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Conserved domains on  [gi|524957055|ref|XP_005078490|]
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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

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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, ...
18-329 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  Cd Length: 315  Bit Score: 527.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVS 97
Cdd:cd00354    1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  98 EENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354   81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 178 TGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354  161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524957055 258 VYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQEYL 329
Cdd:cd00354  241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVE 312
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
18-329 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  Cd Length: 315  Bit Score: 527.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVS 97
Cdd:cd00354    1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  98 EENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354   81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 178 TGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354  161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524957055 258 VYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQEYL 329
Cdd:cd00354  241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVE 312
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-327 1.23e-161

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 455.03  E-value: 1.23e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055   9 TDMLTLTRYVM-EKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  88 SSYSTCVLVSEENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 168 YGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 248 SMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
11-329 1.88e-140

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 400.54  E-value: 1.88e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  11 MLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSS 89
Cdd:COG0158    1 MKTLGRFLVEKQKEFKAaTAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  90 YSTCVLVSEEnKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDePSEKDALQPGRNIVAAGYALYG 169
Cdd:COG0158   81 GNVAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 170 SATLVALSTGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSA-PYGARYVGS 248
Cdd:COG0158  159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDKGTRrPYNMRYIGS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 249 MVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQEY 328
Cdd:COG0158  239 MVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEKL 318

                 .
gi 524957055 329 L 329
Cdd:COG0158  319 E 319
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
13-199 7.22e-92

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: 271.98  E-value: 7.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055   13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYS 91
Cdd:pfam00316   2 TLTRFIIEEQHEFPnATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVLADEILKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055   92 TCVLVSEENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSA 171
Cdd:pfam00316  82 VAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAGYVVYGSS 161
                         170       180
                  ....*....|....*....|....*...
gi 524957055  172 TLVALSTGQGVDLFMLDPALGEFVLVEK 199
Cdd:pfam00316 162 TMLVLTTGCGVHGFTLDPSLGEFILTHE 189
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
18-329 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  Cd Length: 315  Bit Score: 527.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVS 97
Cdd:cd00354    1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  98 EENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354   81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 178 TGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354  161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524957055 258 VYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQEYL 329
Cdd:cd00354  241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVE 312
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-327 1.23e-161

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 455.03  E-value: 1.23e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055   9 TDMLTLTRYVM-EKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  88 SSYSTCVLVSEENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 168 YGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 248 SMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
10-327 2.43e-153

class 1 fructose-bisphosphatase;


Pssm-ID: 236458  Cd Length: 327  Bit Score: 433.12  E-value: 2.43e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  10 DMLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS 88
Cdd:PRK09293   1 SMKTLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  89 SYSTCVLVSEEnKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTeDEPSEKDALQPGRNIVAAGYALY 168
Cdd:PRK09293  81 RGHVAGLASEE-EDEIVPIPENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 169 GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEYVQ-KKKFPEDGSAPYGARYVG 247
Cdd:PRK09293 159 GPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIElLAGKDGPRGRPYNMRYIG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 248 SMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQE 327
Cdd:PRK09293 239 SMVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVER 318
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
11-329 1.88e-140

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 400.54  E-value: 1.88e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  11 MLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSS 89
Cdd:COG0158    1 MKTLGRFLVEKQKEFKAaTAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  90 YSTCVLVSEEnKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDePSEKDALQPGRNIVAAGYALYG 169
Cdd:COG0158   81 GNVAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 170 SATLVALSTGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSA-PYGARYVGS 248
Cdd:COG0158  159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDKGTRrPYNMRYIGS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 249 MVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQEY 328
Cdd:COG0158  239 MVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEKL 318

                 .
gi 524957055 329 L 329
Cdd:COG0158  319 E 319
PLN02542 PLN02542
fructose-1,6-bisphosphatase
2-327 5.87e-105

fructose-1,6-bisphosphatase


Pssm-ID: 215298  Cd Length: 412  Bit Score: 313.73  E-value: 5.87e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055   2 TDRSPFEtdMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSL 81
Cdd:PLN02542  69 TKKSGYE--IQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  82 VINMLQSSYSTCVLVSEENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTE-----------DEPSE 150
Cdd:PLN02542 147 FSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDEcladigddstlDSVEQ 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 151 K---DALQPGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEGYAKYFDAATTEY 227
Cdd:PLN02542 227 RcivNVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKY 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 228 VQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVK 307
Cdd:PLN02542 307 IDDLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQ 386
                        330       340
                 ....*....|....*....|
gi 524957055 308 PETIHQRVPLILGSPEDVQE 327
Cdd:PLN02542 387 PTEIHQRVPLYIGSVEEVEK 406
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
13-199 7.22e-92

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: 271.98  E-value: 7.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055   13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYS 91
Cdd:pfam00316   2 TLTRFIIEEQHEFPnATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVLADEILKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055   92 TCVLVSEENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSA 171
Cdd:pfam00316  82 VAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAGYVVYGSS 161
                         170       180
                  ....*....|....*....|....*...
gi 524957055  172 TLVALSTGQGVDLFMLDPALGEFVLVEK 199
Cdd:pfam00316 162 TMLVLTTGCGVHGFTLDPSLGEFILTHE 189
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
13-327 6.09e-85

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337  Cd Length: 351  Bit Score: 260.11  E-value: 6.09e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  13 TLTRYVmekGRQAKGTG-ELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTG----DEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02628  19 TLMEFL---GTEGSNVGdDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSNEIILSSLR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  88 SSYSTCVLVSEENKEAVITAKEkrGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTE------DEPSEKDALQPGRNIV 161
Cdd:PLN02628  96 NSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEadhlpvEEKAQLNVLQRGSRLV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 162 AAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVRIKKKGKIFSLNEgyAKYFD--AATTEYVQ-----KKKFP 234
Cdd:PLN02628 174 AAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVND--ARYFDwpEGLRKYIDtvrqgKGQYP 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 235 EDgsapYGARYVGSMVADVHRTLVYGGIFMYPANQkspngkLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPETIHQR 314
Cdd:PLN02628 252 KK----YSARYICSLVADLHRTILYGGIAMNPRSH------LRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQR 321
                        330
                 ....*....|...
gi 524957055 315 VPLILGSPEDVQE 327
Cdd:PLN02628 322 LPLFLGSSEDVLE 334
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
206-333 1.22e-65

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: 202.84  E-value: 1.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  206 KGKIFSLNEGYAKYFDAATTEYVQKKKFpedGSAPYGARYVGSMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPV 285
Cdd:pfam18913   1 EGKIYAINEGNARHWNAPYRAYIDDLKS---GGKGYTLRYVGSMVADVHRILLKGGIFLYPADKRAPNGKLRLLYECAPL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 524957055  286 AYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQEYLTCVQ 333
Cdd:pfam18913  78 AFLIEQAGGKASDGKQRILDIVPDSLHQRTPIFLGSREEVERVEAYLK 125
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
30-328 7.77e-48

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256  Cd Length: 304  Bit Score: 162.98  E-value: 7.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  30 ELTQLLNSMLTAIKAISSAVRKAglanLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAKE 109
Cdd:PLN02462  14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 110 KRGKYVVCFDPLDGSSNIDCLASIGTIFAIYrkttedePSEKDALQPGRNIVAAGYALYGSAT--LVALSTGQGVDLFML 187
Cdd:PLN02462  90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTtyVVALKDGPGTHEFLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 188 DPAlGEFVLVEKDVRIkKKGKIFSL--------NEGYAKYFDaattEYVQKKkfpedgsapYGARYVGSMVADVHRTLVY 259
Cdd:PLN02462 163 LDD-GKWQHVKETTEI-GEGKIFSPgnlratfdNPGYEKLIN----YYVSEK---------YTLRYTGGMVPDVYQIIVK 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524957055 260 -GGIFMYPANQKSPnGKLRLLYECNPVAYIIEQAGGMATTGTQP--VLDVKPETIHQRVPLILGSPEDVQEY 328
Cdd:PLN02462 228 eKGVFTNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEVIRF 298
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
35-299 3.52e-31

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: 115.95  E-value: 3.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  35 LNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAkEKRGKY 114
Cdd:cd01636    1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVM-GRRDEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 115 VVCFDPLDGSSN-IDCLASIGTIFAIYRKTTEDEPSEKDalqpgrnivaagyalygsatlvalstgqgvdlfmldpalge 193
Cdd:cd01636   80 TWVIDPIDGTKNfINGLPFVAVVIAVYVILILAEPSHKR----------------------------------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 194 fvlvekdvrikkkgkifslnegyakyfdaatteyVQKKKFPEDGSAPYGARYVGSMVADVHRTLV-YGGIFMYPANQksp 272
Cdd:cd01636  119 ----------------------------------VDEKKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK--- 161
                        250       260
                 ....*....|....*....|....*..
gi 524957055 273 ngklRLLYECNPVAYIIEQAGGMATTG 299
Cdd:cd01636  162 ----RRAWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
35-320 7.60e-18

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: 81.21  E-value: 7.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  35 LNSMLTAIKAISSAVRKAGLANLYGIAGSVNvtGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEaviTAKEKRGKY 114
Cdd:cd01637    1 LELALKAVREAGALILEAFGEELTVETKKGD--GDLVTEADLAAEELIVDVLKALFPDDGILGEEGGG---SGNVSDGGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 115 VVCFDPLDGSSN-IDCLASIGTIFAIYRKtteDEPsekdalqpgrniVAAGYALYGSATLVALSTGQGVDLFMLDPALGE 193
Cdd:cd01637   76 VWVIDPIDGTTNfVAGLPNFAVSIALYED---GKP------------VLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 194 fvlvekdvRIKKKGKIFSLNEGYAKYFDAAtteyvqkkKFPEDGSAPYGARYVGSMVADVHRTLV--YGGIFmypanqkS 271
Cdd:cd01637  141 --------DTPLNDALLSTNASMLRSNRAA--------VLASLVNRALGIRIYGSAGLDLAYVAAgrLDAYL-------S 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 524957055 272 PNGKlrlLYECNPVAYIIEQAGGMATTgtqpvLDVKPETIHQRVPLILG 320
Cdd:cd01637  198 SGLN---PWDYAAGALIVEEAGGIVTD-----LDGEPLDTLNRSGIIAA 238
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
34-147 3.14e-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  Cd Length: 244  Bit Score: 41.66  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  34 LLNSMLTAIKAISSAVRKAGLANLygIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVitakEKRGK 113
Cdd:cd01642    1 MLEVLEKITKEIILLLNEKNRQGL--VKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIR----KGSGE 74
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 524957055 114 YVVCFDPLDGSSN-IDCLASIGTIFAIYRKTTEDE 147
Cdd:cd01642   75 YIAVLDPLDGSTNyLSGIPFYSVSVALADPRSKVK 109
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
45-126 5.54e-04

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673  Cd Length: 263  Bit Score: 41.05  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055  45 ISSAVRKAgLANLYGI--AGSV---NVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVItakeKRGKYVVCFD 119
Cdd:PRK12676  13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVG----NGPEYTVVLD 87

                 ....*..
gi 524957055 120 PLDGSSN 126
Cdd:PRK12676  88 PLDGTYN 94
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
68-126 9.50e-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: 40.05  E-value: 9.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 524957055  68 GDEVKKLDVLSNSLVINMLQSsYSTCVLVSEENKEAVItakEKRGKYVVCFDPLDGSSN 126
Cdd:cd01515   35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEIGVIDN---GDEPEYTVVLDPLDGTYN 89
Inositol_P pfam00459
Inositol monophosphatase family;
39-134 2.41e-03

Inositol monophosphatase family;


Pssm-ID: 395369 [Multi-domain]  Cd Length: 270  Bit Score: 38.86  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055   39 LTAIKAISSAVRKAGLANLYGI-AGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAKEKRGKYVVC 117
Cdd:pfam00459   9 AVELAAKAGEVLREAFSNKLTIeEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQSELTDDGPTWI 88
                          90       100
                  ....*....|....*....|..
gi 524957055  118 FDPLDGSSN----IDCLA-SIG 134
Cdd:pfam00459  89 IDPIDGTTNfvhgIPQFAvSIG 110
 
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.
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