|
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 [Multi-domain] 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 |
1.25e-161 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215147 [Multi-domain] Cd Length: 340 Bit Score: 455.03 E-value: 1.25e-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 |
1.90e-140 |
|
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
Pssm-ID: 223236 [Multi-domain] Cd Length: 326 Bit Score: 400.54 E-value: 1.90e-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 |
2.61e-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: 268.17 E-value: 2.61e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYS 91
Cdd:pfam00316 2 TLTRFIIEQQHEFPnATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 92 TCVLVSEENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTE-DEPSEK-DALQPGRNIVAAGYALYG 169
Cdd:pfam00316 82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPTTIeDVLQPGNEQVAAGYAMYG 161
|
170 180 190
....*....|....*....|....*....|
gi 524957055 170 SATLVALSTGQGVDLFMLDPALGEFVLVEK 199
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILTHE 191
|
|
|
|
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 [Multi-domain] 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 |
1.25e-161 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215147 [Multi-domain] Cd Length: 340 Bit Score: 455.03 E-value: 1.25e-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 |
2.46e-153 |
|
class 1 fructose-bisphosphatase;
Pssm-ID: 236458 [Multi-domain] Cd Length: 327 Bit Score: 433.12 E-value: 2.46e-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 |
1.90e-140 |
|
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
Pssm-ID: 223236 [Multi-domain] Cd Length: 326 Bit Score: 400.54 E-value: 1.90e-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 |
5.95e-105 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215298 [Multi-domain] Cd Length: 412 Bit Score: 313.73 E-value: 5.95e-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 |
2.61e-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: 268.17 E-value: 2.61e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLANLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQSSYS 91
Cdd:pfam00316 2 TLTRFIIEQQHEFPnATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 92 TCVLVSEENKEAVITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTTE-DEPSEK-DALQPGRNIVAAGYALYG 169
Cdd:pfam00316 82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPTTIeDVLQPGNEQVAAGYAMYG 161
|
170 180 190
....*....|....*....|....*....|
gi 524957055 170 SATLVALSTGQGVDLFMLDPALGEFVLVEK 199
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILTHE 191
|
|
| PLN02628 |
PLN02628 |
fructose-1,6-bisphosphatase family protein |
13-327 |
6.16e-85 |
|
fructose-1,6-bisphosphatase family protein
Pssm-ID: 215337 [Multi-domain] Cd Length: 351 Bit Score: 260.11 E-value: 6.16e-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 ... |
205-333 |
1.42e-64 |
|
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: 200.15 E-value: 1.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 205 KKGKIFSLNEGYAKYFDAATTEYVQKKKFPEdgsaPYGARYVGSMVADVHRTLVYGGIFMYPANQKSPNGKLRLLYECNP 284
Cdd:pfam18913 1 EEGKIYAINEGNARFWNAPYRAYIDDLVSGK----GYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGKLRLLYECAP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 524957055 285 VAYIIEQAGGMATTGTQPVLDVKPETIHQRVPLILGSPEDVQEYLTCVQ 333
Cdd:pfam18913 77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAYLK 125
|
|
| PLN02462 |
PLN02462 |
sedoheptulose-1,7-bisphosphatase |
30-328 |
7.86e-48 |
|
sedoheptulose-1,7-bisphosphatase
Pssm-ID: 215256 [Multi-domain] Cd Length: 304 Bit Score: 162.98 E-value: 7.86e-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 |
3.56e-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: 3.56e-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 |
7.70e-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: 7.70e-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 |
3.17e-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: 3.17e-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
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
68-126 |
5.02e-04 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 41.64 E-value: 5.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 524957055 68 GDEVKKLDVLSNSLVINMLQSSYSTcVLVSEENKEAVItaKEKRGKYVVCFDPLDGSSN 126
Cdd:PRK14076 39 GTPTKRIDLIAENIAINSLEKFCSG-ILISEEIGFKKI--GKNKPEYIFVLDPIDGTYN 94
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
45-126 |
5.61e-04 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 41.05 E-value: 5.61e-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 |
9.62e-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 [Multi-domain] Cd Length: 257 Bit Score: 40.05 E-value: 9.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 524957055 68 GDEVKKLDVLSNSLVINMLQSsYSTCVLVSEENKEAVItakEKRGKYVVCFDPLDGSSN 126
Cdd:cd01515 35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEIGVIDN---GDEPEYTVVLDPLDGTYN 89
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
42-134 |
3.00e-03 |
|
Inositol monophosphatase family;
Pssm-ID: 425694 [Multi-domain] Cd Length: 271 Bit Score: 38.87 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524957055 42 IKAISSAVRKAG--LANLYGIAGSVNVTG-----DEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAVITAKEKRGKY 114
Cdd:pfam00459 6 LKVAVELAAKAGevLREAFSNKLTIEEKGksganDLVTAADKAAEELILEALAALFPSHKIIGEEGGAPGDQSELTDDGP 85
|
90 100
....*....|....*....|....*
gi 524957055 115 VVCFDPLDGSSN----IDCLA-SIG 134
Cdd:pfam00459 86 TWIIDPIDGTTNfvhgIPQFAvSIG 110
|
|
|