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Conserved domains on  [gi|1929406128|ref|XP_037121181|]
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fructose-1,6-bisphosphatase 1-like [Syngnathus acus]

Protein Classification

class 1 fructose-bisphosphatase( domain architecture ID 10086071)

class 1 fructose-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:0000287
SCOP:  4002766

Graphical summary

 Zoom to residue level

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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, ...
 18-332 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: 548.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  18 VLEEGRKAHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFSSCVLVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  98 EEDEHAIVVESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTDDAPNEKDALQPGRNLVAAGYALYGSATMLVLS 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 178 TGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQKKKFPEDGSAPYGSRYIGSMVADVHRTL 257
Cdd:cd00354   161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929406128 258 VYGGIFLYPANTKSPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLGSPDDVQEYIAIY 332
Cdd:cd00354   241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
 18-332 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: 548.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  18 VLEEGRKAHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFSSCVLVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  98 EEDEHAIVVESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTDDAPNEKDALQPGRNLVAAGYALYGSATMLVLS 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 178 TGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQKKKFPEDGSAPYGSRYIGSMVADVHRTL 257
Cdd:cd00354   161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929406128 258 VYGGIFLYPANTKSPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLGSPDDVQEYIAIY 332
Cdd:cd00354   241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
 8-335 2.18e-173

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: 484.62  E-value: 2.18e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128   8 DTNVLTLTRFVLEE-GRKAHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINML 86
Cdd:COG0158     1 MMKGTTLTQFLIEQqRRFPGATGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  87 KSSFSSCVLVSEEDEHAIVV-ESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTD-DAPNEKDALQPGRNLVAAG 164
Cdd:COG0158    81 EWGGHVAAMASEEMDDPIPIpEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGgGPVTEEDFLQPGSEQVAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 165 YALYGSATMLVLSTGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQ--KKKFPEDGSAPYG 242
Cdd:COG0158   161 YVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDecLAGKEGPRGRDFN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 243 SRYIGSMVADVHRTLVYGGIFLYPANTK--SPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLG 320
Cdd:COG0158   241 MRWIGSLVADVHRILLRGGIFLYPADSRdgYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILG 320

                         330
                  ....*....|....*
gi 1929406128 321 SPDDVQEYIAIYKKH 335
Cdd:COG0158   321 SKEEVERVERYHAEP 335
PLN02262 PLN02262
fructose-1,6-bisphosphatase
 6-333 3.33e-165

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 463.89  E-value: 3.33e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128   6 DFDTNVLTLTRFVL-EEGRKAHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVIN 84
Cdd:PLN02262    7 AHRTDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  85 MLKSSFSSCVLVSEEDEHAIVVESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTDDAPNEKDALQPGRNLVAAG 164
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 165 YALYGSATMLVLSTGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQKKKFPEDGSAPYGSR 244
Cdd:PLN02262  167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 245 YIGSMVADVHRTLVYGGIFLYPANTKSPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLGSPDD 324
Cdd:PLN02262  247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326


                  ....*....
gi 1929406128 325 VQEYIAIYK 333
Cdd:PLN02262  327 VEEIKALYA 335
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
 13-198 4.68e-99

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: 290.52  E-value: 4.68e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  13 TLTRFVLEEGRKA-HGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFS 91
Cdd:pfam00316   2 TLTRFIIEQQHEFpNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  92 SCVLVSEEDEHAIVVESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKK--TTDDAPNEKDALQPGRNLVAAGYALYG 169
Cdd:pfam00316  82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRvsPTDSPTTIEDVLQPGNEQVAAGYAMYG 161

                         170       180
                  ....*....|....*....|....*....
gi 1929406128 170 SATMLVLSTGQGVNCFMLDPAIGEFILVD 198
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILTH 190
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
 18-332 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: 548.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  18 VLEEGRKAHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFSSCVLVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  98 EEDEHAIVVESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTDDAPNEKDALQPGRNLVAAGYALYGSATMLVLS 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 178 TGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQKKKFPEDGSAPYGSRYIGSMVADVHRTL 257
Cdd:cd00354   161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929406128 258 VYGGIFLYPANTKSPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLGSPDDVQEYIAIY 332
Cdd:cd00354   241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
 8-335 2.18e-173

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: 484.62  E-value: 2.18e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128   8 DTNVLTLTRFVLEE-GRKAHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINML 86
Cdd:COG0158     1 MMKGTTLTQFLIEQqRRFPGATGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  87 KSSFSSCVLVSEEDEHAIVV-ESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTD-DAPNEKDALQPGRNLVAAG 164
Cdd:COG0158    81 EWGGHVAAMASEEMDDPIPIpEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGgGPVTEEDFLQPGSEQVAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 165 YALYGSATMLVLSTGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQ--KKKFPEDGSAPYG 242
Cdd:COG0158   161 YVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDecLAGKEGPRGRDFN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 243 SRYIGSMVADVHRTLVYGGIFLYPANTK--SPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLG 320
Cdd:COG0158   241 MRWIGSLVADVHRILLRGGIFLYPADSRdgYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILG 320

                         330
                  ....*....|....*
gi 1929406128 321 SPDDVQEYIAIYKKH 335
Cdd:COG0158   321 SKEEVERVERYHAEP 335
PLN02262 PLN02262
fructose-1,6-bisphosphatase
 6-333 3.33e-165

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 463.89  E-value: 3.33e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128   6 DFDTNVLTLTRFVL-EEGRKAHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVIN 84
Cdd:PLN02262    7 AHRTDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  85 MLKSSFSSCVLVSEEDEHAIVVESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTDDAPNEKDALQPGRNLVAAG 164
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 165 YALYGSATMLVLSTGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQKKKFPEDGSAPYGSR 244
Cdd:PLN02262  167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 245 YIGSMVADVHRTLVYGGIFLYPANTKSPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLGSPDD 324
Cdd:PLN02262  247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326


                  ....*....
gi 1929406128 325 VQEYIAIYK 333
Cdd:PLN02262  327 VEEIKALYA 335
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
13-335 4.69e-160

class 1 fructose-bisphosphatase;


Pssm-ID: 236458 [Multi-domain]  Cd Length: 327  Bit Score: 450.46  E-value: 4.69e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  13 TLTRFVLEEGRK-AHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFS 91
Cdd:PRK09293    4 TLGEFLVEQQREfPHATGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  92 SCVLVSEEDEHAIVVESDKsGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTDDaPNEKDALQPGRNLVAAGYALYGSA 171
Cdd:PRK09293   84 VAGLASEEEDEIVPIPENE-GKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPVGT-PTEEDFLQPGNNQVAAGYVLYGPS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 172 TMLVLSTGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQ-KKKFPEDGSAPYGSRYIGSMV 250
Cdd:PRK09293  162 TMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIElLAGKDGPRGRPYNMRYIGSMV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 251 ADVHRTLVYGGIFLYPANTKSPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLGSPDDVQEYIA 330
Cdd:PRK09293  242 ADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERVEE 321


                  ....*
gi 1929406128 331 IYKKH 335
Cdd:PRK09293  322 YHAEA 326
PLN02542 PLN02542
fructose-1,6-bisphosphatase
 2-327 3.23e-111

fructose-1,6-bisphosphatase


Pssm-ID: 215298 [Multi-domain]  Cd Length: 412  Bit Score: 329.53  E-value: 3.23e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128   2 SEKGDFDtnVLTLTRFVLEEGRKAHGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDL 81
Cdd:PLN02542   69 TKKSGYE--IQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  82 VINMLKSSFSSCVLVSEEDEHAIVVESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKT----TDDAPNEK------ 151
Cdd:PLN02542  147 FSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNdeclADIGDDSTldsveq 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 152 ----DALQPGRNLVAAGYALYGSATMLVLSTGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEY 227
Cdd:PLN02542  227 rcivNVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKY 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 228 IQKKKFPEDGSAPYGSRYIGSMVADVHRTLVYGGIFLYPANTKSPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQ 307
Cdd:PLN02542  307 IDDLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQ 386

                         330       340
                  ....*....|....*....|
gi 1929406128 308 PTNIHQRVPVVLGSPDDVQE 327
Cdd:PLN02542  387 PTEIHQRVPLYIGSVEEVEK 406
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
 13-198 4.68e-99

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: 290.52  E-value: 4.68e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  13 TLTRFVLEEGRKA-HGTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFS 91
Cdd:pfam00316   2 TLTRFIIEQQHEFpNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  92 SCVLVSEEDEHAIVVESDKSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKK--TTDDAPNEKDALQPGRNLVAAGYALYG 169
Cdd:pfam00316  82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRvsPTDSPTTIEDVLQPGNEQVAAGYAMYG 161

                         170       180
                  ....*....|....*....|....*....
gi 1929406128 170 SATMLVLSTGQGVNCFMLDPAIGEFILVD 198
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILTH 190
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
 5-327 5.78e-88

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337 [Multi-domain]  Cd Length: 351  Bit Score: 268.20  E-value: 5.78e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128   5 GDFDTNVLTLTRFVLEEGRKAhgTGELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTG----DQVKKLDVLSND 80
Cdd:PLN02628   11 ARGAEGVCTLMEFLGTEGSNV--GDDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSNE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  81 LVINMLKSSFSSCVLVSEEDEHAIVVESDksGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKK--TTDDAPNEKDA----L 154
Cdd:PLN02628   89 IILSSLRNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRlvEADHLPVEEKAqlnvL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 155 QPGRNLVAAGYALYGSATMLVLSTGQGVNCFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQHFYPDVTEYIQ----- 229
Cdd:PLN02628  167 QRGSRLVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIDtvrqg 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 230 KKKFPEDgsapYGSRYIGSMVADVHRTLVYGGIFLypantkSPKGKLRLLYECNPMSFIVEQAGGMATTGAGNILDIQPT 309
Cdd:PLN02628  247 KGQYPKK----YSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPV 316

                         330
                  ....*....|....*...
gi 1929406128 310 NIHQRVPVVLGSPDDVQE 327
Cdd:PLN02628  317 KLHQRLPLFLGSSEDVLE 334
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
 205-333 9.63e-66

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: 203.23  E-value: 9.63e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 205 KKGKIYSLNEGYAQHFYPDVTEYIQKKKFPEdgsaPYGSRYIGSMVADVHRTLVYGGIFLYPANTKSPKGKLRLLYECNP 284
Cdd:pfam18913   1 EEGKIYAINEGNARFWNAPYRAYIDDLVSGK----GYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGKLRLLYECAP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1929406128 285 MSFIVEQAGGMATTGAGNILDIQPTNIHQRVPVVLGSPDDVQEYIAIYK 333
Cdd:pfam18913  77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAYLK 125
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
 30-328 2.99e-43

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256 [Multi-domain]  Cd Length: 304  Bit Score: 151.04  E-value: 2.99e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  30 ELTNLLNSICTAVKAISTAVRKAgianLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFSSCVLVSEEDEHAIVVESD 109
Cdd:PLN02462   14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 110 KSGKYIVCFDPLDGSSNIDCLVSIGTIFAIYkkttddaPNEKDALQPGRNLVAAGYALYGSATMLV--LSTGQGVNCFML 187
Cdd:PLN02462   90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTTYVvaLKDGPGTHEFLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 188 DPAiGEFILVDRDVKIkKKGKIYS---LNEGYAQHFYPDVTEYIQKKKfpedgsapYGSRYIGSMVADVHRTLVY-GGIF 263
Cdd:PLN02462  163 LDD-GKWQHVKETTEI-GEGKIFSpgnLRATFDNPGYEKLINYYVSEK--------YTLRYTGGMVPDVYQIIVKeKGVF 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929406128 264 LYPANTKSPkGKLRLLYECNPMSFIVEQAGGMATTG--AGNILDIQPTNIHQRVPVVLGSPDDVQEY 328
Cdd:PLN02462  233 TNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGvqGGSVLDKQINNLDQRTQVAYGSKNEVIRF 298
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 35-299 1.17e-35

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: 127.51  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  35 LNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFSSCVLVSEEDEHAIVVESdKSGKY 114
Cdd:cd01636     1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMG-RRDEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 115 IVCFDPLDGSSNID-CLVSIGTIFAIYkkttddapnekdalqpgrnlvaagyalygsatmlvlstgqgvncfmldpaige 193
Cdd:cd01636    80 TWVIDPIDGTKNFInGLPFVAVVIAVY----------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 194 filvdrdvkikkkgKIYSLNEGYAQHFYPdvteyiqkKKFPEDGSAPYGSRYIGSMVADVHRTLV-YGGIFLYPANTksp 272
Cdd:cd01636   107 --------------VILILAEPSHKRVDE--------KKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK--- 161

                         250       260
                  ....*....|....*....|....*..
gi 1929406128 273 kgklRLLYECNPMSFIVEQAGGMATTG 299
Cdd:cd01636   162 ----RRAWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 35-307 2.15e-20

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: 88.53  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  35 LNSICTAVKAISTAVRKAGIANLYgiAGSTNVTGDQVKKLDVLSNDLVINMLKSSFSSCVLVSEEDEHAivvESDKSGKY 114
Cdd:cd01637     1 LELALKAVREAGALILEAFGEELT--VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGS---GNVSDGGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 115 IVCFDPLDGSSN-IDCLVSIGTIFAIYKkttDDAPnekdalqpgrnlVAAGYALYGSATMLVLSTGQGVNCFMLDPAIge 193
Cdd:cd01637    76 VWVIDPIDGTTNfVAGLPNFAVSIALYE---DGKP------------VLGVIYDPMLDELYYAGRGKGAFLNGKKLPL-- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128 194 filvdrdVKIKKKGKIY-SLNEGYAQHFYPDVteyiqkkkFPEDGSAPYGSRYIGSMVADVHRTLVY-GGIFLYPANtks 271
Cdd:cd01637   139 -------SKDTPLNDALlSTNASMLRSNRAAV--------LASLVNRALGIRIYGSAGLDLAYVAAGrLDAYLSSGL--- 200

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1929406128 272 pkgklrLLYECNPMSFIVEQAGGMATTGAGNILDIQ 307
Cdd:cd01637   201 ------NPWDYAAGALIVEEAGGIVTDLDGEPLDTL 230
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
35-126 6.94e-07

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 49.91  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  35 LNSICtavKAISTAVRKAgIANLYGI--AGST---NVTGDQVKKLDVLSNDLVINMLKSSFSSCVLVSEEdehaIVVESD 109
Cdd:PRK12676    6 WLEIC---DDMAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEE----LGEIVG 77

                          90
                  ....*....|....*..
gi 1929406128 110 KSGKYIVCFDPLDGSSN 126
Cdd:PRK12676   78 NGPEYTVVLDPLDGTYN 94
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 68-147 8.04e-06

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: 46.60  E-value: 8.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  68 GDQVKKLDVLSNDLVINMLKSsFSSCVLVSEEDehAIVVESDKSGkYIVCFDPLDGSSNIdcLVSI---GTIFAIYKKTT 144
Cdd:cd01515    35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEI--GVIDNGDEPE-YTVVLDPLDGTYNA--INGIpfySVSVAVFKIDK 108


                  ...
gi 1929406128 145 DDA 147
Cdd:cd01515   109 SDP 111
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
68-126 1.52e-05

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 46.64  E-value: 1.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1929406128  68 GDQVKKLDVLSNDLVINMLKSsFSSCVLVSEEDEHAIVveSDKSGKYIVCFDPLDGSSN 126
Cdd:PRK14076   39 GTPTKRIDLIAENIAINSLEK-FCSGILISEEIGFKKI--GKNKPEYIFVLDPIDGTYN 94
Inositol_P pfam00459
Inositol monophosphatase family;
30-134 8.42e-05

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 43.49  E-value: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929406128  30 ELTNLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDLVINMLKSSFSSCVLVSEEDEHAIVVESD 109
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1929406128 110 KSGKYIVCFDPLDGSSN----IDCL-VSIG 134
Cdd:pfam00459  81 TDDGPTWIIDPIDGTKNfvhgIPQFaVSIG 110
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 68-126 1.24e-04

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: 42.82  E-value: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1929406128  68 GDQVKKLDVLSNDLVINMLKSSFSSCVLVSEEdehAIVVESdKSGKYIVCFDPLDGSSN 126
Cdd:cd01642    33 GDVTRVADLKAEEIILKLLREEGVFGQIISEE---SGEIRK-GSGEYIAVLDPLDGSTN 87
 
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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