.28e-65

Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this protein family.


Pssm-ID: 395249  Cd Length: 189  Bit Score: 202.25  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286    1 MLKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAG 80
Cdd:pfam00316  75 ALKASGIVAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAG 154
                          90       100       110
                  ....*....|....*....|....*....|....
gi 755545286   81 YALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVD 114
Cdd:pfam00316 155 YVVYGSSTMLVLTTGCGVHGFTLDPSLGEFILTH 188
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
122-248 1.24e-62

Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of Fructose-1-6-bisphosphatase enzymes. According to ECOD this domain has a Rossmann-like fold.


Pssm-ID: 408683 [Multi-domain]  Cd Length: 125  Bit Score: 192.05  E-value: 1.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  122 KGNIYSLNEGYAKDFDPAINEYLQRKKFppdGSAPYGARYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPI 201
Cdd:pfam18913   1 EGKIYAINEGNARHWNAPYRAYIDDLKS---GGKGYTLRYVGSMVADVHRILLKGGIFLYPADKRAPNGKLRLLYECAPL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 755545286  202 AYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEFLEIY 248
Cdd:pfam18913  78 AFLIEQAGGKASDGKQRILDIVPDSLHQRTPIFLGSREEVERVEAYL 124
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
2-246 8.22e-38

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256  Cd Length: 304  Bit Score: 134.09  E-value: 8.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   2 LKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYrkkstdePSEKDALQPGRDLVAAGY 81
Cdd:PLN02462  66 LKYSHVCKYACSEEVPEVQDMGGPVEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAM 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  82 ALYGSATMLVLAMDCGVNCFmldpsigEFIMVDRDVKMKKKGNIySLNEGyaKDFDPA--------------INEYLQRK 147
Cdd:PLN02462 139 GIYGPRTTYVVALKDGPGTH-------EFLLLDDGKWQHVKETT-EIGEG--KIFSPGnlratfdnpgyeklINYYVSEK 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286 148 kfppdgsapYGARYVGSMVADIHRTLVY-GGIFLYPANKKSPSgKLRLLYECNPIAYVMEKAGGLATTGDKD--ILDIVP 224
Cdd:PLN02462 209 ---------YTLRYTGGMVPDVYQIIVKeKGVFTNVTSPKSKA-KLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQI 278
                        250       260
                 ....*....|....*....|..
gi 755545286 225 TEIHQKAPVVMGSSEDVQEFLE 246
Cdd:PLN02462 279 NNLDQRTQVAYGSKNEVIRFEE 300
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
1-215 5.98e-21

FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.


Pssm-ID: 238814 [Multi-domain]  Cd Length: 184  Bit Score: 86.68  E-value: 5.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   1 MLKSSYATCVLVSEENtNAIIIEPEKRGKYVVCFDPLDGSSN-IDCLVSIGTIFGIYrkkstdepsekdalqpgrdlvaa 79
Cdd:cd01636   51 MLKSSFPDVKIVGEES-GVAEEVMGRRDEYTWVIDPIDGTKNfINGLPFVAVVIAVY----------------------- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  80 gyalygsatmlvlamdcgvncfmldpsigefimvdrdvkmkkkgNIYSLNEGYAKDFDPaineylqrKKFPPDGSAPYGA 159
Cdd:cd01636  107 --------------------------------------------VILILAEPSHKRVDE--------KKAELQLLAVYRI 134
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755545286 160 RYVGSMVADIHRTLV-YGGIFLYPANKkspsgklRLLYECNPIAYVMEKAGGLATTG 215
Cdd:cd01636  135 RIVGSAVAKMCLVALgLADIYYEPGGK-------RRAWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
1-216 2.27e-13

Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others.


Pssm-ID: 238815 [Multi-domain]  Cd Length: 238  Bit Score: 67.34  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286   1 MLKSSYATCVLVSEENTNAIIiepEKRGKYVVCFDPLDGSSN-IDCLVSIGTIFGIYRKKSTdepsekdalqpgrdlVAA 79
Cdd:cd01637   49 VLKALFPDDGILGEEGGGSGN---VSDGGRVWVIDPIDGTTNfVAGLPNFAVSIALYEDGKP---------------VLG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755545286  80 GYALYGsATMLVLAM-DCGVNCFMLDPSIgefimvdrdVKMKKKGNIYSLNEGYAKDFDPAineylqrKKFPPDGSAPYG 158
Cdd:cd01637  111 VIYDPM-LDELYYAGrGKGAFLNGKKLPL---------SKDTPLNDALLSTNASMLRSNRA-------AVLASLVNRALG 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755545286 159 ARYVGSMVADIHRTLVY-GGIFLYPANKkspsgklrlLYECNPIAYVMEKAGGLATTGD 216
Cdd:cd01637  174 IRIYGSAGLDLAYVAAGrLDAYLSSGLN---------PWDYAAGALIVEEAGGIVTDLD 223
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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