NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|85097320|ref|XP_960423|]
View 

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
31-347 8.67e-176

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


:

Pssm-ID: 238214  Cd Length: 315  Bit Score: 490.14  E-value: 8.67e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  31 EEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSSGKCALLVSE 110
Cdd:cd00354   2 LEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 111 EEEHVIYFKDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKLAEDSTGTKEDILKPGTELVAAGFTMYGASAQLVITM 190
Cdd:cd00354  82 EEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLTL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 191 KGGsVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKEtQEDSGKPYSARYIGSMVADAYRT 270
Cdd:cd00354 162 GQG-VHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKA-GEDGGKPYNLRYIGSMVADVHRI 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85097320 271 LLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDEVEKVKKYH 347
Cdd:cd00354 240 LVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGK-ERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
31-347 8.67e-176

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


Pssm-ID: 238214  Cd Length: 315  Bit Score: 490.14  E-value: 8.67e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  31 EEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSSGKCALLVSE 110
Cdd:cd00354   2 LEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 111 EEEHVIYFKDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKLAEDSTGTKEDILKPGTELVAAGFTMYGASAQLVITM 190
Cdd:cd00354  82 EEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLTL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 191 KGGsVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKEtQEDSGKPYSARYIGSMVADAYRT 270
Cdd:cd00354 162 GQG-VHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKA-GEDGGKPYNLRYIGSMVADVHRI 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85097320 271 LLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDEVEKVKKYH 347
Cdd:cd00354 240 LVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGK-ERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
20-350 3.10e-151

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 428.84  E-value: 3.10e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   20 THIVTLTRFLTEEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMR 99
Cdd:PLN02262  10 TDLMTITRFVLNEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  100 SSGKCALLVSEEEEHVIYFKDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKLAEDSTGTKEDILKPGTELVAAGFTM 179
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  180 YGASAQLVITMkGGSVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKETQEDSgKPYSARY 259
Cdd:PLN02262 170 YGSSCTLVLST-GGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGS-SPKSLRY 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  260 IGSMVADAYRTLLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDE 339
Cdd:PLN02262 248 IGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGK-QRALDLVPTKIHERSPIFLGSYDD 326
                        330
                 ....*....|.
gi 85097320  340 VEKVKKYHGKA 350
Cdd:PLN02262 327 VEEIKALYAAE 337
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
22-349 1.18e-147

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 419.41  E-value: 1.18e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  22 IVTLTRFLTEEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSS 101
Cdd:COG0158   1 MKTLGRFLVEKQKEFKAATAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 102 GKCALLVSEEEEHVIYFkDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKlAEDSTGTKEDILKPGTELVAAGFTMYG 181
Cdd:COG0158  81 GNVAGIASEEEDEPVTF-PENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYR-RPGSPGTEEDFLQPGNKQVAAGYVVYG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 182 ASAQLVITMkGGSVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKETQEDSGKPYSARYIG 261
Cdd:COG0158 159 PSTMLVYTL-GEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDKGTRRPYNMRYIG 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 262 SMVADAYRTLLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDEVE 341
Cdd:COG0158 238 SMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGK-QRILDIVPEKLHQRVPLFLGSKEEVE 316

                ....*...
gi 85097320 342 KVKKYHGK 349
Cdd:COG0158 317 KLERFIKE 324
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
24-212 1.24e-85

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


Pssm-ID: 395249  Cd Length: 189  Bit Score: 256.57  E-value: 1.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320    24 TLTRFLTEEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSSGK 103
Cdd:pfam00316   2 TLTRFIIEEQHEFPNATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVLADEILKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   104 CALLVSEEEEHVIYFKDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKLAEDSTGTKEDILKPGTELVAAGFTMYGAS 183
Cdd:pfam00316  82 VAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAGYVVYGSS 161
                         170       180
                  ....*....|....*....|....*....
gi 85097320   184 AQLVITMKGGsVNGFTLDQGVGEFILTHP 212
Cdd:pfam00316 162 TMLVLTTGCG-VHGFTLDPSLGEFILTHE 189
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
31-347 8.67e-176

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


Pssm-ID: 238214  Cd Length: 315  Bit Score: 490.14  E-value: 8.67e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  31 EEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSSGKCALLVSE 110
Cdd:cd00354   2 LEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 111 EEEHVIYFKDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKLAEDSTGTKEDILKPGTELVAAGFTMYGASAQLVITM 190
Cdd:cd00354  82 EEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLTL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 191 KGGsVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKEtQEDSGKPYSARYIGSMVADAYRT 270
Cdd:cd00354 162 GQG-VHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKA-GEDGGKPYNLRYIGSMVADVHRI 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 85097320 271 LLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDEVEKVKKYH 347
Cdd:cd00354 240 LVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGK-ERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
20-350 3.10e-151

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 428.84  E-value: 3.10e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   20 THIVTLTRFLTEEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMR 99
Cdd:PLN02262  10 TDLMTITRFVLNEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  100 SSGKCALLVSEEEEHVIYFKDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKLAEDSTGTKEDILKPGTELVAAGFTM 179
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  180 YGASAQLVITMkGGSVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKETQEDSgKPYSARY 259
Cdd:PLN02262 170 YGSSCTLVLST-GGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGS-SPKSLRY 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  260 IGSMVADAYRTLLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDE 339
Cdd:PLN02262 248 IGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGK-QRALDLVPTKIHERSPIFLGSYDD 326
                        330
                 ....*....|.
gi 85097320  340 VEKVKKYHGKA 350
Cdd:PLN02262 327 VEEIKALYAAE 337
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
23-350 9.16e-148

class 1 fructose-bisphosphatase;


Pssm-ID: 236458  Cd Length: 327  Bit Score: 419.64  E-value: 9.16e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   23 VTLTRFLTEEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSSG 102
Cdd:PRK09293   3 KTLGEFLVEQQREFPHATGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  103 KCALLVSEEEEHVIYFkDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKlAEDSTGTKEDILKPGTELVAAGFTMYGA 182
Cdd:PRK09293  83 HVAGLASEEEDEIVPI-PENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYR-APVGTPTEEDFLQPGNNQVAAGYVLYGP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  183 SAQLVITMKGGsVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKETQEDSGKPYSARYIGS 262
Cdd:PRK09293 161 STMLVLTTGDG-VHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIELLAGKDGPRGRPYNMRYIGS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  263 MVADAYRTLLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDEVEK 342
Cdd:PRK09293 240 MVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGK-QRILDIEPESLHQRVPLFLGSKEEVER 318

                 ....*...
gi 85097320  343 VKKYHGKA 350
Cdd:PRK09293 319 VEEYHAEA 326
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
22-349 1.18e-147

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 419.41  E-value: 1.18e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  22 IVTLTRFLTEEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSS 101
Cdd:COG0158   1 MKTLGRFLVEKQKEFKAATAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 102 GKCALLVSEEEEHVIYFkDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKlAEDSTGTKEDILKPGTELVAAGFTMYG 181
Cdd:COG0158  81 GNVAGIASEEEDEPVTF-PENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYR-RPGSPGTEEDFLQPGNKQVAAGYVVYG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 182 ASAQLVITMkGGSVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKETQEDSGKPYSARYIG 261
Cdd:COG0158 159 PSTMLVYTL-GEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDKGTRRPYNMRYIG 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 262 SMVADAYRTLLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDEVE 341
Cdd:COG0158 238 SMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGK-QRILDIVPEKLHQRVPLFLGSKEEVE 316

                ....*...
gi 85097320 342 KVKKYHGK 349
Cdd:COG0158 317 KLERFIKE 324
PLN02542 PLN02542
fructose-1,6-bisphosphatase
22-346 6.26e-104

fructose-1,6-bisphosphatase


Pssm-ID: 215298  Cd Length: 412  Bit Score: 311.42  E-value: 6.26e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   22 IVTLTRFLTEEQVKhKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSS 101
Cdd:PLN02542  76 IQTLTTWLLKQEQA-GVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEVFSNCLRSS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  102 GKCALLVSEEEEHVIYFKDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHK--------LAEDSTGTKE------DILK 167
Cdd:PLN02542 155 GRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSpndecladIGDDSTLDSVeqrcivNVCQ 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  168 PGTELVAAGFTMYGASAQLVITMkGGSVNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYWEDDVKAYFNSLKET 247
Cdd:PLN02542 235 PGSNLLAAGYCMYSSSVIFVLTI-GTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKDP 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  248 QEdSGKPYSARYIGSMVADAYRTLLYGGMFAYPADKKSPKGKLRILYECAPMAMIFENAGGQAVDSKmNRMLEVVPEHIH 327
Cdd:PLN02542 314 GP-SGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGH-QRILDIQPTEIH 391
                        330
                 ....*....|....*....
gi 85097320  328 DKAGIFMGSYDEVEKVKKY 346
Cdd:PLN02542 392 QRVPLYIGSVEEVEKLEKY 410
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
24-212 1.24e-85

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


Pssm-ID: 395249  Cd Length: 189  Bit Score: 256.57  E-value: 1.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320    24 TLTRFLTEEQVKHKEATGDFTLLCHALQFSFKSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSSGK 103
Cdd:pfam00316   2 TLTRFIIEEQHEFPNATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVLADEILKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   104 CALLVSEEEEHVIYFKDAKNARYAVACDPIDGSSNLDAGVSVGTIFAIHKLAEDSTGTKEDILKPGTELVAAGFTMYGAS 183
Cdd:pfam00316  82 VAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAGYVVYGSS 161
                         170       180
                  ....*....|....*....|....*....
gi 85097320   184 AQLVITMKGGsVNGFTLDQGVGEFILTHP 212
Cdd:pfam00316 162 TMLVLTTGCG-VHGFTLDPSLGEFILTHE 189
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
4-346 4.78e-78

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337  Cd Length: 351  Bit Score: 243.16  E-value: 4.78e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320    4 FTTNGAGAENdgekvnthIVTLTRFLTEEQvkhKEATGDFTLLCHALQFSFKSIAYYI---RRATLVNLTGLAGSSNTTG 80
Cdd:PLN02628   7 LYTAARGAEG--------VCTLMEFLGTEG---SNVGDDLVVLMAHIQAACKRIAALLaspFNSELGKTSSGASGASGSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   81 -DEQKKLDVISNDLFIEAMRSSGKCALLVSEEEEHVIYFKDakNARYAVACDPIDGSSNLDAGVSVGTIFAI-HKLAE-D 157
Cdd:PLN02628  76 rDAPKPLDIVSNEIILSSLRNSGKVAVMASEEDDAPIWIGD--DGPYVVVFDPLDGSRNIDASIPTGTIFGIyNRLVEaD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  158 STGTKE----DILKPGTELVAAGFTMYGASAQLVITMKGGSvNGFTLDQGVGEFILTHPNMTIPRKRSIYSVNEGNSLYW 233
Cdd:PLN02628 154 HLPVEEkaqlNVLQRGSRLVAAGYVLYSSATILCISFGSGT-HGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDW 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  234 EDDVKAYFNSLKETQEDSGKPYSARYIGSMVADAYRTLLYGGMfaypadKKSPKGKLRILYECAPMAMIFENAGGQAVDS 313
Cdd:PLN02628 233 PEGLRKYIDTVRQGKGQYPKKYSARYICSLVADLHRTILYGGI------AMNPRSHLRLVYEANPLSFLVEQAGGRGSDG 306
                        330       340       350
                 ....*....|....*....|....*....|...
gi 85097320  314 KmNRMLEVVPEHIHDKAGIFMGSYDEVEKVKKY 346
Cdd:PLN02628 307 K-RRILSIQPVKLHQRLPLFLGSSEDVLELESY 338
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
221-347 1.46e-57

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


Pssm-ID: 408683 [Multi-domain]  Cd Length: 125  Bit Score: 182.42  E-value: 1.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   221 SIYSVNEGNSLYWEDDVKAYFNSLKEtqedSGKPYSARYIGSMVADAYRTLLYGGMFAYPADKKSPKGKLRILYECAPMA 300
Cdd:pfam18913   3 KIYAINEGNARHWNAPYRAYIDDLKS----GGKGYTLRYVGSMVADVHRILLKGGIFLYPADKRAPNGKLRLLYECAPLA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 85097320   301 MIFENAGGQAVDSKmNRMLEVVPEHIHDKAGIFMGSYDEVEKVKKYH 347
Cdd:pfam18913  79 FLIEQAGGKASDGK-QRILDIVPDSLHQRTPIFLGSREEVERVEAYL 124
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
57-346 8.42e-39

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256  Cd Length: 304  Bit Score: 139.87  E-value: 8.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   57 IAYYIRRAtlvnLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSSGKCALLVSEEEEHVIYFKDAKNARYAVACDPIDGS 136
Cdd:PLN02462  29 IAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGPVEGGFSVAFDPLDGS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  137 SNLDAGVSVGTIFAIHKlAEDSTGTKedilkpGTELVAAGFTMYGASAQLVITMKGGSvngftldqGVGEFILTHPNMTI 216
Cdd:PLN02462 105 SIVDTNFAVGTIFGVWP-GDKLTGVT------GRDQVAAAMGIYGPRTTYVVALKDGP--------GTHEFLLLDDGKWQ 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  217 PRKRSIySVNEGN-----SLYWEDDVKAYFNSLKETQEDSgkpYSARYIGSMVADAYRTLLY-GGMFAYPADKKSPkGKL 290
Cdd:PLN02462 170 HVKETT-EIGEGKifspgNLRATFDNPGYEKLINYYVSEK---YTLRYTGGMVPDVYQIIVKeKGVFTNVTSPKSK-AKL 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 85097320  291 RILYECAPMAMIFENAGGQAVD-SKMNRMLEVVPEHIHDKAGIFMGSYDEVEKVKKY 346
Cdd:PLN02462 245 RLLFEVAPLGLLVEKAGGKSSDgVQGGSVLDKQINNLDQRTQVAYGSKNEVIRFEET 301
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
55-154 7.14e-10

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: 57.40  E-value: 7.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  55 KSIAYYIRRATLVNLTGLAGSSNTTGDEQKKLDVISNDLFIEAMRSSGKCALLVSEEEEHVIYfKDAKNARYAVACDPID 134
Cdd:cd01636   9 KEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEE-VMGRRDEYTWVIDPID 87
                        90       100
                ....*....|....*....|.
gi 85097320 135 GSSNLDAG-VSVGTIFAIHKL 154
Cdd:cd01636  88 GTKNFINGlPFVAVVIAVYVI 108
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
73-314 1.06e-06

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: 49.24  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  73 AGSSNTTGDEQKKLDVISNDLFIEAMRSSGKCALLVSEEEEHVIyfKDAKNARYAVAcDPIDGSSNLDAG-VSVGTIFAI 151
Cdd:cd01637  25 VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSG--NVSDGGRVWVI-DPIDGTTNFVAGlPNFAVSIAL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 152 HKLAEDSTGtkedilkpGTELVAAGfTMYGAsaqlvitmkggsvngftlDQGVGEFILTHPnMTIPRKRSIYSVNEGNSL 231
Cdd:cd01637 102 YEDGKPVLG--------VIYDPMLD-ELYYA------------------GRGKGAFLNGKK-LPLSKDTPLNDALLSTNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320 232 YWEDDvkayfNSLKETQEDSGKPYSARYIGSMVADAYRTLLyGGMFAYPadkkSPKGKlriLYECAPMAMIFENAGGQAV 311
Cdd:cd01637 154 SMLRS-----NRAAVLASLVNRALGIRIYGSAGLDLAYVAA-GRLDAYL----SSGLN---PWDYAAGALIVEEAGGIVT 220

                ...
gi 85097320 312 DSK 314
Cdd:cd01637 221 DLD 223
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
52-151 9.76e-06

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673  Cd Length: 263  Bit Score: 46.44  E-value: 9.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320   52 FSFKSIAYYIRRATLVNLTGLAGSS--------NTTGDEQKKLDVISNDLFIEAMRSSGKCALLVSEEEEHVIyfkdAKN 123
Cdd:PRK12676   4 MEWLEICDDMAKEVEKAIMPLFGTPdagetvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIV----GNG 79
                         90       100
                 ....*....|....*....|....*...
gi 85097320  124 ARYAVACDPIDGSSNLDAGVSvgtIFAI 151
Cdd:PRK12676  80 PEYTVVLDPLDGTYNAINGIP---FYAI 104
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
80-154 1.14e-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  Cd Length: 257  Bit Score: 43.13  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85097320  80 GDEQKKLDVISNDLFIEAMRSSGKcALLVSEEeehvIYFKD-AKNARYAVACDPIDGSSNLDAG-----VSVGtIFAIHK 153
Cdd:cd01515  35 GTPTKLIDKVAEDAAIEILKKLGS-VNIVSEE----IGVIDnGDEPEYTVVLDPLDGTYNAINGipfysVSVA-VFKIDK 108

                .
gi 85097320 154 L 154
Cdd:cd01515 109 S 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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