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Conserved domains on  [gi|1570588161|ref|XP_027880338|]
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fructose-1,6-bisphosphatase 1-like [Xiphophorus couchianus]

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: 545.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  18 VLEQGRKAQGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSFTSCVLVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  98 EEDEKAIIVEPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTAGEPCEQDALQPGRNIVAAGYALYGSATMMVIS 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 178 TGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLHKKKHPEDGSAPYGSRYIGSMVADVHRTL 257
Cdd:cd00354   161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570588161 258 VYGGIFLYPANDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLGSPDDVQEYLSIY 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: 545.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  18 VLEQGRKAQGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSFTSCVLVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  98 EEDEKAIIVEPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTAGEPCEQDALQPGRNIVAAGYALYGSATMMVIS 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 178 TGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLHKKKHPEDGSAPYGSRYIGSMVADVHRTL 257
Cdd:cd00354   161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570588161 258 VYGGIFLYPANDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLGSPDDVQEYLSIY 332
Cdd:cd00354   241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
 8-337 9.86e-172

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: 480.38  E-value: 9.86e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161   8 DTNVVTLTRFVLE-QGRKAQGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMI 86
Cdd:COG0158     1 MMKGTTLTQFLIEqQRRFPGATGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  87 KSSFTSCVLVSEEDEKAIIV-EPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTAGEPC-EQDALQPGRNIVAAG 164
Cdd:COG0158    81 EWGGHVAAMASEEMDDPIPIpEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGGGPVtEEDFLQPGSEQVAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 165 YALYGSATMMVISTGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLHKKKHPEDGSA--PYG 242
Cdd:COG0158   161 YVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDECLAGKEGPRgrDFN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 243 SRYIGSMVADVHRTLVYGGIFLYPA--NDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLG 320
Cdd:COG0158   241 MRWIGSLVADVHRILLRGGIFLYPAdsRDGYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILG 320

                         330
                  ....*....|....*..
gi 1570588161 321 SPDDVQEYLSIYKKHNK 337
Cdd:COG0158   321 SKEEVERVERYHAEPDA 337
PLN02262 PLN02262
fructose-1,6-bisphosphatase
 6-337 1.02e-168

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 472.75  E-value: 1.02e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161   6 AFDTNVVTLTRFVL-EQGRKAQGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVIN 84
Cdd:PLN02262    7 AHRTDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  85 MIKSSFTSCVLVSEEDEKAIIVEPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTAGEPCEQDALQPGRNIVAAG 164
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 165 YALYGSATMMVISTGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLHKKKHPEDGSAPYGSR 244
Cdd:PLN02262  167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 245 YIGSMVADVHRTLVYGGIFLYPANDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLGSPDD 324
Cdd:PLN02262  247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326

                         330
                  ....*....|...
gi 1570588161 325 VQEYLSIYKKHNK 337
Cdd:PLN02262  327 VEEIKALYAAEAA 339
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
 13-198 8.91e-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: 289.74  E-value: 8.91e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  13 TLTRFVLEQGRKA-QGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSFT 91
Cdd:pfam00316   2 TLTRFIIEQQHEFpNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  92 SCVLVSEEDEKAIIVEPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTA-GEPC-EQDALQPGRNIVAAGYALYG 169
Cdd:pfam00316  82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPTtIEDVLQPGNEQVAAGYAMYG 161

                         170       180
                  ....*....|....*....|....*....
gi 1570588161 170 SATMMVISTGQGVNGFMLDPAIGEFILVD 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: 545.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  18 VLEQGRKAQGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSFTSCVLVS 97
Cdd:cd00354     1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  98 EEDEKAIIVEPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTAGEPCEQDALQPGRNIVAAGYALYGSATMMVIS 177
Cdd:cd00354    81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 178 TGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLHKKKHPEDGSAPYGSRYIGSMVADVHRTL 257
Cdd:cd00354   161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570588161 258 VYGGIFLYPANDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLGSPDDVQEYLSIY 332
Cdd:cd00354   241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
 8-337 9.86e-172

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: 480.38  E-value: 9.86e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161   8 DTNVVTLTRFVLE-QGRKAQGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMI 86
Cdd:COG0158     1 MMKGTTLTQFLIEqQRRFPGATGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  87 KSSFTSCVLVSEEDEKAIIV-EPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTAGEPC-EQDALQPGRNIVAAG 164
Cdd:COG0158    81 EWGGHVAAMASEEMDDPIPIpEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGGGPVtEEDFLQPGSEQVAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 165 YALYGSATMMVISTGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLHKKKHPEDGSA--PYG 242
Cdd:COG0158   161 YVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDECLAGKEGPRgrDFN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 243 SRYIGSMVADVHRTLVYGGIFLYPA--NDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLG 320
Cdd:COG0158   241 MRWIGSLVADVHRILLRGGIFLYPAdsRDGYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILG 320

                         330
                  ....*....|....*..
gi 1570588161 321 SPDDVQEYLSIYKKHNK 337
Cdd:COG0158   321 SKEEVERVERYHAEPDA 337
PLN02262 PLN02262
fructose-1,6-bisphosphatase
 6-337 1.02e-168

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 472.75  E-value: 1.02e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161   6 AFDTNVVTLTRFVL-EQGRKAQGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVIN 84
Cdd:PLN02262    7 AHRTDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  85 MIKSSFTSCVLVSEEDEKAIIVEPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTAGEPCEQDALQPGRNIVAAG 164
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 165 YALYGSATMMVISTGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLHKKKHPEDGSAPYGSR 244
Cdd:PLN02262  167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 245 YIGSMVADVHRTLVYGGIFLYPANDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLGSPDD 324
Cdd:PLN02262  247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326

                         330
                  ....*....|...
gi 1570588161 325 VQEYLSIYKKHNK 337
Cdd:PLN02262  327 VEEIKALYAAEAA 339
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
12-335 2.40e-162

class 1 fructose-bisphosphatase;


Pssm-ID: 236458 [Multi-domain]  Cd Length: 327  Bit Score: 456.23  E-value: 2.40e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  12 VTLTRFVLEQGRKAQG-TGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSF 90
Cdd:PRK09293    3 KTLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  91 TSCVLVSEEDEKAIIVePDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTaGEPCEQDALQPGRNIVAAGYALYGS 170
Cdd:PRK09293   83 HVAGLASEEEDEIVPI-PENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLYGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 171 ATMMVISTGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLhKKKHPEDGS--APYGSRYIGS 248
Cdd:PRK09293  161 STMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYI-ELLAGKDGPrgRPYNMRYIGS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 249 MVADVHRTLVYGGIFLYPANDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLGSPDDVQEY 328
Cdd:PRK09293  240 MVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERV 319


                  ....*..
gi 1570588161 329 LSIYKKH 335
Cdd:PRK09293  320 EEYHAEA 326
PLN02542 PLN02542
fructose-1,6-bisphosphatase
 11-327 9.82e-110

fructose-1,6-bisphosphatase


Pssm-ID: 215298 [Multi-domain]  Cd Length: 412  Bit Score: 325.68  E-value: 9.82e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  11 VVTLTRFVLEQGRKAQGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSF 90
Cdd:PLN02542   76 IQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEVFSNCLRSSG 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  91 TSCVLVSEEDEKAIIVEPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKT--------------TAGEPCEQDALQP 156
Cdd:PLN02542  156 RTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNdecladigddstldSVEQRCIVNVCQP 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 157 GRNIVAAGYALYGSATMMVISTGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLHKKKHPED 236
Cdd:PLN02542  236 GSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKDPGP 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 237 GSAPYGSRYIGSMVADVHRTLVYGGIFLYPANDKSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQPTNIHQRVP 316
Cdd:PLN02542  316 SGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRVP 395

                         330
                  ....*....|.
gi 1570588161 317 VVLGSPDDVQE 327
Cdd:PLN02542  396 LYIGSVEEVEK 406
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
 13-198 8.91e-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: 289.74  E-value: 8.91e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  13 TLTRFVLEQGRKA-QGTGELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSFT 91
Cdd:pfam00316   2 TLTRFIIEQQHEFpNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  92 SCVLVSEEDEKAIIVEPDKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTA-GEPC-EQDALQPGRNIVAAGYALYG 169
Cdd:pfam00316  82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPTtIEDVLQPGNEQVAAGYAMYG 161

                         170       180
                  ....*....|....*....|....*....
gi 1570588161 170 SATMMVISTGQGVNGFMLDPAIGEFILVD 198
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILTH 190
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
 5-330 1.37e-89

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337 [Multi-domain]  Cd Length: 351  Bit Score: 272.05  E-value: 1.37e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161   5 GAFDTNVVTLTRFVleqGRKAQGTG-ELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTG----DQVKKLDVLSN 79
Cdd:PLN02628   11 ARGAEGVCTLMEFL---GTEGSNVGdDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  80 DLVINMIKSSFTSCVLVSEEDEKAIIVEPDkrGKYIVCFDPLDGSSNIDCLVSIGTIFAIYKKTTAGE--PCEQDA---- 153
Cdd:PLN02628   88 EIILSSLRNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEADhlPVEEKAqlnv 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 154 LQPGRNIVAAGYALYGSATMMVISTGQGVNGFMLDPAIGEFILVDRDVKIKKKGKIYSLNEGYAQDFYPDVTEYLH---- 229
Cdd:PLN02628  166 LQRGSRLVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIDtvrq 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 230 -KKKHPEDgsapYGSRYIGSMVADVHRTLVYGGIFLypandkSPKGKLRLLYECNPMAFIMEQAGGKATTGSENVLDIQP 308
Cdd:PLN02628  246 gKGQYPKK----YSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQP 315

                         330       340
                  ....*....|....*....|..
gi 1570588161 309 TNIHQRVPVVLGSPDDVQEYLS 330
Cdd:PLN02628  316 VKLHQRLPLFLGSSEDVLELES 337
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
 205-333 3.27e-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: 3.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 205 KKGKIYSLNEGYAQDFYPDVTEYLHKKKHPEdgsaPYGSRYIGSMVADVHRTLVYGGIFLYPANDKSPKGKLRLLYECNP 284
Cdd:pfam18913   1 EEGKIYAINEGNARFWNAPYRAYIDDLVSGK----GYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGKLRLLYECAP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1570588161 285 MAFIMEQAGGKATTGSENVLDIQPTNIHQRVPVVLGSPDDVQEYLSIYK 333
Cdd:pfam18913  77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAYLK 125
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
 30-328 2.08e-45

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256 [Multi-domain]  Cd Length: 304  Bit Score: 156.81  E-value: 2.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  30 ELTTLLNSICTAVKAISSAVRKAglanLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSFTSCVLVSEEDEKAIIVEPD 109
Cdd:PLN02462   14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 110 KRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYkkttagePCEQDALQPGRNIVAAGYALYGSATMMVIS--TGQGVNGFML 187
Cdd:PLN02462   90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTTYVVAlkDGPGTHEFLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 188 DPAiGEFILVDRDVKIkKKGKIYS---LNEGYAQDFYPDVTEYLHKKKhpedgsapYGSRYIGSMVADVHRTLVY-GGIF 263
Cdd:PLN02462  163 LDD-GKWQHVKETTEI-GEGKIFSpgnLRATFDNPGYEKLINYYVSEK--------YTLRYTGGMVPDVYQIIVKeKGVF 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1570588161 264 LYPANDKSPkGKLRLLYECNPMAFIMEQAGGKATTGSE--NVLDIQPTNIHQRVPVVLGSPDDVQEY 328
Cdd:PLN02462  233 TNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGVQggSVLDKQINNLDQRTQVAYGSKNEVIRF 298
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 35-299 3.27e-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: 124.04  E-value: 3.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  35 LNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSFTSCVLVSEEDEKAIIVEpDKRGKY 114
Cdd:cd01636     1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVM-GRRDEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 115 IVCFDPLDGSSNID-CLVSIGTIFAIYkkttagepceqdalqpgrnivaagyalygsatmmvistgqgvngfmldpaige 193
Cdd:cd01636    80 TWVIDPIDGTKNFInGLPFVAVVIAVY----------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 194 filvdrdvkikkkgKIYSLNEGYAQDFYPdvteylhkKKHPEDGSAPYGSRYIGSMVADVHRTLV-YGGIFLYPANDksp 272
Cdd:cd01636   107 --------------VILILAEPSHKRVDE--------KKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK--- 161

                         250       260
                  ....*....|....*....|....*..
gi 1570588161 273 kgklRLLYECNPMAFIMEQAGGKATTG 299
Cdd:cd01636   162 ----RRAWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 35-307 2.74e-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: 88.14  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  35 LNSICTAVKAISSAVRKAGLANLYgiAGSTNVTGDQVKKLDVLSNDLVINMIKSSFTSCVLVSEEDEKAIIVEpdkRGKY 114
Cdd:cd01637     1 LELALKAVREAGALILEAFGEELT--VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVS---DGGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 115 IVCFDPLDGSSN-IDCLVSIGTIFAIYKKttaGEPceqdalqpgrniVAAGYALYGsATMMViSTGQGVNGFMLDPAIge 193
Cdd:cd01637    76 VWVIDPIDGTTNfVAGLPNFAVSIALYED---GKP------------VLGVIYDPM-LDELY-YAGRGKGAFLNGKKL-- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161 194 filvdRDVKIKKKGKIY-SLNEGYAQDFYPDVTEYLHKkkhpedgsAPYGSRYIGSMVADVHRTLVY-GGIFLYPANdks 271
Cdd:cd01637   137 -----PLSKDTPLNDALlSTNASMLRSNRAAVLASLVN--------RALGIRIYGSAGLDLAYVAAGrLDAYLSSGL--- 200

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1570588161 272 pkgklrLLYECNPMAFIMEQAGGKATTGSENVLDIQ 307
Cdd:cd01637   201 ------NPWDYAAGALIVEEAGGIVTDLDGEPLDTL 230
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
35-126 5.85e-06

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 46.82  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  35 LNSICtavKAISSAVRKAgLANLYGI--AGST---NVTGDQVKKLDVLSNDLVINMIKSSFTSCVLVSEEDEKAIIVEPD 109
Cdd:PRK12676    6 WLEIC---DDMAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPE 81

                          90
                  ....*....|....*..
gi 1570588161 110 krgkYIVCFDPLDGSSN 126
Cdd:PRK12676   82 ----YTVVLDPLDGTYN 94
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
68-126 1.58e-04

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 43.18  E-value: 1.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  68 GDQVKKLDVLSNDLVINMIKSsFTSCVLVSEE-DEKAIivePDKRGKYIVCFDPLDGSSN 126
Cdd:PRK14076   39 GTPTKRIDLIAENIAINSLEK-FCSGILISEEiGFKKI---GKNKPEYIFVLDPIDGTYN 94
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 68-126 1.62e-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: 42.75  E-value: 1.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  68 GDQVKKLDVLSNDLVINMIKSsFTSCVLVSEE-DEKAIIVEPDkrgkYIVCFDPLDGSSN 126
Cdd:cd01515    35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEiGVIDNGDEPE----YTVVLDPLDGTYN 89
Inositol_P pfam00459
Inositol monophosphatase family;
30-146 4.36e-04

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 41.18  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570588161  30 ELTTLLNSICTAVKAISSAVRKAGLANLYGIAGSTNVTGDQVKKLDVLSNDLVINMIKSSFTSCVLVSEEDEKAIIVEPD 109
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1570588161 110 KRGKYIVCFDPLDGSSN----IDCL-VSIGtiFAIYKKTTAG 146
Cdd:pfam00459  81 TDDGPTWIIDPIDGTKNfvhgIPQFaVSIG--LAVNGEPVLG 120
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 68-126 7.92e-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: 37.43  E-value: 7.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1570588161  68 GDQVKKLDVLSNDLVINMIKSSFTSCVLVSEEdekAIIVEPdKRGKYIVCFDPLDGSSN 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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