|
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
|
|
|