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Conserved domains on  [gi|2280411784|ref|XP_049652213|]
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fructose-1,6-bisphosphatase 1 [Accipiter gentilis]

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, ...
 18-331 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: 535.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  18 VMEEGRRAKGTGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSFSTCVIVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  98 EENKDAVIVEAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVSLDEPSGKDALQPGRNLVAAGYALYGSATMLVLA 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 178 TSaGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITEYLKKKKFPEDGSSPYGGRYIGSMVADVHRT 257
Cdd:cd00354   161 LG-QGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRI 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2280411784 258 LVYGGIFLYPANSKSPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVLGSPDDVKEYLE 331
Cdd:cd00354   240 LVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEE 313
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
 18-331 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: 535.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  18 VMEEGRRAKGTGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSFSTCVIVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  98 EENKDAVIVEAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVSLDEPSGKDALQPGRNLVAAGYALYGSATMLVLA 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 178 TSaGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITEYLKKKKFPEDGSSPYGGRYIGSMVADVHRT 257
Cdd:cd00354   161 LG-QGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRI 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2280411784 258 LVYGGIFLYPANSKSPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVLGSPDDVKEYLE 331
Cdd:cd00354   240 LVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEE 313
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
 8-339 2.69e-162

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: 456.50  E-value: 2.69e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784   8 DTNVITMTRFVMEEGRRAKG-TGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINML 86
Cdd:COG0158     1 MMKGTTLTQFLIEQQRRFPGaTGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  87 KSSFSTCVIVSEENKDAVIV-EAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVS-LDEPSGKDALQPGRNLVAAG 164
Cdd:COG0158    81 EWGGHVAAMASEEMDDPIPIpEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSgGGPVTEEDFLQPGSEQVAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 165 YALYGSATMLVLATSaGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITEYLK--KKKFPEDGSSPY 242
Cdd:COG0158   161 YVLYGPSTMLVLTTG-NGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDecLAGKEGPRGRDF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 243 GGRYIGSMVADVHRTLVYGGIFLYPANSK--SPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVL 320
Cdd:COG0158   240 NMRWIGSLVADVHRILLRGGIFLYPADSRdgYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLIL 319

                         330
                  ....*....|....*....
gi 2280411784 321 GSPDDVKEYLEIVRKHSAK 339
Cdd:COG0158   320 GSKEEVERVERYHAEPDAS 338
PLN02262 PLN02262
fructose-1,6-bisphosphatase
 6-339 2.81e-159

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 448.87  E-value: 2.81e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784   6 AFDTNVITMTRFVM-EEGRRAKGTGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVIN 84
Cdd:PLN02262    7 AHRTDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  85 MLKSSFSTCVIVSEENKDAVIVEAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVSLDEPSGKDALQPGRNLVAAG 164
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 165 YALYGSATMLVLATsAGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITEYLKKKKFPEDGSSPYGG 244
Cdd:PLN02262  167 YCMYGSSCTLVLST-GGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 245 RYIGSMVADVHRTLVYGGIFLYPANSKSPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVLGSPD 324
Cdd:PLN02262  246 RYIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYD 325

                         330
                  ....*....|....*
gi 2280411784 325 DVKEYLEIVRKHSAK 339
Cdd:PLN02262  326 DVEEIKALYAAEAAK 340
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
 12-199 3.14e-97

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: 285.89  E-value: 3.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  12 ITMTRFVMEEGRRAK-GTGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSF 90
Cdd:pfam00316   1 ITLTRFIIEQQHEFPnATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  91 STCVIVSEENKDAVIVEAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVSL-DEPSGK-DALQPGRNLVAAGYALY 168
Cdd:pfam00316  81 IVKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPTTIeDVLQPGNEQVAAGYAMY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2280411784 169 GSATMLVLATsAGGVNCFMLDPAIGEFILVD 199
Cdd:pfam00316 161 GSSTMLVLTT-GCGVHGFTLDPSLGEFILTH 190
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
 18-331 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: 535.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  18 VMEEGRRAKGTGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSFSTCVIVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  98 EENKDAVIVEAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVSLDEPSGKDALQPGRNLVAAGYALYGSATMLVLA 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 178 TSaGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITEYLKKKKFPEDGSSPYGGRYIGSMVADVHRT 257
Cdd:cd00354   161 LG-QGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRI 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2280411784 258 LVYGGIFLYPANSKSPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVLGSPDDVKEYLE 331
Cdd:cd00354   240 LVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEE 313
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
 8-339 2.69e-162

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: 456.50  E-value: 2.69e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784   8 DTNVITMTRFVMEEGRRAKG-TGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINML 86
Cdd:COG0158     1 MMKGTTLTQFLIEQQRRFPGaTGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  87 KSSFSTCVIVSEENKDAVIV-EAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVS-LDEPSGKDALQPGRNLVAAG 164
Cdd:COG0158    81 EWGGHVAAMASEEMDDPIPIpEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSgGGPVTEEDFLQPGSEQVAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 165 YALYGSATMLVLATSaGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITEYLK--KKKFPEDGSSPY 242
Cdd:COG0158   161 YVLYGPSTMLVLTTG-NGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDecLAGKEGPRGRDF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 243 GGRYIGSMVADVHRTLVYGGIFLYPANSK--SPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVL 320
Cdd:COG0158   240 NMRWIGSLVADVHRILLRGGIFLYPADSRdgYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLIL 319

                         330
                  ....*....|....*....
gi 2280411784 321 GSPDDVKEYLEIVRKHSAK 339
Cdd:COG0158   320 GSKEEVERVERYHAEPDAS 338
PLN02262 PLN02262
fructose-1,6-bisphosphatase
 6-339 2.81e-159

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 448.87  E-value: 2.81e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784   6 AFDTNVITMTRFVM-EEGRRAKGTGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVIN 84
Cdd:PLN02262    7 AHRTDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  85 MLKSSFSTCVIVSEENKDAVIVEAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVSLDEPSGKDALQPGRNLVAAG 164
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 165 YALYGSATMLVLATsAGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITEYLKKKKFPEDGSSPYGG 244
Cdd:PLN02262  167 YCMYGSSCTLVLST-GGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 245 RYIGSMVADVHRTLVYGGIFLYPANSKSPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVLGSPD 324
Cdd:PLN02262  246 RYIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYD 325

                         330
                  ....*....|....*
gi 2280411784 325 DVKEYLEIVRKHSAK 339
Cdd:PLN02262  326 DVEEIKALYAAEAAK 340
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
12-336 9.52e-153

class 1 fructose-bisphosphatase;


Pssm-ID: 236458 [Multi-domain]  Cd Length: 327  Bit Score: 431.97  E-value: 9.52e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  12 ITMTRFVMEEGRRAKG-TGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSF 90
Cdd:PRK09293    3 KTLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  91 STCVIVSEENKDAVIVEaEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVSlDEPSGKDALQPGRNLVAAGYALYGS 170
Cdd:PRK09293   83 HVAGLASEEEDEIVPIP-ENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLYGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 171 ATMLVLATSaGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITEYLKKKKfPEDGSS--PYGGRYIG 248
Cdd:PRK09293  161 STMLVLTTG-DGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIELLA-GKDGPRgrPYNMRYIG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 249 SMVADVHRTLVYGGIFLYPANSKSPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVLGSPDDVKE 328
Cdd:PRK09293  239 SMVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVER 318


                  ....*...
gi 2280411784 329 YLEIVRKH 336
Cdd:PRK09293  319 VEEYHAEA 326
PLN02542 PLN02542
fructose-1,6-bisphosphatase
 2-331 1.37e-102

fructose-1,6-bisphosphatase


Pssm-ID: 215298 [Multi-domain]  Cd Length: 412  Bit Score: 307.57  E-value: 1.37e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784   2 TDRSAFDtnVITMTRFVMEEGRRAKGTGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDL 81
Cdd:PLN02542   69 TKKSGYE--IQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  82 VINMLKSSFSTCVIVSEENKDAVIVEAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYR-----------KVSLDEPSG 150
Cdd:PLN02542  147 FSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSpndecladigdDSTLDSVEQ 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 151 K---DALQPGRNLVAAGYALYGSATMLVLaTSAGGVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEGYAKYFDPAITE 227
Cdd:PLN02542  227 RcivNVCQPGSNLLAAGYCMYSSSVIFVL-TIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKK 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 228 YLKKKKFPEDGSSPYGGRYIGSMVADVHRTLVYGGIFLYPANSKSPKGKLRLLYECNPMAFVIEKAGGIATTGHQAILDI 307
Cdd:PLN02542  306 YIDDLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDI 385

                         330       340
                  ....*....|....*....|....
gi 2280411784 308 VPEDIHQRVPIVLGSPDDVkEYLE 331
Cdd:PLN02542  386 QPTEIHQRVPLYIGSVEEV-EKLE 408
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
 12-199 3.14e-97

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: 285.89  E-value: 3.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  12 ITMTRFVMEEGRRAK-GTGEFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSF 90
Cdd:pfam00316   1 ITLTRFIIEQQHEFPnATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  91 STCVIVSEENKDAVIVEAEKRGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVSL-DEPSGK-DALQPGRNLVAAGYALY 168
Cdd:pfam00316  81 IVKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPTTIeDVLQPGNEQVAAGYAMY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2280411784 169 GSATMLVLATsAGGVNCFMLDPAIGEFILVD 199
Cdd:pfam00316 161 GSSTMLVLTT-GCGVHGFTLDPSLGEFILTH 190
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
 1-328 2.02e-81

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337 [Multi-domain]  Cd Length: 351  Bit Score: 251.25  E-value: 2.02e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784   1 MTDRSAFDTNVITMTRFVmeeGRRAKGTG-EFTQLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTG----DQVKKLD 75
Cdd:PLN02628    7 LYTAARGAEGVCTLMEFL---GTEGSNVGdDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  76 ILSNDLVINMLKSSFSTCVIVSEENKDAVIVEAEkrGKYIVCIDPLDGSSNIDCLVSIGTIFAIYRKVS------LDEPS 149
Cdd:PLN02628   84 IVSNEIILSSLRNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVeadhlpVEEKA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 150 GKDALQPGRNLVAAGYALYGSATMLvlATSAG-GVNCFMLDPAIGEFILVDRDVKIKKKGNIYSLNEgyAKYFD--PAIT 226
Cdd:PLN02628  162 QLNVLQRGSRLVAAGYVLYSSATIL--CISFGsGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVND--ARYFDwpEGLR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 227 EYLK-----KKKFPEDgsspYGGRYIGSMVADVHRTLVYGGIFLypanskSPKGKLRLLYECNPMAFVIEKAGGIATTGH 301
Cdd:PLN02628  238 KYIDtvrqgKGQYPKK----YSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGK 307

                         330       340
                  ....*....|....*....|....*..
gi 2280411784 302 QAILDIVPEDIHQRVPIVLGSPDDVKE 328
Cdd:PLN02628  308 RRILSIQPVKLHQRLPLFLGSSEDVLE 334
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
 206-328 3.48e-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: 191.68  E-value: 3.48e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 206 KKGNIYSLNEGYAKYFDPAITEYLKKKKFPEdgssPYGGRYIGSMVADVHRTLVYGGIFLYPANSKSPKGKLRLLYECNP 285
Cdd:pfam18913   1 EEGKIYAINEGNARFWNAPYRAYIDDLVSGK----GYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGKLRLLYECAP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2280411784 286 MAFVIEKAGGIATTGHQAILDIVPEDIHQRVPIVLGSPDDVKE 328
Cdd:pfam18913  77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVAR 119
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
 33-333 5.04e-44

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256 [Multi-domain]  Cd Length: 304  Bit Score: 153.35  E-value: 5.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  33 QLLNSLCTAIKAISTAVRKAgianLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSFSTCVIVSEENKDAVIVEAEKRG 112
Cdd:PLN02462   17 RLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGPVEG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 113 KYIVCIDPLDGSSNIDCLVSIGTIFAIYrkvsldePSGKDALQPGRNLVAAGYALYGSATMLVLA-TSAGGVNCFMLDPA 191
Cdd:PLN02462   93 GFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTTYVVAlKDGPGTHEFLLLDD 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 192 iGEFILVDRDVKIKKK-----GNIYSL--NEGYAKYFDpaitEYLKKKkfpedgsspYGGRYIGSMVADVHRTLVY-GGI 263
Cdd:PLN02462  166 -GKWQHVKETTEIGEGkifspGNLRATfdNPGYEKLIN----YYVSEK---------YTLRYTGGMVPDVYQIIVKeKGV 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2280411784 264 FLYPANSKSPkGKLRLLYECNPMAFVIEKAGGIATTGHQA--ILDIVPEDIHQRVPIVLGSPDDVKEYLEIV 333
Cdd:PLN02462  232 FTNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEVIRFEETL 302
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 35-300 8.37e-34

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: 122.89  E-value: 8.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  35 LNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSFSTCVIVSEENKDAVIVEaEKRGKY 114
Cdd:cd01636     1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVM-GRRDEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 115 IVCIDPLDGSSN-IDCLVSIGTIFAIYrkvsldepsgkdalqpgrnlvaagyalygsatmlvlatsaggvncfmldpaig 193
Cdd:cd01636    80 TWVIDPIDGTKNfINGLPFVAVVIAVY----------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 194 efilvdrdvkikkkgNIYSLNEGYAKYFDPaiteylkkKKFPEDGSSPYGGRYIGSMVADVHRTLV-YGGIFLYPANSks 272
Cdd:cd01636   107 ---------------VILILAEPSHKRVDE--------KKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK-- 161

                         250       260
                  ....*....|....*....|....*...
gi 2280411784 273 pkgklRLLYECNPMAFVIEKAGGIATTG 300
Cdd:cd01636   162 -----RRAWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 35-299 1.78e-19

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: 85.83  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  35 LNSLCTAIKAISTAVRKAGIANLYgiAGSTNVTGDQVKKLDILSNDLVINMLKSSFSTCVIVSEENKDAvivEAEKRGKY 114
Cdd:cd01637     1 LELALKAVREAGALILEAFGEELT--VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGS---GNVSDGGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 115 IVCIDPLDGSSN-IDCLVSIGTIFAIYRKvsldepsGKDalqpgrnlVAAGYALYGsATMLVLATSAGGVNCFMLDPAIg 193
Cdd:cd01637    76 VWVIDPIDGTTNfVAGLPNFAVSIALYED-------GKP--------VLGVIYDPM-LDELYYAGRGKGAFLNGKKLPL- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784 194 efilvdrdVKIKKKGNIYSLNEGYAKYFDPAiteylkkKKFPEDGSSPYGGRYIGSMVADVHRTLVY-GGIFLYPANSks 272
Cdd:cd01637   139 --------SKDTPLNDALLSTNASMLRSNRA-------AVLASLVNRALGIRIYGSAGLDLAYVAAGrLDAYLSSGLN-- 201

                         250       260
                  ....*....|....*....|....*..
gi 2280411784 273 pkgklrlLYECNPMAFVIEKAGGIATT 299
Cdd:cd01637   202 -------PWDYAAGALIVEEAGGIVTD 221
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
45-126 2.69e-06

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 47.98  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  45 ISTAVRKAgIANLYGI--AGST---NVTGDQVKKLDILSNDLVINMLKSSFSTCVIVSEENKDAVIVEAEkrgkYIVCID 119
Cdd:PRK12676   13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPE----YTVVLD 87


                  ....*..
gi 2280411784 120 PLDGSSN 126
Cdd:PRK12676   88 PLDGTYN 94
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 68-147 2.67e-05

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: 44.75  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  68 GDQVKKLDILSNDLVINMLKSSFSTCVIVSEENKdaviVEAEKRGKYIVCIDPLDGSSN-IDCLVSIGTIFAIYRKVSLD 146
Cdd:cd01642    33 GDVTRVADLKAEEIILKLLREEGVFGQIISEESG----EIRKGSGEYIAVLDPLDGSTNyLSGIPFYSVSVALADPRSKV 108


                  .
gi 2280411784 147 E 147
Cdd:cd01642   109 K 109
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 68-126 1.12e-04

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: 43.13  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2280411784  68 GDQVKKLDILSNDLVINMLKSsFSTCVIVSEENkdAVIVEaEKRGKYIVCIDPLDGSSN 126
Cdd:cd01515    35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEI--GVIDN-GDEPEYTVVLDPLDGTYN 89
Inositol_P pfam00459
Inositol monophosphatase family;
33-134 1.20e-04

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 43.10  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  33 QLLNSLCTAIKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSFSTCVIVSEENKDAVIVEAEKRG 112
Cdd:pfam00459   4 EVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDD 83

                          90       100
                  ....*....|....*....|....*..
gi 2280411784 113 KYIVCIDPLDGSSN----IDCL-VSIG 134
Cdd:pfam00459  84 GPTWIIDPIDGTKNfvhgIPQFaVSIG 110
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 48-126 1.46e-04

Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family [Carbohydrate transport and metabolism]; Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440251 [Multi-domain]  Cd Length: 255  Bit Score: 42.52  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280411784  48 AVRKAG--IANLYGiAGSTNVT----GDQVKKLDILSNDLVINMLKSSFSTCVIVSEENKDAVIVEAEkrgkYIVCIDPL 121
Cdd:COG0483    10 AARAAGalILRRFR-ELDLEVEtkgdGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSG----YVWVIDPI 84


                  ....*
gi 2280411784 122 DGSSN 126
Cdd:COG0483    85 DGTTN 89
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
68-126 1.70e-04

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 43.18  E-value: 1.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2280411784  68 GDQVKKLDILSNDLVINMLKSsFSTCVIVSEENKDAVIveAEKRGKYIVCIDPLDGSSN 126
Cdd:PRK14076   39 GTPTKRIDLIAENIAINSLEK-FCSGILISEEIGFKKI--GKNKPEYIFVLDPIDGTYN 94
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 75-123 2.15e-04

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 42.07  E-value: 2.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2280411784  75 DILSNDLVINMLKSSFSTCVIVSEENKDAVIVEAEKRGKYIvCIDPLDG 123
Cdd:COG1218    42 DLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFW-LVDPLDG 89
 
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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