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Conserved domains on  [gi|1863409921|ref|XP_035020980|]
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fructose-1,6-bisphosphatase isozyme 2 [Hippoglossus stenolepis]

Protein Classification

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

class 1 fructose-1,6-bisphosphatase 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

CATH:  3.40.190.80|3.30.540.10
EC:  3.1.3.11
Gene Ontology:  GO:0042132|GO:0046872|GO:0016208
PubMed:  8816077
SCOP:  4002766

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, ...
 23-332 0e+00

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 [Multi-domain]  Cd Length: 315  Bit Score: 504.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  23 RQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYGTCCLVSEENA 102
Cdd:cd00354     5 LRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASEEEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 103 ELVITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISEGEPTEKDALQPGSSIVCAGYALYGSATLVALSTGAG 182
Cdd:cd00354    85 EPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLTLGQG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 183 LNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKYPEDGSPPYGARYVGSMVSDVHRTIAYGG 262
Cdd:cd00354   165 VHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRILVRGG 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 263 IFLYPASEKSPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVGSCDDVNDYLSF 332
Cdd:cd00354   245 IFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEY 314
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
 23-332 0e+00

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 [Multi-domain]  Cd Length: 315  Bit Score: 504.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  23 RQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYGTCCLVSEENA 102
Cdd:cd00354     5 LRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASEEEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 103 ELVITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISEGEPTEKDALQPGSSIVCAGYALYGSATLVALSTGAG 182
Cdd:cd00354    85 EPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLTLGQG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 183 LNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKYPEDGSPPYGARYVGSMVSDVHRTIAYGG 262
Cdd:cd00354   165 VHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRILVRGG 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 263 IFLYPASEKSPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVGSCDDVNDYLSF 332
Cdd:cd00354   245 IFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEY 314
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
 8-337 1.33e-168

Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1,6-bisphosphatase is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 439928 [Multi-domain]  Cd Length: 338  Bit Score: 472.29  E-value: 1.33e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921   8 DTDVWTLTRFILETGRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINML 87
Cdd:COG0158     1 MMKGTTLTQFLIEQQRRFPGATGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  88 QASYGTCCLVSEENAELV-ITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISEGEP-TEKDALQPGSSIVCAG 165
Cdd:COG0158    81 EWGGHVAAMASEEMDDPIpIPEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGGGPvTEEDFLQPGSEQVAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 166 YALYGSATLVALSTGAGLNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKYPEDGS--PPYG 243
Cdd:COG0158   161 YVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDECLAGKEGPrgRDFN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 244 ARYVGSMVSDVHRTIAYGGIFLYPASEK--SPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVG 321
Cdd:COG0158   241 MRWIGSLVADVHRILLRGGIFLYPADSRdgYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILG 320

                         330
                  ....*....|....*.
gi 1863409921 322 SCDDVNDYLSFVKKFP 337
Cdd:COG0158   321 SKEEVERVERYHAEPD 336
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
13-337 4.47e-157

class 1 fructose-bisphosphatase;


Pssm-ID: 236458 [Multi-domain]  Cd Length: 327  Bit Score: 442.75  E-value: 4.47e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  13 TLTRFILETGRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYG 92
Cdd:PRK09293    4 TLGEFLVEQQREFPHATGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  93 TCCLVSEENAELVITPKDkRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISeGEPTEKDALQPGSSIVCAGYALYGSA 172
Cdd:PRK09293   84 VAGLASEEEDEIVPIPEN-EGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLYGPS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 173 TLVALSTGAGLNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKyPEDGSP--PYGARYVGSM 250
Cdd:PRK09293  162 TMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIELLA-GKDGPRgrPYNMRYIGSM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 251 VSDVHRTIAYGGIFLYPASEKSPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVGSCDDVNDYL 330
Cdd:PRK09293  241 VADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERVE 320


                  ....*..
gi 1863409921 331 SFVKKFP 337
Cdd:PRK09293  321 EYHAEAP 327
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
 13-198 1.98e-86

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


Pssm-ID: 425601  Cd Length: 191  Bit Score: 258.16  E-value: 1.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  13 TLTRFILETGRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYG 92
Cdd:pfam00316   2 TLTRFIIEQQHEFPNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  93 TCCLVSEENAELVITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISE-GEP-TEKDALQPGSSIVCAGYALYG 170
Cdd:pfam00316  82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPtTIEDVLQPGNEQVAAGYAMYG 161

                         170       180
                  ....*....|....*....|....*...
gi 1863409921 171 SATLVALSTGAGLNFFMLDPAIGEFILT 198
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILT 189
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
 23-332 0e+00

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 [Multi-domain]  Cd Length: 315  Bit Score: 504.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  23 RQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYGTCCLVSEENA 102
Cdd:cd00354     5 LRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASEEEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 103 ELVITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISEGEPTEKDALQPGSSIVCAGYALYGSATLVALSTGAG 182
Cdd:cd00354    85 EPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLTLGQG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 183 LNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKYPEDGSPPYGARYVGSMVSDVHRTIAYGG 262
Cdd:cd00354   165 VHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRILVRGG 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 263 IFLYPASEKSPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVGSCDDVNDYLSF 332
Cdd:cd00354   245 IFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEY 314
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
 8-337 1.33e-168

Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1,6-bisphosphatase is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 439928 [Multi-domain]  Cd Length: 338  Bit Score: 472.29  E-value: 1.33e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921   8 DTDVWTLTRFILETGRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINML 87
Cdd:COG0158     1 MMKGTTLTQFLIEQQRRFPGATGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  88 QASYGTCCLVSEENAELV-ITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISEGEP-TEKDALQPGSSIVCAG 165
Cdd:COG0158    81 EWGGHVAAMASEEMDDPIpIPEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGGGPvTEEDFLQPGSEQVAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 166 YALYGSATLVALSTGAGLNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKYPEDGS--PPYG 243
Cdd:COG0158   161 YVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDECLAGKEGPrgRDFN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 244 ARYVGSMVSDVHRTIAYGGIFLYPASEK--SPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVG 321
Cdd:COG0158   241 MRWIGSLVADVHRILLRGGIFLYPADSRdgYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILG 320

                         330
                  ....*....|....*.
gi 1863409921 322 SCDDVNDYLSFVKKFP 337
Cdd:COG0158   321 SKEEVERVERYHAEPD 336
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
13-337 4.47e-157

class 1 fructose-bisphosphatase;


Pssm-ID: 236458 [Multi-domain]  Cd Length: 327  Bit Score: 442.75  E-value: 4.47e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  13 TLTRFILETGRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYG 92
Cdd:PRK09293    4 TLGEFLVEQQREFPHATGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  93 TCCLVSEENAELVITPKDkRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISeGEPTEKDALQPGSSIVCAGYALYGSA 172
Cdd:PRK09293   84 VAGLASEEEDEIVPIPEN-EGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLYGPS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 173 TLVALSTGAGLNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKyPEDGSP--PYGARYVGSM 250
Cdd:PRK09293  162 TMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIELLA-GKDGPRgrPYNMRYIGSM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 251 VSDVHRTIAYGGIFLYPASEKSPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVGSCDDVNDYL 330
Cdd:PRK09293  241 VADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERVE 320


                  ....*..
gi 1863409921 331 SFVKKFP 337
Cdd:PRK09293  321 EYHAEAP 327
PLN02262 PLN02262
fructose-1,6-bisphosphatase
 6-328 4.97e-150

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 425.37  E-value: 4.97e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921   6 AFDTDVWTLTRFILETGRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFIN 85
Cdd:PLN02262    7 AHRTDLMTITRFVLNEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  86 MLQASYGTCCLVSEENAELVITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISEGEPTEKDALQPGSSIVCAG 165
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 166 YALYGSATLVALSTGAGLNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKYPEDGSPPYGAR 245
Cdd:PLN02262  167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 246 YVGSMVSDVHRTIAYGGIFLYPASEKSPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVGSCDD 325
Cdd:PLN02262  247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326


                  ...
gi 1863409921 326 VND 328
Cdd:PLN02262  327 VEE 329
PLN02542 PLN02542
fructose-1,6-bisphosphatase
 10-333 8.48e-101

fructose-1,6-bisphosphatase


Pssm-ID: 215298 [Multi-domain]  Cd Length: 412  Bit Score: 302.95  E-value: 8.48e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  10 DVWTLTRFILETgRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQA 89
Cdd:PLN02542   75 EIQTLTTWLLKQ-EQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEVFSNCLRS 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  90 SYGTCCLVSEENAELVITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISE-----GEPTEKDAL--------- 155
Cdd:PLN02542  154 SGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDEcladiGDDSTLDSVeqrcivnvc 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 156 QPGSSIVCAGYALYGSATLVALSTGAGLNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEGYAKYFHPSMNEYLKHKKYP 235
Cdd:PLN02542  234 QPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKDP 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 236 EDGSPPYGARYVGSMVSDVHRTIAYGGIFLYPASEKSPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEGLHQR 315
Cdd:PLN02542  314 GPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQR 393

                         330
                  ....*....|....*...
gi 1863409921 316 VPFVVGSCDDVNDYLSFV 333
Cdd:PLN02542  394 VPLYIGSVEEVEKLEKYL 411
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
 5-332 2.17e-87

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337 [Multi-domain]  Cd Length: 351  Bit Score: 266.66  E-value: 2.17e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921   5 SAFDTDVWTLTRFIletGRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTG----DDVKKLDVLSN 80
Cdd:PLN02628   11 ARGAEGVCTLMEFL---GTEGSNVGDDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  81 DLFINMLQASYGTCCLVSEENaELVITPKDKrGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISEGE--PTEKDA---- 154
Cdd:PLN02628   88 EIILSSLRNSGKVAVMASEED-DAPIWIGDD-GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEADhlPVEEKAqlnv 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 155 LQPGSSIVCAGYALYGSATLVALSTGAGLNFFMLDPAIGEFILTERNVRIKPKGKIYSMNEgyAKYFH--PSMNEYLKHK 232
Cdd:PLN02628  166 LQRGSRLVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVND--ARYFDwpEGLRKYIDTV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 233 KYPEDGSPP-YGARYVGSMVSDVHRTIAYGGIFLypasekSPKGKLRLLYECNPIAFLVEQAGGLATTGSQRVLDVQPEG 311
Cdd:PLN02628  244 RQGKGQYPKkYSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVK 317

                         330       340
                  ....*....|....*....|.
gi 1863409921 312 LHQRVPFVVGSCDDVNDYLSF 332
Cdd:PLN02628  318 LHQRLPLFLGSSEDVLELESY 338
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
 13-198 1.98e-86

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


Pssm-ID: 425601  Cd Length: 191  Bit Score: 258.16  E-value: 1.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  13 TLTRFILETGRQAKGATGELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYG 92
Cdd:pfam00316   2 TLTRFIIEQQHEFPNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  93 TCCLVSEENAELVITPKDKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYKRISE-GEP-TEKDALQPGSSIVCAGYALYG 170
Cdd:pfam00316  82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPtTIEDVLQPGNEQVAAGYAMYG 161

                         170       180
                  ....*....|....*....|....*...
gi 1863409921 171 SATLVALSTGAGLNFFMLDPAIGEFILT 198
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILT 189
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
 206-334 5.10e-61

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: 436826 [Multi-domain]  Cd Length: 125  Bit Score: 190.90  E-value: 5.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 206 PKGKIYSMNEGYAKYFHPSMNEYLKHKKYPEdgspPYGARYVGSMVSDVHRTIAYGGIFLYPASEKSPKGKLRLLYECNP 285
Cdd:pfam18913   1 EEGKIYAINEGNARFWNAPYRAYIDDLVSGK----GYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGKLRLLYECAP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1863409921 286 IAFLVEQAGGLATTGSQRVLDVQPEGLHQRVPFVVGSCDDVNDYLSFVK 334
Cdd:pfam18913  77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAYLK 125
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
 31-333 9.05e-47

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256 [Multi-domain]  Cd Length: 304  Bit Score: 160.28  E-value: 9.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  31 ELTQLITAILTAIKAISSAVRKAglahLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYGTCCLVSEENAELVITPKD 110
Cdd:PLN02462   14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 111 KRGKYVVCFDPLDGSSNIDCLASIGTIFAIYkrisegePTEKDALQPGSSIVCAGYALYGSAT--LVALSTGAGLNFFML 188
Cdd:PLN02462   90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTtyVVALKDGPGTHEFLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 189 DPAiGEFILTERNVRIKPkGKIYSM--------NEGYAKYfhpsMNEYLKHKkypedgsppYGARYVGSMVSDVHRTIAY 260
Cdd:PLN02462  163 LDD-GKWQHVKETTEIGE-GKIFSPgnlratfdNPGYEKL----INYYVSEK---------YTLRYTGGMVPDVYQIIVK 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863409921 261 -GGIFLYPASEKSPkGKLRLLYECNPIAFLVEQAGGLATTGSQR--VLDVQPEGLHQRVPFVVGSCDDVNDYLSFV 333
Cdd:PLN02462  228 eKGVFTNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEVIRFEETL 302
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 39-300 7.21e-26

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: 101.70  E-value: 7.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  39 ILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYGTCCLVSEEnAELVITPKDKRGKYVVC 118
Cdd:cd01636     4 LCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEE-SGVAEEVMGRRDEYTWV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 119 FDPLDGSSN-IDCLASIGTIFAIYkrisegeptekdalqpgssivcagyalygsatlvalstgaglnffmldpaigefil 197
Cdd:cd01636    83 IDPIDGTKNfINGLPFVAVVIAVY-------------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 198 ternvrikpkgKIYSMNEGYAKYFHPsmneylkhKKYPEDGSPPYGARYVGSMVSDVHRTIA-YGGIFLYPAsekspkGK 276
Cdd:cd01636   107 -----------VILILAEPSHKRVDE--------KKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPG------GK 161

                         250       260
                  ....*....|....*....|....
gi 1863409921 277 LRlLYECNPIAFLVEQAGGLATTG 300
Cdd:cd01636   162 RR-AWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 49-299 9.38e-15

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: 72.73  E-value: 9.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  49 AVRKAGLAHLQGMAGSVNVT-----GDDVKKLDVLSNDLFINMLQASYGTCCLVSEENAElviTPKDKRGKYVVCFDPLD 123
Cdd:cd01637     7 AVREAGALILEAFGEELTVEtkkgdGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGG---SGNVSDGGRVWVIDPID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 124 GSSN-IDCLASIGTIFAIYKRiseGEPTEkdalqpgssivcagyalygsatlvalstgAGLNFFMLD------PAIGEFI 196
Cdd:cd01637    84 GTTNfVAGLPNFAVSIALYED---GKPVL-----------------------------GVIYDPMLDelyyagRGKGAFL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921 197 LTE--RNVRIKPKGKIYSMnegyakyFHPSMNEYLKHKKYPEDGSPPYGARYVGSMVSDVHRTIAY-GGIFLYPasekSP 273
Cdd:cd01637   132 NGKklPLSKDTPLNDALLS-------TNASMLRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGrLDAYLSS----GL 200

                         250       260
                  ....*....|....*....|....*.
gi 1863409921 274 KgklrlLYECNPIAFLVEQAGGLATT 299
Cdd:cd01637   201 N-----PWDYAAGALIVEEAGGIVTD 221
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 69-127 5.41e-05

Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles.


Pssm-ID: 238773 [Multi-domain]  Cd Length: 257  Bit Score: 43.91  E-value: 5.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1863409921  69 GDDVKKLDVLSNDLFINMLQaSYGTCCLVSEENAELVItpkDKRGKYVVCFDPLDGSSN 127
Cdd:cd01515    35 GTPTKLIDKVAEDAAIEILK-KLGSVNIVSEEIGVIDN---GDEPEYTVVLDPLDGTYN 89
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
69-127 1.55e-04

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 43.56  E-value: 1.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1863409921  69 GDDVKKLDVLSNDLFINMLQASYGTCcLVSEENAELVItpKDKRGKYVVCFDPLDGSSN 127
Cdd:PRK14076   39 GTPTKRIDLIAENIAINSLEKFCSGI-LISEEIGFKKI--GKNKPEYIFVLDPIDGTYN 94
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
46-127 4.42e-04

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 41.43  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  46 ISSAVRKAgLAHLQGM--AGSV---NVTGDDVKKLDVLSNDLFINMLQaSYGTCC-LVSEENAELVitpkDKRGKYVVCF 119
Cdd:PRK12676   13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLK-PLGRCVnIISEELGEIV----GNGPEYTVVL 86


                  ....*...
gi 1863409921 120 DPLDGSSN 127
Cdd:PRK12676   87 DPLDGTYN 94
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 35-127 1.91e-03

Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. These are Mg++ dependent phosphatases. Members in this family may have fructose-1,6-bisphosphatase and/or inositol-monophosphatase activity. Fructose-1,6-bisphosphatase catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway.


Pssm-ID: 238820 [Multi-domain]  Cd Length: 244  Bit Score: 39.35  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  35 LITAILTAIKAISSAVRKAGLAHLQGmagsvnVTGDDVKKLDVLSNDLFINMLQASYGTCCLVSEENAELVItpkdKRGK 114
Cdd:cd01642     5 LEKITKEIILLLNEKNRQGLVKLIRG------AGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRK----GSGE 74

                          90
                  ....*....|...
gi 1863409921 115 YVVCFDPLDGSSN 127
Cdd:cd01642    75 YIAVLDPLDGSTN 87
Inositol_P pfam00459
Inositol monophosphatase family;
31-135 3.16e-03

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 38.86  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863409921  31 ELTQLITAILTAIKAISSAVRKAGLAHLQGMAGSVNVTGDDVKKLDVLSNDLFINMLQASYGTCCLVSEE----NAELVI 106
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggakGDQTEL 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1863409921 107 TPKDkrgkYVVCFDPLDGSSN----IDCLA-SIG 135
Cdd:pfam00459  81 TDDG----PTWIIDPIDGTKNfvhgIPQFAvSIG 110
 
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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