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Conserved domains on  [gi|16758954|ref|NP_446168|]
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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, ...
18-330 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: 526.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  98 EENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 178 TGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758954 258 VYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQEYLS 330
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEE 313
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
18-330 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: 526.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  98 EENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 178 TGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758954 258 VYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQEYLS 330
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEE 313
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-327 5.05e-163

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 458.50  E-value: 5.05e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954    9 TDMLTLTRYVM-EKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   88 SSYSTCVLVSEENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  168 YGSATLVALSTGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQKKKFPEDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  248 SMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
11-330 3.12e-141

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 402.46  E-value: 3.12e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  11 MLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSS 89
Cdd:COG0158   1 MKTLGRFLVEKQKEFKAaTAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  90 YSTCVLVSEEnKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDePSEKDALQPGRNIVAAGYALYG 169
Cdd:COG0158  81 GNVAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 170 SATLVALSTGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQKKKFPEDGSA-PYGARYVGS 248
Cdd:COG0158 159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDKGTRrPYNMRYIGS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 249 MVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQEY 328
Cdd:COG0158 239 MVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEKL 318

                ..
gi 16758954 329 LS 330
Cdd:COG0158 319 ER 320
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
13-199 5.26e-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: 272.36  E-value: 5.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954    13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYS 91
Cdd:pfam00316   2 TLTRFIIEEQHEFPnATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVLADEILKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954    92 TCVLVSEENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSA 171
Cdd:pfam00316  82 VAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAGYVVYGSS 161
                         170       180
                  ....*....|....*....|....*...
gi 16758954   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, ...
18-330 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: 526.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  98 EENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 178 TGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758954 258 VYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQEYLS 330
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEE 313
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-327 5.05e-163

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 458.50  E-value: 5.05e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954    9 TDMLTLTRYVM-EKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   88 SSYSTCVLVSEENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  168 YGSATLVALSTGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQKKKFPEDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  248 SMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
10-336 8.68e-154

class 1 fructose-bisphosphatase;


Pssm-ID: 236458  Cd Length: 327  Bit Score: 434.28  E-value: 8.68e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   10 DMLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS 88
Cdd:PRK09293   1 SMKTLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   89 SYSTCVLVSEEnKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTeDEPSEKDALQPGRNIVAAGYALY 168
Cdd:PRK09293  81 RGHVAGLASEE-EDEIVPIPENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  169 GSATLVALSTGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQ-KKKFPEDGSAPYGARYVG 247
Cdd:PRK09293 159 GPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIElLAGKDGPRGRPYNMRYIG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  248 SMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQE 327
Cdd:PRK09293 239 SMVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVER 318

                 ....*....
gi 16758954  328 YLSCVQRNQ 336
Cdd:PRK09293 319 VEEYHAEAP 327
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
11-330 3.12e-141

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 402.46  E-value: 3.12e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  11 MLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSS 89
Cdd:COG0158   1 MKTLGRFLVEKQKEFKAaTAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  90 YSTCVLVSEEnKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDePSEKDALQPGRNIVAAGYALYG 169
Cdd:COG0158  81 GNVAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 170 SATLVALSTGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEYVQKKKFPEDGSA-PYGARYVGS 248
Cdd:COG0158 159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDKGTRrPYNMRYIGS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 249 MVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQEY 328
Cdd:COG0158 239 MVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEKL 318

                ..
gi 16758954 329 LS 330
Cdd:COG0158 319 ER 320
PLN02542 PLN02542
fructose-1,6-bisphosphatase
2-327 1.98e-105

fructose-1,6-bisphosphatase


Pssm-ID: 215298  Cd Length: 412  Bit Score: 314.89  E-value: 1.98e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954    2 TDRSPFEtdMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSL 81
Cdd:PLN02542  69 TKKSGYE--IQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   82 VINMLQSSYSTCVLVSEENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTE-----------DEPSE 150
Cdd:PLN02542 147 FSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDEcladigddstlDSVEQ 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  151 K---DALQPGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEGYAKYFDAATAEY 227
Cdd:PLN02542 227 RcivNVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKY 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  228 VQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPVAYIIEQAGGMATTGTQPVLDVK 307
Cdd:PLN02542 307 IDDLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQ 386
                        330       340
                 ....*....|....*....|
gi 16758954  308 PESIHQRVPLILGSPEDVQE 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 5.26e-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: 272.36  E-value: 5.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954    13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYS 91
Cdd:pfam00316   2 TLTRFIIEEQHEFPnATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVLADEILKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954    92 TCVLVSEENKEAVITAKERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEDEPSEKDALQPGRNIVAAGYALYGSA 171
Cdd:pfam00316  82 VAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAGYVVYGSS 161
                         170       180
                  ....*....|....*....|....*...
gi 16758954   172 TLVALSTGQGVDLFMLDPALGEFVLVEK 199
Cdd:pfam00316 162 TMLVLTTGCGVHGFTLDPSLGEFILTHE 189
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
13-330 2.79e-85

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337  Cd Length: 351  Bit Score: 261.27  E-value: 2.79e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   13 TLTRYVmekGRQAKGTG-ELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTG----DEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02628  19 TLMEFL---GTEGSNVGdDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSNEIILSSLR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   88 SSYSTCVLVSEENKEAVITAKErrGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTE------DEPSEKDALQPGRNIV 161
Cdd:PLN02628  96 NSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEadhlpvEEKAQLNVLQRGSRLV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  162 AAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDIRIKKKGKIFSLNEgyAKYFD--AATAEYVQ-----KKKFP 234
Cdd:PLN02628 174 AAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVND--ARYFDwpEGLRKYIDtvrqgKGQYP 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  235 EDgsapYGARYVGSMVADVHRTLVYGGIFMYPANQkspngkLRLLYECNPVAYIIEQAGGMATTGTQPVLDVKPESIHQR 314
Cdd:PLN02628 252 KK----YSARYICSLVADLHRTILYGGIAMNPRSH------LRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQR 321
                        330
                 ....*....|....*.
gi 16758954  315 VPLILGSPEDVQEYLS 330
Cdd:PLN02628 322 LPLFLGSSEDVLELES 337
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
206-333 5.85e-66

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


Pssm-ID: 408683 [Multi-domain]  Cd Length: 125  Bit Score: 203.61  E-value: 5.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   206 KGKIFSLNEGYAKYFDAATAEYVQKKKFpedGSAPYGARYVGSMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNPV 285
Cdd:pfam18913   1 EGKIYAINEGNARHWNAPYRAYIDDLKS---GGKGYTLRYVGSMVADVHRILLKGGIFLYPADKRAPNGKLRLLYECAPL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 16758954   286 AYIIEQAGGMATTGTQPVLDVKPESIHQRVPLILGSPEDVQEYLSCVQ 333
Cdd:pfam18913  78 AFLIEQAGGKASDGKQRILDIVPDSLHQRTPIFLGSREEVERVEAYLK 125
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
30-328 5.18e-48

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256  Cd Length: 304  Bit Score: 163.75  E-value: 5.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   30 ELTQLLNSMLTAIKAISSAVRKAglanLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAKE 109
Cdd:PLN02462  14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  110 RRGKYVVCFDPLDGSSNIDCLASIGTIFAIYrkttedePSEKDALQPGRNIVAAGYALYGSAT--LVALSTGQGVDLFML 187
Cdd:PLN02462  90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTtyVVALKDGPGTHEFLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  188 DPAlGEFVLVEKDIRIkKKGKIFSL--------NEGYAKYFDaataEYVQKKkfpedgsapYGARYVGSMVADVHRTLVY 259
Cdd:PLN02462 163 LDD-GKWQHVKETTEI-GEGKIFSPgnlratfdNPGYEKLIN----YYVSEK---------YTLRYTGGMVPDVYQIIVK 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758954  260 -GGIFMYPANQKSPnGKLRLLYECNPVAYIIEQAGGMATTGTQP--VLDVKPESIHQRVPLILGSPEDVQEY 328
Cdd:PLN02462 228 eKGVFTNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEVIRF 298
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
35-299 4.16e-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: 115.57  E-value: 4.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  35 LNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAkERRGKY 114
Cdd:cd01636   1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVM-GRRDEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 115 VVCFDPLDGSSN-IDCLASIGTIFAIYRKTTEDEPSEKDalqpgrnivaagyalygsatlvalstgqgvdlfmldpalge 193
Cdd:cd01636  80 TWVIDPIDGTKNfINGLPFVAVVIAVYVILILAEPSHKR----------------------------------------- 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 194 fvlvekdirikkkgkifslnegyakyfdaataeyVQKKKFPEDGSAPYGARYVGSMVADVHRTLV-YGGIFMYPANQksp 272
Cdd:cd01636 119 ----------------------------------VDEKKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK--- 161
                       250       260
                ....*....|....*....|....*..
gi 16758954 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 1.89e-17

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: 80.05  E-value: 1.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  35 LNSMLTAIKAISSAVRKAGLANLYGIAGSVNvtGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEaviTAKERRGKY 114
Cdd:cd01637   1 LELALKAVREAGALILEAFGEELTVETKKGD--GDLVTEADLAAEELIVDVLKALFPDDGILGEEGGG---SGNVSDGGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 115 VVCFDPLDGSSN-IDCLASIGTIFAIYRKtteDEPsekdalqpgrniVAAGYALYGSATLVALSTGQGVDLFMLDPALGE 193
Cdd:cd01637  76 VWVIDPIDGTTNfVAGLPNFAVSIALYED---GKP------------VLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954 194 fvlvekdiRIKKKGKIFSLNEGYAKYFDAAtaeyvqkkKFPEDGSAPYGARYVGSMVADVHRTLV--YGGIFmypanqkS 271
Cdd:cd01637 141 --------DTPLNDALLSTNASMLRSNRAA--------VLASLVNRALGIRIYGSAGLDLAYVAAgrLDAYL-------S 197
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 16758954 272 PNGKlrlLYECNPVAYIIEQAGGMATTgtqpvLDVKPESIHQRVPLILG 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 5.46e-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: 40.89  E-value: 5.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954  34 LLNSMLTAIKAISSAVRKAGLANLygIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAkerrGK 113
Cdd:cd01642   1 MLEVLEKITKEIILLLNEKNRQGL--VKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGS----GE 74
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16758954 114 YVVCFDPLDGSSN-IDCLASIGTIFAIYRKTTEDE 147
Cdd:cd01642  75 YIAVLDPLDGSTNyLSGIPFYSVSVALADPRSKVK 109
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
45-126 8.39e-04

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673  Cd Length: 263  Bit Score: 40.28  E-value: 8.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954   45 ISSAVRKAgLANLYGI--AGSV---NVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAKErrgkYVVCFD 119
Cdd:PRK12676  13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPE----YTVVLD 87

                 ....*..
gi 16758954  120 PLDGSSN 126
Cdd:PRK12676  88 PLDGTYN 94
Inositol_P pfam00459
Inositol monophosphatase family;
39-134 2.64e-03

Inositol monophosphatase family;


Pssm-ID: 395369 [Multi-domain]  Cd Length: 270  Bit Score: 38.86  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758954    39 LTAIKAISSAVRKAGLANLYGI-AGSVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAKERRGKYVVC 117
Cdd:pfam00459   9 AVELAAKAGEVLREAFSNKLTIeEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQSELTDDGPTWI 88
                          90       100
                  ....*....|....*....|..
gi 16758954   118 FDPLDGSSN----IDCLA-SIG 134
Cdd:pfam00459  89 IDPIDGTTNfvhgIPQFAvSIG 110
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
68-126 2.78e-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  Cd Length: 257  Bit Score: 38.90  E-value: 2.78e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16758954  68 GDEVKKLDVLSNSLVINMLQSsYSTCVLVSEENKEAVItakERRGKYVVCFDPLDGSSN 126
Cdd:cd01515  35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEIGVIDN---GDEPEYTVVLDPLDGTYN 89
 
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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