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Conserved domains on  [gi|9506589|ref|NP_062268|]
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fructose-1,6-bisphosphatase 1 [Mus musculus]

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

EC:  3.1.3.11
Gene Ontology:  GO:0042132|GO:0000287
SCOP:  4002766

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
18-332 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: 531.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   18 VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   98 EENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYALYGSATMLVLA 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  178 MDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVGSMVADIHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506589  258 VYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEFLEIY 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: 531.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   18 VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   98 EENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYALYGSATMLVLA 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  178 MDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVGSMVADIHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506589  258 VYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEFLEIY 332
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-338 2.74e-162

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 456.58  E-value: 2.74e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589     9 TDISTLTRFVM-EQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLK 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    88 SSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   168 YGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   248 SMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
                        330
                 ....*....|.
gi 9506589   328 FLEIYRKHKAK 338
Cdd:PLN02262 330 IKALYAAEAAK 340
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
11-336 6.66e-139

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


Pssm-ID: 223236 [Multi-domain]  Cd Length: 326  Bit Score: 396.68  E-value: 6.66e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   11 ISTLTRF-VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSS 89
Cdd:COG0158   1 MKTLGRFlVEKQKEFKAATAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   90 YATCVLVSEENTNAIIIEPEKrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDePSEKDALQPGRDLVAAGYALYG 169
Cdd:COG0158  81 GNVAGIASEEEDEPVTFPENN-GSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  170 SATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLqRKKFPPDGSA--PYGARYVG 247
Cdd:COG0158 159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYI-KDCFAEDKGTrrPYNMRYIG 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  248 SMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQE 327
Cdd:COG0158 238 SMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEK 317

                ....*....
gi 9506589  328 FLEIYRKHK 336
Cdd:COG0158 318 LERFIKEFP 326
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
12-198 7.01e-103

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: 300.15  E-value: 7.01e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589     12 STLTRFVMEQGRKA-QGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSY 90
Cdd:pfam00316   1 ITLTRFIIEQQHEFpNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589     91 ATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKS-TDEPSEK-DALQPGRDLVAAGYALY 168
Cdd:pfam00316  81 IVKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSpTDSPTTIeDVLQPGNEQVAAGYAMY 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 9506589    169 GSATMLVLAMDCGVNCFMLDPSIGEFIMVD 198
Cdd:pfam00316 161 GSSTMLVLTTGCGVHGFTLDPSLGEFILTH 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: 531.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   18 VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   98 EENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYALYGSATMLVLA 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  178 MDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVGSMVADIHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506589  258 VYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEFLEIY 332
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-338 2.74e-162

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 456.58  E-value: 2.74e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589     9 TDISTLTRFVM-EQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLK 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    88 SSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   168 YGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   248 SMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
                        330
                 ....*....|.
gi 9506589   328 FLEIYRKHKAK 338
Cdd:PLN02262 330 IKALYAAEAAK 340
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
13-336 1.79e-152

class 1 fructose-bisphosphatase;


Pssm-ID: 236458 [Multi-domain]  Cd Length: 327  Bit Score: 431.20  E-value: 1.79e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    13 TLTRFVMEQGRKAQG-TGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYA 91
Cdd:PRK09293   4 TLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARGH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    92 TCVLVSEENTNAIIIePEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKStDEPSEKDALQPGRDLVAAGYALYGSA 171
Cdd:PRK09293  84 VAGLASEEEDEIVPI-PENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLYGPS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   172 TMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAIN---EYLQRKKFPpdGSAPYGARYVGS 248
Cdd:PRK09293 162 TMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKkyiELLAGKDGP--RGRPYNMRYIGS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   249 MVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEF 328
Cdd:PRK09293 240 MVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERV 319

                 ....*...
gi 9506589   329 LEIYRKHK 336
Cdd:PRK09293 320 EEYHAEAP 327
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
11-336 6.66e-139

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


Pssm-ID: 223236 [Multi-domain]  Cd Length: 326  Bit Score: 396.68  E-value: 6.66e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   11 ISTLTRF-VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSS 89
Cdd:COG0158   1 MKTLGRFlVEKQKEFKAATAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   90 YATCVLVSEENTNAIIIEPEKrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDePSEKDALQPGRDLVAAGYALYG 169
Cdd:COG0158  81 GNVAGIASEEEDEPVTFPENN-GSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  170 SATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLqRKKFPPDGSA--PYGARYVG 247
Cdd:COG0158 159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYI-KDCFAEDKGTrrPYNMRYIG 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  248 SMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQE 327
Cdd:COG0158 238 SMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEK 317

                ....*....
gi 9506589  328 FLEIYRKHK 336
Cdd:COG0158 318 LERFIKEFP 326
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
12-198 7.01e-103

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: 300.15  E-value: 7.01e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589     12 STLTRFVMEQGRKA-QGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSY 90
Cdd:pfam00316   1 ITLTRFIIEQQHEFpNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589     91 ATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKS-TDEPSEK-DALQPGRDLVAAGYALY 168
Cdd:pfam00316  81 IVKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSpTDSPTTIeDVLQPGNEQVAAGYAMY 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 9506589    169 GSATMLVLAMDCGVNCFMLDPSIGEFIMVD 198
Cdd:pfam00316 161 GSSTMLVLTTGCGVHGFTLDPSLGEFILTH 190
PLN02542 PLN02542
fructose-1,6-bisphosphatase
10-332 1.05e-101

fructose-1,6-bisphosphatase


Pssm-ID: 215298 [Multi-domain]  Cd Length: 412  Bit Score: 305.26  E-value: 1.05e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    10 DISTLTRFVMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSS 89
Cdd:PLN02542  75 EIQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEVFSNCLRSS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    90 YATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYR-----------KKSTDEPSEK---DALQ 155
Cdd:PLN02542 155 GRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSpndecladigdDSTLDSVEQRcivNVCQ 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   156 PGRDLVAAGYALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPP 235
Cdd:PLN02542 235 PGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKDPG 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   236 DGSAPYGARYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKA 315
Cdd:PLN02542 315 PSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRV 394
                        330
                 ....*....|....*..
gi 9506589   316 PVVMGSSEDVqEFLEIY 332
Cdd:PLN02542 395 PLYIGSVEEV-EKLEKY 410
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
12-332 1.58e-83

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337 [Multi-domain]  Cd Length: 351  Bit Score: 256.65  E-value: 1.58e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    12 STLTRFVmeqGRKAQGTG-ELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTG----DQVKKLDILSNDLVINML 86
Cdd:PLN02628  18 CTLMEFL---GTEGSNVGdDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSNEIILSSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    87 KSSYATCVLVSEENTNAIIIEPEkrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKS------TDEPSEKDALQPGRDL 160
Cdd:PLN02628  95 RNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVeadhlpVEEKAQLNVLQRGSRL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   161 VAAGYALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYL----QRKkfppd 236
Cdd:PLN02628 173 VAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIdtvrQGK----- 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   237 GSAP--YGARYVGSMVADIHRTLVYGGIFLypankkSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQK 314
Cdd:PLN02628 248 GQYPkkYSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQR 321
                        330
                 ....*....|....*...
gi 9506589   315 APVVMGSSEDVQEfLEIY 332
Cdd:PLN02628 322 LPLFLGSSEDVLE-LESY 338
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
205-332 6.67e-59

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: 185.51  E-value: 6.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    205 KKGNIYSLNEGYAKDFDPAINEYLQRKKFPpdgsAPYGARYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNP 284
Cdd:pfam18913   1 EEGKIYAINEGNARFWNAPYRAYIDDLVSG----KGYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGKLRLLYECAP 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 9506589    285 IAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEFLEIY 332
Cdd:pfam18913  77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAYL 124
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
30-330 1.69e-46

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256 [Multi-domain]  Cd Length: 304  Bit Score: 159.51  E-value: 1.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    30 ELTQLLNSLCTAIKAISSAVRQAgiaqLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENTNAIIIEPE 109
Cdd:PLN02462  14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   110 KRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYrkkstdePSEKDALQPGRDLVAAGYALYGSATMLVLAMDCGVNCFmldp 189
Cdd:PLN02462  90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTTYVVALKDGPGTH---- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   190 sigEFIMVDRDVKMKKKGNIySLNEGyaKDFDPA--------------INEYLQRKkfppdgsapYGARYVGSMVADIHR 255
Cdd:PLN02462 159 ---EFLLLDDGKWQHVKETT-EIGEG--KIFSPGnlratfdnpgyeklINYYVSEK---------YTLRYTGGMVPDVYQ 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506589   256 TLVY-GGIFLYPANKKSPSgKLRLLYECNPIAYVMEKAGGLATTGDKD--ILDIVPTEIHQKAPVVMGSSEDVQEFLE 330
Cdd:PLN02462 224 IIVKeKGVFTNVTSPKSKA-KLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEVIRFEE 300
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
35-299 2.54e-38

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: 134.44  E-value: 2.54e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   35 LNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENtNAIIIEPEKRGKY 114
Cdd:cd01636   1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEES-GVAEEVMGRRDEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  115 VVCFDPLDGSSN-IDCLVSIGTIFGIYrkkstdepsekdalqpgrdlvaagyalygsatmlvlamdcgvncfmldpsige 193
Cdd:cd01636  80 TWVIDPIDGTKNfINGLPFVAVVIAVY----------------------------------------------------- 106
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  194 fimvdrdvkmkkkgNIYSLNEGYAKDFDPaineylqrKKFPPDGSAPYGARYVGSMVADIHRTLV-YGGIFLYPANKksp 272
Cdd:cd01636 107 --------------VILILAEPSHKRVDE--------KKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK--- 161
                       250       260
                ....*....|....*....|....*..
gi 9506589  273 sgklRLLYECNPIAYVMEKAGGLATTG 299
Cdd:cd01636 162 ----RRAWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
35-300 2.32e-23

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: 96.61  E-value: 2.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   35 LNSLCTAIKAISSAVRQAGIAQLYgiAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENTNAIIiepEKRGKY 114
Cdd:cd01637   1 LELALKAVREAGALILEAFGEELT--VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGN---VSDGGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  115 VVCFDPLDGSSN-IDCLVSIGTIFGIYRKKSTdepsekdalqpgrdlVAAGYALYGsATMLVLAM-DCGVNCFMLDPSIg 192
Cdd:cd01637  76 VWVIDPIDGTTNfVAGLPNFAVSIALYEDGKP---------------VLGVIYDPM-LDELYYAGrGKGAFLNGKKLPL- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589  193 efimvdrdVKMKKKGNIYSLNEGYAKDFDPAineylqrKKFPPDGSAPYGARYVGSMVADIHRTLVY-GGIFLYPANKks 271
Cdd:cd01637 139 --------SKDTPLNDALLSTNASMLRSNRA-------AVLASLVNRALGIRIYGSAGLDLAYVAAGrLDAYLSSGLN-- 201
                       250       260
                ....*....|....*....|....*....
gi 9506589  272 psgklrlLYECNPIAYVMEKAGGLATTGD 300
Cdd:cd01637 202 -------PWDYAAGALIVEEAGGIVTDLD 223
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
45-126 8.27e-06

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 46.44  E-value: 8.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589    45 ISSAVRQAgIAQLYGI--AGST---NVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENTNAIIIEPEkrgkYVVCFD 119
Cdd:PRK12676  13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPE----YTVVLD 87

                 ....*..
gi 9506589   120 PLDGSSN 126
Cdd:PRK12676  88 PLDGTYN 94
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
34-147 3.40e-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: 41.66  E-value: 3.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589   34 LLNSLCTAIKAISSAVR---QAGIAQLYGIAGstnvtGDQVKKLDILSNDLVINMLKSSYATCVLVSEEntnAIIIEPEK 110
Cdd:cd01642   1 MLEVLEKITKEIILLLNeknRQGLVKLIRGAG-----GDVTRVADLKAEEIILKLLREEGVFGQIISEE---SGEIRKGS 72
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 9506589  111 rGKYVVCFDPLDGSSN-IDCLVSIGTIFGIYRKKSTDE 147
Cdd:cd01642  73 -GEYIAVLDPLDGSTNyLSGIPFYSVSVALADPRSKVK 109
Inositol_P pfam00459
Inositol monophosphatase family;
30-134 9.04e-04

Inositol monophosphatase family;


Pssm-ID: 425694 [Multi-domain]  Cd Length: 271  Bit Score: 40.41  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589     30 ELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENTNAIIIEPE 109
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEVLREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAPGDQSEL 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 9506589    110 KRGKYVVCFDPLDGSSN----IDCL-VSIG 134
Cdd:pfam00459  81 TDDGPTWIIDPIDGTTNfvhgIPQFaVSIG 110
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
68-126 2.69e-03

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 39.33  E-value: 2.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 9506589    68 GDQVKKLDILSNDLVINMLKSsYATCVLVSEENTNAIIiePEKRGKYVVCFDPLDGSSN 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 4.61e-03

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: 38.13  E-value: 4.61e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 9506589   68 GDQVKKLDILSNDLVINMLKSsYATCVLVSEENTnaiIIEPEKRGKYVVCFDPLDGSSN 126
Cdd:cd01515  35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEIG---VIDNGDEPEYTVVLDPLDGTYN 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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