NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|512967936|ref|XP_004846134|]
View 

fructose-1,6-bisphosphatase isozyme 2 isoform X1 [Heterocephalus glaber]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
18-275 1.05e-142

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: 406.17  E-value: 1.05e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSSYSTCVLVS 97
Cdd:cd00354    1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  98 EENKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEEEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354   81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 178 TGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354  161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                        250
                 ....*....|....*...
gi 512967936 258 VYGGIFLYPANQKSPKGK 275
Cdd:cd00354  241 VRGGIFLYPADKKSPKGK 258
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
18-275 1.05e-142

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: 406.17  E-value: 1.05e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSSYSTCVLVS 97
Cdd:cd00354    1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  98 EENKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEEEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354   81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 178 TGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354  161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                        250
                 ....*....|....*...
gi 512967936 258 VYGGIFLYPANQKSPKGK 275
Cdd:cd00354  241 VRGGIFLYPADKKSPKGK 258
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-275 5.48e-123

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 357.19  E-value: 5.48e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936   9 TDMLTLTRYVM-EKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQ 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  88 SSYSTCVLVSEENKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEEEPSEKDALQPGRNIVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 168 YGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260
                 ....*....|....*....|....*...
gi 512967936 248 SMVADVHRTLVYGGIFLYPANQKSPKGK 275
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGK 277
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
11-275 1.22e-96

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


Pssm-ID: 223236 [Multi-domain]  Cd Length: 326  Bit Score: 289.60  E-value: 1.22e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  11 MLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSS 89
Cdd:COG0158    1 MKTLGRFLVEKQKEFKAaTAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  90 YSTCVLVSEEnKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEEePSEKDALQPGRNIVAAGYALYG 169
Cdd:COG0158   81 GNVAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 170 SATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSA-PYGARYVGS 248
Cdd:COG0158  159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDKGTRrPYNMRYIGS 238
                        250       260
                 ....*....|....*....|....*..
gi 512967936 249 MVADVHRTLVYGGIFLYPANQKSPKGK 275
Cdd:COG0158  239 MVADVHRILLKGGIFLYPSDKRAPNGK 265
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
13-197 1.72e-90

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: 268.94  E-value: 1.72e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936   13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSSYS 91
Cdd:pfam00316   2 TLTRFIIEQQHEFPnATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936   92 TCVLVSEENKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEE-EPSEK-DALQPGRNIVAAGYALYG 169
Cdd:pfam00316  82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPTdSPTTIeDVLQPGNEQVAAGYAMYG 161
                         170       180
                  ....*....|....*....|....*...
gi 512967936  170 SATLVALSTGQGVDLFMLDPALGEFVLV 197
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILT 189
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
18-275 1.05e-142

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: 406.17  E-value: 1.05e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSSYSTCVLVS 97
Cdd:cd00354    1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  98 EENKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEEEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354   81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 178 TGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354  161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                        250
                 ....*....|....*...
gi 512967936 258 VYGGIFLYPANQKSPKGK 275
Cdd:cd00354  241 VRGGIFLYPADKKSPKGK 258
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-275 5.48e-123

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 357.19  E-value: 5.48e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936   9 TDMLTLTRYVM-EKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQ 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  88 SSYSTCVLVSEENKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEEEPSEKDALQPGRNIVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 168 YGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260
                 ....*....|....*....|....*...
gi 512967936 248 SMVADVHRTLVYGGIFLYPANQKSPKGK 275
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGK 277
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
10-275 4.91e-105

class 1 fructose-bisphosphatase;


Pssm-ID: 236458 [Multi-domain]  Cd Length: 327  Bit Score: 311.01  E-value: 4.91e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  10 DMLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQS 88
Cdd:PRK09293   1 SMKTLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  89 SYSTCVLVSEEnKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEEePSEKDALQPGRNIVAAGYALY 168
Cdd:PRK09293  81 RGHVAGLASEE-EDEIVPIPENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPVGT-PTEEDFLQPGNNQVAAGYVLY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 169 GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEYVQ-KKKFPEDGSAPYGARYVG 247
Cdd:PRK09293 159 GPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIElLAGKDGPRGRPYNMRYIG 238
                        250       260
                 ....*....|....*....|....*...
gi 512967936 248 SMVADVHRTLVYGGIFLYPANQKSPKGK 275
Cdd:PRK09293 239 SMVADVHRILLKGGIFLYPADEPYPNGK 266
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
11-275 1.22e-96

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


Pssm-ID: 223236 [Multi-domain]  Cd Length: 326  Bit Score: 289.60  E-value: 1.22e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  11 MLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSS 89
Cdd:COG0158    1 MKTLGRFLVEKQKEFKAaTAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  90 YSTCVLVSEEnKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEEePSEKDALQPGRNIVAAGYALYG 169
Cdd:COG0158   81 GNVAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 170 SATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEYVQKKKFPEDGSA-PYGARYVGS 248
Cdd:COG0158  159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDKGTRrPYNMRYIGS 238
                        250       260
                 ....*....|....*....|....*..
gi 512967936 249 MVADVHRTLVYGGIFLYPANQKSPKGK 275
Cdd:COG0158  239 MVADVHRILLKGGIFLYPSDKRAPNGK 265
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
13-197 1.72e-90

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: 268.94  E-value: 1.72e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936   13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSSYS 91
Cdd:pfam00316   2 TLTRFIIEQQHEFPnATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936   92 TCVLVSEENKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTEE-EPSEK-DALQPGRNIVAAGYALYG 169
Cdd:pfam00316  82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPTdSPTTIeDVLQPGNEQVAAGYAMYG 161
                         170       180
                  ....*....|....*....|....*...
gi 512967936  170 SATLVALSTGQGVDLFMLDPALGEFVLV 197
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILT 189
PLN02542 PLN02542
fructose-1,6-bisphosphatase
2-275 4.44e-69

fructose-1,6-bisphosphatase


Pssm-ID: 215298 [Multi-domain]  Cd Length: 412  Bit Score: 221.67  E-value: 4.44e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936   2 TDRSPFEtdMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNAL 81
Cdd:PLN02542  69 TKKSGYE--IQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  82 VINMLQSSYSTCVLVSEENKEAIITSQERRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTE--------------EE 147
Cdd:PLN02542 147 FSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDEcladigddstldsvEQ 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 148 PSEKDALQPGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEGYAKYFDAATTEY 227
Cdd:PLN02542 227 RCIVNVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKY 306
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 512967936 228 VQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFLYPANQKSPKGK 275
Cdd:PLN02542 307 IDDLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGK 354
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
13-269 1.93e-53

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337 [Multi-domain]  Cd Length: 351  Bit Score: 179.22  E-value: 1.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  13 TLTRYVmekGRQAKGTG-ELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTG----DEVKKLDVLSNALVINMLQ 87
Cdd:PLN02628  19 TLMEFL---GTEGSNVGdDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSNEIILSSLR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  88 SSYSTCVLVSEENKEAIITSQErrGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTE------EEPSEKDALQPGRNIV 161
Cdd:PLN02628  96 NSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEadhlpvEEKAQLNVLQRGSRLV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 162 AAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIFSLNEgyAKYFD--AATTEYVQ-----KKKFP 234
Cdd:PLN02628 174 AAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVND--ARYFDwpEGLRKYIDtvrqgKGQYP 251
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 512967936 235 EDgsapYGARYVGSMVADVHRTLVYGGIFLYPANQ 269
Cdd:PLN02628 252 KK----YSARYICSLVADLHRTILYGGIAMNPRSH 282
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
30-272 5.30e-29

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256 [Multi-domain]  Cd Length: 304  Bit Score: 113.67  E-value: 5.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  30 ELTQLLNSMLTAIKAISSAVRKAglahLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSSYSTCVLVSEENKEAIITSQE 109
Cdd:PLN02462  14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 110 RRGKYVVCFDPLDGSSNIDCLASIGTIFAIYrktteeePSEKDALQPGRNIVAAGYALYGSAT--LVALSTGQGVDLFML 187
Cdd:PLN02462  90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTtyVVALKDGPGTHEFLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 188 DPAlGEFVLVEkDVKIKKKGKIFSL--------NEGYAKYFDaattEYVQKKkfpedgsapYGARYVGSMVADVHRTLVY 259
Cdd:PLN02462 163 LDD-GKWQHVK-ETTEIGEGKIFSPgnlratfdNPGYEKLIN----YYVSEK---------YTLRYTGGMVPDVYQIIVK 227
                        250
                 ....*....|....
gi 512967936 260 -GGIFLYPANQKSP 272
Cdd:PLN02462 228 eKGVFTNVTSPKSK 241
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
35-278 1.94e-28

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: 108.63  E-value: 1.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  35 LNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNALVINMLQSSYSTCVLVSEENKEAIITSqERRGKY 114
Cdd:cd01636    1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVM-GRRDEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 115 VVCFDPLDGSSNID-CLASIGTIFAIYRKTTEEEPSEKDalqpgrnivaagyalygsatlvalstgqgvdlfmldpalge 193
Cdd:cd01636   80 TWVIDPIDGTKNFInGLPFVAVVIAVYVILILAEPSHKR----------------------------------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 194 fvlvekdvkikkkgkifslnegyakyfdaatteyVQKKKFPEDGSAPYGARYVGSMVADVHRTLV-YGGIFLYPAnqksP 272
Cdd:cd01636  119 ----------------------------------VDEKKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPG----G 160

                 ....*.
gi 512967936 273 KGKPPE 278
Cdd:cd01636  161 KRRAWD 166
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
209-275 2.57e-24

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: 95.76  E-value: 2.57e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512967936  209 IFSLNEGYAKYFDAATTEYVQKKKFPEdgsaPYGARYVGSMVADVHRTLVYGGIFLYPANQKSPKGK 275
Cdd:pfam18913   5 IYAINEGNARFWNAPYRAYIDDLVSGK----GYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGK 67
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
35-270 7.69e-16

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: 75.81  E-value: 7.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  35 LNSMLTAIKAISSAVRKAGLAHLYGIAGSVNvtGDEVKKLDVLSNALVINMLQSSYSTCVLVSEENKEAIITSqerRGKY 114
Cdd:cd01637    1 LELALKAVREAGALILEAFGEELTVETKKGD--GDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVS---DGGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 115 VVCFDPLDGSSN-IDCLASIGTIFAIYRKtteeepsekdalqpGR------NIVAAGYALYGSATLVALSTGQGVDLFMl 187
Cdd:cd01637   76 VWVIDPIDGTTNfVAGLPNFAVSIALYED--------------GKpvlgviYDPMLDELYYAGRGKGAFLNGKKLPLSK- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936 188 DPALGEFVLvekdvkikkkgkifSLNEGYAKYFDAAtteyvqkkKFPEDGSAPYGARYVGSMVADVHRTLVY-GGIFLYP 266
Cdd:cd01637  141 DTPLNDALL--------------STNASMLRSNRAA--------VLASLVNRALGIRIYGSAGLDLAYVAAGrLDAYLSS 198

                 ....
gi 512967936 267 ANQK 270
Cdd:cd01637  199 GLNP 202
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
45-126 2.31e-04

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 42.20  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  45 ISSAVRKAgLAHLYGI--AGSV---NVTGDEVKKLDVLSNALVINMLQSSYSTCVLVSEENKEAIITSQErrgkYVVCFD 119
Cdd:PRK12676  13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPE----YTVVLD 87

                 ....*..
gi 512967936 120 PLDGSSN 126
Cdd:PRK12676  88 PLDGTYN 94
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
34-142 3.48e-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: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936  34 LLNSMLTAIKAISSAVRKAGLAHLYGiagsvnVTGDEVKKLDVLSNALVINMLQSSYSTCVLVSEEnkeaiitSQERRGK 113
Cdd:cd01642    5 LEKITKEIILLLNEKNRQGLVKLIRG------AGGDVTRVADLKAEEIILKLLREEGVFGQIISEE-------SGEIRKG 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 512967936 114 ---YVVCFDPLDGSSN-IDCLASIGTIFAIYRK 142
Cdd:cd01642   72 sgeYIAVLDPLDGSTNyLSGIPFYSVSVALADP 104
Inositol_P pfam00459
Inositol monophosphatase family;
42-134 5.02e-04

Inositol monophosphatase family;


Pssm-ID: 425694 [Multi-domain]  Cd Length: 271  Bit Score: 41.18  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512967936   42 IKAISSAVRKAG--LAHLYGIAGSVNVTG-----DEVKKLDVLSNALVINMLQSSYSTCVLVSEENKEAIITSQERRGKY 114
Cdd:pfam00459   6 LKVAVELAAKAGevLREAFSNKLTIEEKGksganDLVTAADKAAEELILEALAALFPSHKIIGEEGGAPGDQSELTDDGP 85
                          90       100
                  ....*....|....*....|....*
gi 512967936  115 VVCFDPLDGSSN----IDCLA-SIG 134
Cdd:pfam00459  86 TWIIDPIDGTTNfvhgIPQFAvSIG 110
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
68-126 7.89e-04

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 41.25  E-value: 7.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 512967936  68 GDEVKKLDVLSNALVINMLQSSYSTcVLVSEENKEAIITsqERRGKYVVCFDPLDGSSN 126
Cdd:PRK14076  39 GTPTKRIDLIAENIAINSLEKFCSG-ILISEEIGFKKIG--KNKPEYIFVLDPIDGTYN 94
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
68-126 7.45e-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: 37.36  E-value: 7.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 512967936  68 GDEVKKLDVLSNALVINMLQSsYSTCVLVSEENKEAIItsqERRGKYVVCFDPLDGSSN 126
Cdd:cd01515   35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEIGVIDN---GDEPEYTVVLDPLDGTYN 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH