|
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: 503.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVS 97
Cdd:cd00354 1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 98 EENKEAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354 81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 178 TGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYAARYVGSMVADVHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149755235 258 VYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPDDVQEYL 329
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVE 312
|
|
| PLN02262 |
PLN02262 |
fructose-1,6-bisphosphatase |
9-327 |
2.29e-154 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215147 [Multi-domain] Cd Length: 340 Bit Score: 436.55 E-value: 2.29e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 9 TDMLTLTRYVM-EKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02262 10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 88 SSYSTCVLVSEENKEAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQPGRNIVAAGYAL 167
Cdd:PLN02262 90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 168 YGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYAARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 248 SMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPDDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
|
|
| Fbp |
COG0158 |
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ... |
9-338 |
1.06e-153 |
|
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1,6-bisphosphatase is part of the Pathway/BioSystem: Gluconeogenesis
Pssm-ID: 439928 [Multi-domain] Cd Length: 338 Bit Score: 434.54 E-value: 1.06e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 9 TDMLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:COG0158 2 MKGTTLTQFLIEQQRRFPGaTGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEALE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 88 SSYSTCVLVSEENKEAI-ITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEP-SEKDALQPGRNIVAAGY 165
Cdd:COG0158 82 WGGHVAAMASEEMDDPIpIPEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGGGPvTEEDFLQPGSEQVAAGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 166 ALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQ--KKKFPEDGSAPYAA 243
Cdd:COG0158 162 VLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDecLAGKEGPRGRDFNM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 244 RYVGSMVADVHRTLVYGGIFLYPANQK--SPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGS 321
Cdd:COG0158 242 RWIGSLVADVHRILLRGGIFLYPADSRdgYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILGS 321
|
330
....*....|....*..
gi 149755235 322 PDDVQEYLTCVQKNQAG 338
Cdd:COG0158 322 KEEVERVERYHAEPDAS 338
|
|
| FBPase |
pfam00316 |
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ... |
13-197 |
3.50e-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: 267.79 E-value: 3.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQSSYS 91
Cdd:pfam00316 2 TLTRFIIEQQHEFPnATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 92 TCVLVSEENKEAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSE-DEPSEK-DALQPGRNIVAAGYALYG 169
Cdd:pfam00316 82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPTTIeDVLQPGNEQVAAGYAMYG 161
|
170 180
....*....|....*....|....*...
gi 149755235 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, ... |
18-329 |
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: 503.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 18 VMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVS 97
Cdd:cd00354 1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 98 EENKEAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQPGRNIVAAGYALYGSATLVALS 177
Cdd:cd00354 81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 178 TGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYAARYVGSMVADVHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149755235 258 VYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPDDVQEYL 329
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVE 312
|
|
| PLN02262 |
PLN02262 |
fructose-1,6-bisphosphatase |
9-327 |
2.29e-154 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215147 [Multi-domain] Cd Length: 340 Bit Score: 436.55 E-value: 2.29e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 9 TDMLTLTRYVM-EKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02262 10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 88 SSYSTCVLVSEENKEAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQPGRNIVAAGYAL 167
Cdd:PLN02262 90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 168 YGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYAARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 248 SMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPDDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
|
|
| Fbp |
COG0158 |
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ... |
9-338 |
1.06e-153 |
|
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1,6-bisphosphatase is part of the Pathway/BioSystem: Gluconeogenesis
Pssm-ID: 439928 [Multi-domain] Cd Length: 338 Bit Score: 434.54 E-value: 1.06e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 9 TDMLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:COG0158 2 MKGTTLTQFLIEQQRRFPGaTGELSALLNAIALAAKIISREVNKGGLAGILGAAGSENVQGETQKKLDVIANEIFIEALE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 88 SSYSTCVLVSEENKEAI-ITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEP-SEKDALQPGRNIVAAGY 165
Cdd:COG0158 82 WGGHVAAMASEEMDDPIpIPEQYPRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGGGPvTEEDFLQPGSEQVAAGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 166 ALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQ--KKKFPEDGSAPYAA 243
Cdd:COG0158 162 VLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDecLAGKEGPRGRDFNM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 244 RYVGSMVADVHRTLVYGGIFLYPANQK--SPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGS 321
Cdd:COG0158 242 RWIGSLVADVHRILLRGGIFLYPADSRdgYPPGKLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVPLILGS 321
|
330
....*....|....*..
gi 149755235 322 PDDVQEYLTCVQKNQAG 338
Cdd:COG0158 322 KEEVERVERYHAEPDAS 338
|
|
| PRK09293 |
PRK09293 |
class 1 fructose-bisphosphatase; |
10-327 |
1.15e-143 |
|
class 1 fructose-bisphosphatase;
Pssm-ID: 236458 [Multi-domain] Cd Length: 327 Bit Score: 408.85 E-value: 1.15e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 10 DMLTLTRYVMEKGRQAKG-TGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQS 88
Cdd:PRK09293 1 SMKTLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 89 SYSTCVLVSEEnKEAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSeDEPSEKDALQPGRNIVAAGYALY 168
Cdd:PRK09293 81 RGHVAGLASEE-EDEIVPIPENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 169 GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQ-KKKFPEDGSAPYAARYVG 247
Cdd:PRK09293 159 GPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIElLAGKDGPRGRPYNMRYIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 248 SMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPDDVQE 327
Cdd:PRK09293 239 SMVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVER 318
|
|
| PLN02542 |
PLN02542 |
fructose-1,6-bisphosphatase |
2-327 |
1.49e-96 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215298 [Multi-domain] Cd Length: 412 Bit Score: 292.16 E-value: 1.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 2 TDRSPFEtdMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSL 81
Cdd:PLN02542 69 TKKSGYE--IQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 82 VINMLQSSYSTCVLVSEENKEAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSE-----------DEPSE 150
Cdd:PLN02542 147 FSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDEcladigddstlDSVEQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 151 K---DALQPGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEY 227
Cdd:PLN02542 227 RcivNVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKY 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 228 VQKKKFPEDGSAPYAARYVGSMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVK 307
Cdd:PLN02542 307 IDDLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQ 386
|
330 340
....*....|....*....|
gi 149755235 308 PEAIHQRVPLILGSPDDVQE 327
Cdd:PLN02542 387 PTEIHQRVPLYIGSVEEVEK 406
|
|
| FBPase |
pfam00316 |
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ... |
13-197 |
3.50e-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: 267.79 E-value: 3.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 13 TLTRYVMEKGRQAK-GTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQSSYS 91
Cdd:pfam00316 2 TLTRFIIEQQHEFPnATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 92 TCVLVSEENKEAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSE-DEPSEK-DALQPGRNIVAAGYALYG 169
Cdd:pfam00316 82 VKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSPtDSPTTIeDVLQPGNEQVAAGYAMYG 161
|
170 180
....*....|....*....|....*...
gi 149755235 170 SATLVALSTGQGVDLFMLDPALGEFVLV 197
Cdd:pfam00316 162 SSTMLVLTTGCGVHGFTLDPSLGEFILT 189
|
|
| PLN02628 |
PLN02628 |
fructose-1,6-bisphosphatase family protein |
13-327 |
7.74e-78 |
|
fructose-1,6-bisphosphatase family protein
Pssm-ID: 215337 [Multi-domain] Cd Length: 351 Bit Score: 242.01 E-value: 7.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 13 TLTRYVmekGRQAKGTG-ELTQLLNSMLTAIKAISSAVRKAGLA----HLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQ 87
Cdd:PLN02628 19 TLMEFL---GTEGSNVGdDLVVLMAHIQAACKRIAALLASPFNSelgkTSSGASGASGSGRDAPKPLDIVSNEIILSSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 88 SSYSTCVLVSEENKEAIITAKEkrGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSE------DEPSEKDALQPGRNIV 161
Cdd:PLN02628 96 NSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEadhlpvEEKAQLNVLQRGSRLV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 162 AAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEgyAKYFD--AATTEYVQ-----KKKFP 234
Cdd:PLN02628 174 AAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVND--ARYFDwpEGLRKYIDtvrqgKGQYP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 235 EDgsapYAARYVGSMVADVHRTLVYGGIFLYPANQkspkgkLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQR 314
Cdd:PLN02628 252 KK----YSARYICSLVADLHRTILYGGIAMNPRSH------LRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQR 321
|
330
....*....|...
gi 149755235 315 VPLILGSPDDVQE 327
Cdd:PLN02628 322 LPLFLGSSEDVLE 334
|
|
| FBPase_C |
pfam18913 |
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ... |
209-333 |
2.18e-61 |
|
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: 192.06 E-value: 2.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 209 IYSLNEGYAKYFDAATTEYVQKKKFPEdgsaPYAARYVGSMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI 288
Cdd:pfam18913 5 IYAINEGNARFWNAPYRAYIDDLVSGK----GYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGKLRLLYECAPLAFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 149755235 289 IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPDDVQEYLTCVQ 333
Cdd:pfam18913 81 IEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAYLK 125
|
|
| PLN02462 |
PLN02462 |
sedoheptulose-1,7-bisphosphatase |
30-328 |
4.18e-43 |
|
sedoheptulose-1,7-bisphosphatase
Pssm-ID: 215256 [Multi-domain] Cd Length: 304 Bit Score: 151.04 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 30 ELTQLLNSMLTAIKAISSAVRKAglahLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAIITAKE 109
Cdd:PLN02462 14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 110 KRGKYVVCFDPLDGSSNIDCLASIGTIFAIYrktsedePSEKDALQPGRNIVAAGYALYGSAT--LVALSTGQGVDLFML 187
Cdd:PLN02462 90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTtyVVALKDGPGTHEFLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 188 DPAlGEFVLVEkDVKIKKKGKIYSL--------NEGYAKYFDaattEYVQKKkfpedgsapYAARYVGSMVADVHRTLVY 259
Cdd:PLN02462 163 LDD-GKWQHVK-ETTEIGEGKIFSPgnlratfdNPGYEKLIN----YYVSEK---------YTLRYTGGMVPDVYQIIVK 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149755235 260 -GGIFLYPANQKSPkGKLRLLYECNPVAYIIEQAGGLATTGTQP--VLDVKPEAIHQRVPLILGSPDDVQEY 328
Cdd:PLN02462 228 eKGVFTNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEVIRF 298
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
35-299 |
9.99e-32 |
|
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: 117.49 E-value: 9.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 35 LNSMLTAIKAISSAVRKAGLAHLYGIAGTVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAIITAkEKRGKY 114
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVM-GRRDEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 115 VVCFDPLDGSSN-IDCLASIGTIFAIYRktsedepsekdalqpgrnivaagyalygsatlvalstgqgvdlfmldpalge 193
Cdd:cd01636 80 TWVIDPIDGTKNfINGLPFVAVVIAVYV---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 194 fvlvekdvkikkkgkIYSLNEGYAKYFDaatteyvqKKKFPEDGSAPYAARYVGSMVADVHRTLV-YGGIFLYPANQksp 272
Cdd:cd01636 108 ---------------ILILAEPSHKRVD--------EKKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK--- 161
|
250 260
....*....|....*....|....*..
gi 149755235 273 kgklRLLYECNPVAYIIEQAGGLATTG 299
Cdd:cd01636 162 ----RRAWDVAASAAIVREAGGIMTDW 184
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
35-320 |
6.28e-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: 78.90 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 35 LNSMLTAIKAISSAVRKAGLAHLYgiAGTVNVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAIITAkekRGKY 114
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELT--VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVS---DGGR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 115 VVCFDPLDGSSN-IDCLASIGTIFAIYRKtsedepsekdalqpGR------NIVAAGYALYGSATLVALSTGQGVDLFMl 187
Cdd:cd01637 76 VWVIDPIDGTTNfVAGLPNFAVSIALYED--------------GKpvlgviYDPMLDELYYAGRGKGAFLNGKKLPLSK- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 188 DPALGEFVLvekdvkikkkgkiySLNEGYAKYFDAAtteyvqkkKFPEDGSAPYAARYVGSMVADVHRTLVY-GGIFLYP 266
Cdd:cd01637 141 DTPLNDALL--------------STNASMLRSNRAA--------VLASLVNRALGIRIYGSAGLDLAYVAAGrLDAYLSS 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 149755235 267 ANQkspkgklrlLYECNPVAYIIEQAGGLATTgtqpvLDVKPEAIHQRVPLILG 320
Cdd:cd01637 199 GLN---------PWDYAAGALIVEEAGGIVTD-----LDGEPLDTLNRSGIIAA 238
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
34-147 |
2.84e-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: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 34 LLNSMLTAIKAISSAVRKAGLAHLYGiagtvnVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAiitaKEKRGK 113
Cdd:cd01642 5 LEKITKEIILLLNEKNRQGLVKLIRG------AGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEI----RKGSGE 74
|
90 100 110
....*....|....*....|....*....|....*
gi 149755235 114 YVVCFDPLDGSSN-IDCLASIGTIFAIYRKTSEDE 147
Cdd:cd01642 75 YIAVLDPLDGSTNyLSGIPFYSVSVALADPRSKVK 109
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
42-134 |
4.69e-04 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 41.18 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 42 IKAISSAVRKAG--LAHLYGIAGTVNVTG-----DEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAIITAKEKRGKY 114
Cdd:pfam00459 6 LKVAVELAAKAGeiLREAFSNKLTIEEKGksganDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDDGP 85
|
90 100
....*....|....*....|....*
gi 149755235 115 VVCFDPLDGSSN----IDCLA-SIG 134
Cdd:pfam00459 86 TWIIDPIDGTKNfvhgIPQFAvSIG 110
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
68-126 |
5.52e-04 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 41.64 E-value: 5.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 149755235 68 GDEVKKLDVLSNSLVINMLQSSYSTcVLVSEENKEAIItaKEKRGKYVVCFDPLDGSSN 126
Cdd:PRK14076 39 GTPTKRIDLIAENIAINSLEKFCSG-ILISEEIGFKKI--GKNKPEYIFVLDPIDGTYN 94
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
45-126 |
1.02e-03 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 40.28 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149755235 45 ISSAVRKAgLAHLYGI--AGTV---NVTGDEVKKLDVLSNSLVINMLQSSYSTCVLVSEENKEAIItakeKRGKYVVCFD 119
Cdd:PRK12676 13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVG----NGPEYTVVLD 87
|
....*..
gi 149755235 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 |
3.19e-03 |
|
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles.
Pssm-ID: 238773 [Multi-domain] Cd Length: 257 Bit Score: 38.51 E-value: 3.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 149755235 68 GDEVKKLDVLSNSLVINMLQSsYSTCVLVSEENKEAIItakEKRGKYVVCFDPLDGSSN 126
Cdd:cd01515 35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEIGVIDN---GDEPEYTVVLDPLDGTYN 89
|
|
| |
