|
Name |
Accession |
Description |
Interval |
E-value |
| FBPase |
cd00354 |
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ... |
18-332 |
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: 531.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 18 VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVS 97
Cdd:cd00354 1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 98 EENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYALYGSATMLVLA 177
Cdd:cd00354 81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 178 MDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVGSMVADIHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506589 258 VYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEFLEIY 332
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
|
|
| PLN02262 |
PLN02262 |
fructose-1,6-bisphosphatase |
9-338 |
2.74e-162 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215147 [Multi-domain] Cd Length: 340 Bit Score: 456.58 E-value: 2.74e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 9 TDISTLTRFVM-EQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLK 87
Cdd:PLN02262 10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 88 SSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYAL 167
Cdd:PLN02262 90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 168 YGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 248 SMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
|
330
....*....|.
gi 9506589 328 FLEIYRKHKAK 338
Cdd:PLN02262 330 IKALYAAEAAK 340
|
|
| Fbp |
COG0158 |
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; |
11-336 |
6.66e-139 |
|
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
Pssm-ID: 223236 [Multi-domain] Cd Length: 326 Bit Score: 396.68 E-value: 6.66e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 11 ISTLTRF-VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSS 89
Cdd:COG0158 1 MKTLGRFlVEKQKEFKAATAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 90 YATCVLVSEENTNAIIIEPEKrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDePSEKDALQPGRDLVAAGYALYG 169
Cdd:COG0158 81 GNVAGIASEEEDEPVTFPENN-GSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 170 SATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLqRKKFPPDGSA--PYGARYVG 247
Cdd:COG0158 159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYI-KDCFAEDKGTrrPYNMRYIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 248 SMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQE 327
Cdd:COG0158 238 SMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEK 317
|
....*....
gi 9506589 328 FLEIYRKHK 336
Cdd:COG0158 318 LERFIKEFP 326
|
|
| FBPase |
pfam00316 |
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ... |
12-198 |
7.01e-103 |
|
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: 300.15 E-value: 7.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 12 STLTRFVMEQGRKA-QGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSY 90
Cdd:pfam00316 1 ITLTRFIIEQQHEFpNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 91 ATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKS-TDEPSEK-DALQPGRDLVAAGYALY 168
Cdd:pfam00316 81 IVKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSpTDSPTTIeDVLQPGNEQVAAGYAMY 160
|
170 180 190
....*....|....*....|....*....|
gi 9506589 169 GSATMLVLAMDCGVNCFMLDPSIGEFIMVD 198
Cdd:pfam00316 161 GSSTMLVLTTGCGVHGFTLDPSLGEFILTH 190
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| FBPase |
cd00354 |
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ... |
18-332 |
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: 531.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 18 VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVS 97
Cdd:cd00354 1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 98 EENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYALYGSATMLVLA 177
Cdd:cd00354 81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 178 MDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVGSMVADIHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506589 258 VYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEFLEIY 332
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
|
|
| PLN02262 |
PLN02262 |
fructose-1,6-bisphosphatase |
9-338 |
2.74e-162 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215147 [Multi-domain] Cd Length: 340 Bit Score: 456.58 E-value: 2.74e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 9 TDISTLTRFVM-EQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLK 87
Cdd:PLN02262 10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 88 SSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYAL 167
Cdd:PLN02262 90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 168 YGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 248 SMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329
|
330
....*....|.
gi 9506589 328 FLEIYRKHKAK 338
Cdd:PLN02262 330 IKALYAAEAAK 340
|
|
| PRK09293 |
PRK09293 |
class 1 fructose-bisphosphatase; |
13-336 |
1.79e-152 |
|
class 1 fructose-bisphosphatase;
Pssm-ID: 236458 [Multi-domain] Cd Length: 327 Bit Score: 431.20 E-value: 1.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 13 TLTRFVMEQGRKAQG-TGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYA 91
Cdd:PRK09293 4 TLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 92 TCVLVSEENTNAIIIePEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKStDEPSEKDALQPGRDLVAAGYALYGSA 171
Cdd:PRK09293 84 VAGLASEEEDEIVPI-PENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLYGPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 172 TMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAIN---EYLQRKKFPpdGSAPYGARYVGS 248
Cdd:PRK09293 162 TMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKkyiELLAGKDGP--RGRPYNMRYIGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 249 MVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEF 328
Cdd:PRK09293 240 MVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERV 319
|
....*...
gi 9506589 329 LEIYRKHK 336
Cdd:PRK09293 320 EEYHAEAP 327
|
|
| Fbp |
COG0158 |
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; |
11-336 |
6.66e-139 |
|
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
Pssm-ID: 223236 [Multi-domain] Cd Length: 326 Bit Score: 396.68 E-value: 6.66e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 11 ISTLTRF-VMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSS 89
Cdd:COG0158 1 MKTLGRFlVEKQKEFKAATAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 90 YATCVLVSEENTNAIIIEPEKrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDePSEKDALQPGRDLVAAGYALYG 169
Cdd:COG0158 81 GNVAGIASEEEDEPVTFPENN-GSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 170 SATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLqRKKFPPDGSA--PYGARYVG 247
Cdd:COG0158 159 PSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYI-KDCFAEDKGTrrPYNMRYIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 248 SMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQE 327
Cdd:COG0158 238 SMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEK 317
|
....*....
gi 9506589 328 FLEIYRKHK 336
Cdd:COG0158 318 LERFIKEFP 326
|
|
| FBPase |
pfam00316 |
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ... |
12-198 |
7.01e-103 |
|
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: 300.15 E-value: 7.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 12 STLTRFVMEQGRKA-QGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSY 90
Cdd:pfam00316 1 ITLTRFIIEQQHEFpNATGELTTLLSAIQLAAKFISRDIRKAGLVNLLGLAGAENVQGDQQKKLDVLADELLKNALKASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 91 ATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKS-TDEPSEK-DALQPGRDLVAAGYALY 168
Cdd:pfam00316 81 IVKVLVSEEEEELIVFEPPKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRRVSpTDSPTTIeDVLQPGNEQVAAGYAMY 160
|
170 180 190
....*....|....*....|....*....|
gi 9506589 169 GSATMLVLAMDCGVNCFMLDPSIGEFIMVD 198
Cdd:pfam00316 161 GSSTMLVLTTGCGVHGFTLDPSLGEFILTH 190
|
|
| PLN02542 |
PLN02542 |
fructose-1,6-bisphosphatase |
10-332 |
1.05e-101 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215298 [Multi-domain] Cd Length: 412 Bit Score: 305.26 E-value: 1.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 10 DISTLTRFVMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSS 89
Cdd:PLN02542 75 EIQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEVFSNCLRSS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 90 YATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYR-----------KKSTDEPSEK---DALQ 155
Cdd:PLN02542 155 GRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSpndecladigdDSTLDSVEQRcivNVCQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 156 PGRDLVAAGYALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPP 235
Cdd:PLN02542 235 PGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKDPG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 236 DGSAPYGARYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQKA 315
Cdd:PLN02542 315 PSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRV 394
|
330
....*....|....*..
gi 9506589 316 PVVMGSSEDVqEFLEIY 332
Cdd:PLN02542 395 PLYIGSVEEV-EKLEKY 410
|
|
| PLN02628 |
PLN02628 |
fructose-1,6-bisphosphatase family protein |
12-332 |
1.58e-83 |
|
fructose-1,6-bisphosphatase family protein
Pssm-ID: 215337 [Multi-domain] Cd Length: 351 Bit Score: 256.65 E-value: 1.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 12 STLTRFVmeqGRKAQGTG-ELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTG----DQVKKLDILSNDLVINML 86
Cdd:PLN02628 18 CTLMEFL---GTEGSNVGdDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSNEIILSSL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 87 KSSYATCVLVSEENTNAIIIEPEkrGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKS------TDEPSEKDALQPGRDL 160
Cdd:PLN02628 95 RNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVeadhlpVEEKAQLNVLQRGSRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 161 VAAGYALYGSATMLVLAMDCGVNCFMLDPSIGEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYL----QRKkfppd 236
Cdd:PLN02628 173 VAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIdtvrQGK----- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 237 GSAP--YGARYVGSMVADIHRTLVYGGIFLypankkSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEIHQK 314
Cdd:PLN02628 248 GQYPkkYSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQR 321
|
330
....*....|....*...
gi 9506589 315 APVVMGSSEDVQEfLEIY 332
Cdd:PLN02628 322 LPLFLGSSEDVLE-LESY 338
|
|
| FBPase_C |
pfam18913 |
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ... |
205-332 |
6.67e-59 |
|
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: 185.51 E-value: 6.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 205 KKGNIYSLNEGYAKDFDPAINEYLQRKKFPpdgsAPYGARYVGSMVADIHRTLVYGGIFLYPANKKSPSGKLRLLYECNP 284
Cdd:pfam18913 1 EEGKIYAINEGNARFWNAPYRAYIDDLVSG----KGYTLRYIGSMVADVHRILLKGGIFLYPADRRSPYGKLRLLYECAP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 9506589 285 IAYVMEKAGGLATTGDKDILDIVPTEIHQKAPVVMGSSEDVQEFLEIY 332
Cdd:pfam18913 77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAYL 124
|
|
| PLN02462 |
PLN02462 |
sedoheptulose-1,7-bisphosphatase |
30-330 |
1.69e-46 |
|
sedoheptulose-1,7-bisphosphatase
Pssm-ID: 215256 [Multi-domain] Cd Length: 304 Bit Score: 159.51 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 30 ELTQLLNSLCTAIKAISSAVRQAgiaqLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENTNAIIIEPE 109
Cdd:PLN02462 14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 110 KRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYrkkstdePSEKDALQPGRDLVAAGYALYGSATMLVLAMDCGVNCFmldp 189
Cdd:PLN02462 90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTTYVVALKDGPGTH---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 190 sigEFIMVDRDVKMKKKGNIySLNEGyaKDFDPA--------------INEYLQRKkfppdgsapYGARYVGSMVADIHR 255
Cdd:PLN02462 159 ---EFLLLDDGKWQHVKETT-EIGEG--KIFSPGnlratfdnpgyeklINYYVSEK---------YTLRYTGGMVPDVYQ 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506589 256 TLVY-GGIFLYPANKKSPSgKLRLLYECNPIAYVMEKAGGLATTGDKD--ILDIVPTEIHQKAPVVMGSSEDVQEFLE 330
Cdd:PLN02462 224 IIVKeKGVFTNVTSPKSKA-KLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEVIRFEE 300
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
35-299 |
2.54e-38 |
|
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: 134.44 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 35 LNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENtNAIIIEPEKRGKY 114
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEES-GVAEEVMGRRDEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 115 VVCFDPLDGSSN-IDCLVSIGTIFGIYrkkstdepsekdalqpgrdlvaagyalygsatmlvlamdcgvncfmldpsige 193
Cdd:cd01636 80 TWVIDPIDGTKNfINGLPFVAVVIAVY----------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 194 fimvdrdvkmkkkgNIYSLNEGYAKDFDPaineylqrKKFPPDGSAPYGARYVGSMVADIHRTLV-YGGIFLYPANKksp 272
Cdd:cd01636 107 --------------VILILAEPSHKRVDE--------KKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK--- 161
|
250 260
....*....|....*....|....*..
gi 9506589 273 sgklRLLYECNPIAYVMEKAGGLATTG 299
Cdd:cd01636 162 ----RRAWDVAASAAIVREAGGIMTDW 184
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
35-300 |
2.32e-23 |
|
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: 96.61 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 35 LNSLCTAIKAISSAVRQAGIAQLYgiAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENTNAIIiepEKRGKY 114
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELT--VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGN---VSDGGR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 115 VVCFDPLDGSSN-IDCLVSIGTIFGIYRKKSTdepsekdalqpgrdlVAAGYALYGsATMLVLAM-DCGVNCFMLDPSIg 192
Cdd:cd01637 76 VWVIDPIDGTTNfVAGLPNFAVSIALYEDGKP---------------VLGVIYDPM-LDELYYAGrGKGAFLNGKKLPL- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 193 efimvdrdVKMKKKGNIYSLNEGYAKDFDPAineylqrKKFPPDGSAPYGARYVGSMVADIHRTLVY-GGIFLYPANKks 271
Cdd:cd01637 139 --------SKDTPLNDALLSTNASMLRSNRA-------AVLASLVNRALGIRIYGSAGLDLAYVAAGrLDAYLSSGLN-- 201
|
250 260
....*....|....*....|....*....
gi 9506589 272 psgklrlLYECNPIAYVMEKAGGLATTGD 300
Cdd:cd01637 202 -------PWDYAAGALIVEEAGGIVTDLD 223
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
45-126 |
8.27e-06 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 46.44 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 45 ISSAVRQAgIAQLYGI--AGST---NVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENTNAIIIEPEkrgkYVVCFD 119
Cdd:PRK12676 13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPE----YTVVLD 87
|
....*..
gi 9506589 120 PLDGSSN 126
Cdd:PRK12676 88 PLDGTYN 94
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
34-147 |
3.40e-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: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 34 LLNSLCTAIKAISSAVR---QAGIAQLYGIAGstnvtGDQVKKLDILSNDLVINMLKSSYATCVLVSEEntnAIIIEPEK 110
Cdd:cd01642 1 MLEVLEKITKEIILLLNeknRQGLVKLIRGAG-----GDVTRVADLKAEEIILKLLREEGVFGQIISEE---SGEIRKGS 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 9506589 111 rGKYVVCFDPLDGSSN-IDCLVSIGTIFGIYRKKSTDE 147
Cdd:cd01642 73 -GEYIAVLDPLDGSTNyLSGIPFYSVSVALADPRSKVK 109
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
30-134 |
9.04e-04 |
|
Inositol monophosphatase family;
Pssm-ID: 425694 [Multi-domain] Cd Length: 271 Bit Score: 40.41 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506589 30 ELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEENTNAIIIEPE 109
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEVLREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAPGDQSEL 80
|
90 100 110
....*....|....*....|....*....|
gi 9506589 110 KRGKYVVCFDPLDGSSN----IDCL-VSIG 134
Cdd:pfam00459 81 TDDGPTWIIDPIDGTTNfvhgIPQFaVSIG 110
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
68-126 |
2.69e-03 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 39.33 E-value: 2.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 9506589 68 GDQVKKLDILSNDLVINMLKSsYATCVLVSEENTNAIIiePEKRGKYVVCFDPLDGSSN 126
Cdd:PRK14076 39 GTPTKRIDLIAENIAINSLEK-FCSGILISEEIGFKKI--GKNKPEYIFVLDPIDGTYN 94
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
68-126 |
4.61e-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: 38.13 E-value: 4.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 9506589 68 GDQVKKLDILSNDLVINMLKSsYATCVLVSEENTnaiIIEPEKRGKYVVCFDPLDGSSN 126
Cdd:cd01515 35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEIG---VIDNGDEPEYTVVLDPLDGTYN 89
|
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|