|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02628 |
PLN02628 |
fructose-1,6-bisphosphatase family protein |
49-404 |
0e+00 |
|
fructose-1,6-bisphosphatase family protein
Pssm-ID: 215337 [Multi-domain] Cd Length: 351 Bit Score: 693.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 49 STSFKPLavgrNLTGDDDDGYCTLIDFAGSgggEGKNVGEDLVVLLYHLQHACKRIASLVASPFNSSLGKLS--VNSSSG 126
Cdd:PLN02628 1 MASAPPL----YTAARGAEGVCTLMEFLGT---EGSNVGDDLVVLMAHIQAACKRIAALLASPFNSELGKTSsgASGASG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 127 SDRDAPKPLDIVSNDIVLSSLRNSGKVAVMASEENDSPTWIKDDGPYVVVVDPLDGSRNIDASIPTGTIFGIYNRLVELD 206
Cdd:PLN02628 74 SGRDAPKPLDIVSNEIILSSLRNSGKVAVMASEEDDAPIWIGDDGPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 207 HLPVEEKAELNSLQRGSRLVASGYVLYSSATIFCVTLGSGTHAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWP 286
Cdd:PLN02628 154 HLPVEEKAQLNVLQRGSRLVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 287 EGLRKYIDTVRQGKGQNPKKYSARYICSLVADLHRTLLYGGVAMNPRDHLRLVYEGNPLAFLVEQAGGKSSDGKRGILSI 366
Cdd:PLN02628 234 EGLRKYIDTVRQGKGQYPKKYSARYICSLVADLHRTILYGGIAMNPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSI 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 15237685 367 QPVKLHQRLPLFLGSLEDVAELESYGDVQQTVNPGYEV 404
Cdd:PLN02628 314 QPVKLHQRLPLFLGSSEDVLELESYGDVQQKVNPGYEV 351
|
|
| FBPase |
cd00354 |
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ... |
72-391 |
2.89e-147 |
|
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: 420.04 E-value: 2.89e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 72 LIDFAGSGGGEGknvgeDLVVLLYHLQHACKRIASLVASPFNSslGKLSVNSSSGSDRDAPKPLDIVSNDIVLSSLRNSG 151
Cdd:cd00354 1 LLEQLRKGAATG-----DLTDLLSSLALACKEISRAVRRAGLA--GLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 152 KVAVMASEENDSPTWIKD--DGPYVVVVDPLDGSRNIDASIPTGTIFGIYNRLVELDHlpveekAELNSLQRGSRLVASG 229
Cdd:cd00354 74 VVAVLASEEEEEPVPVEEskDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADA------TEKDFLQPGRNQVAAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 230 YVLYSSATIFCVTLGSGTHAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWPEGLRKYIDTVRQGKGQNpKKYSA 309
Cdd:cd00354 148 YALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGG-KPYNL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 310 RYICSLVADLHRTLLYGGVAMNPRD------HLRLVYEGNPLAFLVEQAGGKSSDGKRGILSIQPVKLHQRLPLFLGSLE 383
Cdd:cd00354 227 RYIGSMVADVHRILVRGGIFLYPADkkspkgKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKE 306
|
....*...
gi 15237685 384 DVAELESY 391
Cdd:cd00354 307 EVERVEEY 314
|
|
| Fbp |
COG0158 |
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ... |
71-391 |
1.12e-129 |
|
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: 376.38 E-value: 1.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 71 TLIDFAGSGGGEGKNVGEDLVVLLYHLQHACKRIASLVAS-PFNSSLGKL-SVNSssgsDRDAPKPLDIVSNDIVLSSLR 148
Cdd:COG0158 6 TLTQFLIEQQRRFPGATGELSALLNAIALAAKIISREVNKgGLAGILGAAgSENV----QGETQKKLDVIANEIFIEALE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 149 NSGKVAVMASEENDSPTWIKD---DGPYVVVVDPLDGSRNIDASIPTGTIFGIYNRLVELDHLPVEEkaelnSLQRGSRL 225
Cdd:COG0158 82 WGGHVAAMASEEMDDPIPIPEqypRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGGGPVTEED-----FLQPGSEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 226 VASGYVLYSSATIFCVTLGSGTHAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWPEGLRKYIDTVRQGK-GQNP 304
Cdd:COG0158 157 VAAGYVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDECLAGKeGPRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 305 KKYSARYICSLVADLHRTLLYGGVAMNPRDH--------LRLVYEGNPLAFLVEQAGGKSSDGKRGILSIQPVKLHQRLP 376
Cdd:COG0158 237 RDFNMRWIGSLVADVHRILLRGGIFLYPADSrdgyppgkLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVP 316
|
330
....*....|....*
gi 15237685 377 LFLGSLEDVAELESY 391
Cdd:COG0158 317 LILGSKEEVERVERY 331
|
|
| FBPase_C |
pfam18913 |
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ... |
271-391 |
7.51e-49 |
|
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: 161.63 E-value: 7.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 271 RGQIYSVNDARYFDWPEGLRKYIDTVRQGKGqnpkkYSARYICSLVADLHRTLLYGGVAMNPRDH------LRLVYEGNP 344
Cdd:pfam18913 2 EGKIYAINEGNARFWNAPYRAYIDDLVSGKG-----YTLRYIGSMVADVHRILLKGGIFLYPADRrspygkLRLLYECAP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15237685 345 LAFLVEQAGGKSSDGKRGILSIQPVKLHQRLPLFLGSLEDVAELESY 391
Cdd:pfam18913 77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAY 123
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02628 |
PLN02628 |
fructose-1,6-bisphosphatase family protein |
49-404 |
0e+00 |
|
fructose-1,6-bisphosphatase family protein
Pssm-ID: 215337 [Multi-domain] Cd Length: 351 Bit Score: 693.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 49 STSFKPLavgrNLTGDDDDGYCTLIDFAGSgggEGKNVGEDLVVLLYHLQHACKRIASLVASPFNSSLGKLS--VNSSSG 126
Cdd:PLN02628 1 MASAPPL----YTAARGAEGVCTLMEFLGT---EGSNVGDDLVVLMAHIQAACKRIAALLASPFNSELGKTSsgASGASG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 127 SDRDAPKPLDIVSNDIVLSSLRNSGKVAVMASEENDSPTWIKDDGPYVVVVDPLDGSRNIDASIPTGTIFGIYNRLVELD 206
Cdd:PLN02628 74 SGRDAPKPLDIVSNEIILSSLRNSGKVAVMASEEDDAPIWIGDDGPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 207 HLPVEEKAELNSLQRGSRLVASGYVLYSSATIFCVTLGSGTHAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWP 286
Cdd:PLN02628 154 HLPVEEKAQLNVLQRGSRLVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 287 EGLRKYIDTVRQGKGQNPKKYSARYICSLVADLHRTLLYGGVAMNPRDHLRLVYEGNPLAFLVEQAGGKSSDGKRGILSI 366
Cdd:PLN02628 234 EGLRKYIDTVRQGKGQYPKKYSARYICSLVADLHRTILYGGIAMNPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSI 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 15237685 367 QPVKLHQRLPLFLGSLEDVAELESYGDVQQTVNPGYEV 404
Cdd:PLN02628 314 QPVKLHQRLPLFLGSSEDVLELESYGDVQQKVNPGYEV 351
|
|
| FBPase |
cd00354 |
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ... |
72-391 |
2.89e-147 |
|
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: 420.04 E-value: 2.89e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 72 LIDFAGSGGGEGknvgeDLVVLLYHLQHACKRIASLVASPFNSslGKLSVNSSSGSDRDAPKPLDIVSNDIVLSSLRNSG 151
Cdd:cd00354 1 LLEQLRKGAATG-----DLTDLLSSLALACKEISRAVRRAGLA--GLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 152 KVAVMASEENDSPTWIKD--DGPYVVVVDPLDGSRNIDASIPTGTIFGIYNRLVELDHlpveekAELNSLQRGSRLVASG 229
Cdd:cd00354 74 VVAVLASEEEEEPVPVEEskDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADA------TEKDFLQPGRNQVAAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 230 YVLYSSATIFCVTLGSGTHAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWPEGLRKYIDTVRQGKGQNpKKYSA 309
Cdd:cd00354 148 YALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGG-KPYNL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 310 RYICSLVADLHRTLLYGGVAMNPRD------HLRLVYEGNPLAFLVEQAGGKSSDGKRGILSIQPVKLHQRLPLFLGSLE 383
Cdd:cd00354 227 RYIGSMVADVHRILVRGGIFLYPADkkspkgKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKE 306
|
....*...
gi 15237685 384 DVAELESY 391
Cdd:cd00354 307 EVERVEEY 314
|
|
| Fbp |
COG0158 |
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ... |
71-391 |
1.12e-129 |
|
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: 376.38 E-value: 1.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 71 TLIDFAGSGGGEGKNVGEDLVVLLYHLQHACKRIASLVAS-PFNSSLGKL-SVNSssgsDRDAPKPLDIVSNDIVLSSLR 148
Cdd:COG0158 6 TLTQFLIEQQRRFPGATGELSALLNAIALAAKIISREVNKgGLAGILGAAgSENV----QGETQKKLDVIANEIFIEALE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 149 NSGKVAVMASEENDSPTWIKD---DGPYVVVVDPLDGSRNIDASIPTGTIFGIYNRLVELDHLPVEEkaelnSLQRGSRL 225
Cdd:COG0158 82 WGGHVAAMASEEMDDPIPIPEqypRGKYLVLFDPLDGSSNIDVNVSVGTIFSILRRPSGGGPVTEED-----FLQPGSEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 226 VASGYVLYSSATIFCVTLGSGTHAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWPEGLRKYIDTVRQGK-GQNP 304
Cdd:COG0158 157 VAAGYVLYGPSTMLVLTTGNGVHGFTLDPSIGEFLLTHPNMRIPEDTKEYAINESNYRHWEPPVRRYIDECLAGKeGPRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 305 KKYSARYICSLVADLHRTLLYGGVAMNPRDH--------LRLVYEGNPLAFLVEQAGGKSSDGKRGILSIQPVKLHQRLP 376
Cdd:COG0158 237 RDFNMRWIGSLVADVHRILLRGGIFLYPADSrdgyppgkLRLLYEANPMAFLVEQAGGAATDGRQRILDIVPTSLHQRVP 316
|
330
....*....|....*
gi 15237685 377 LFLGSLEDVAELESY 391
Cdd:COG0158 317 LILGSKEEVERVERY 331
|
|
| PRK09293 |
PRK09293 |
class 1 fructose-bisphosphatase; |
89-391 |
6.36e-113 |
|
class 1 fructose-bisphosphatase;
Pssm-ID: 236458 [Multi-domain] Cd Length: 327 Bit Score: 333.36 E-value: 6.36e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 89 DLVVLLYHLQHACKRIASLVASP-FNSSLGKLSVNSSSGsdrDAPKPLDIVSNDIVLSSLRNSGKVAVMASEENDSPTWI 167
Cdd:PRK09293 22 ELTALISAIALAAKIISRAINKGgLADILGAAGTENVQG---ETQKKLDVFANEILIEALKARGHVAGLASEEEDEIVPI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 168 -KDDGPYVVVVDPLDGSRNIDASIPTGTIFGIYNRlveldhlPVEEKAELNSLQRGSRLVASGYVLYSSATIFCVTLGSG 246
Cdd:PRK09293 99 pENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRA-------PVGTPTEEDFLQPGNNQVAAGYVLYGPSTMLVLTTGDG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 247 THAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWPEGLRKYIDTVRQGKGQNPKKYSARYICSLVADLHRTLLYG 326
Cdd:PRK09293 172 VHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIELLAGKDGPRGRPYNMRYIGSMVADVHRILLKG 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15237685 327 GVAMNPRDH------LRLVYEGNPLAFLVEQAGGKSSDGKRGILSIQPVKLHQRLPLFLGSLEDVAELESY 391
Cdd:PRK09293 252 GIFLYPADEpypngkLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERVEEY 322
|
|
| PLN02542 |
PLN02542 |
fructose-1,6-bisphosphatase |
89-391 |
1.54e-98 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215298 [Multi-domain] Cd Length: 412 Bit Score: 299.87 E-value: 1.54e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 89 DLVVLLYHLQHACKRIASLVASPFNSSL-GKLSVNSSSGSDRdapKPLDIVSNDIVLSSLRNSGKVAVMASEENDSPTWI 167
Cdd:PLN02542 95 ELTIVLSSISMACKQIASLVQRAGISNLtGVQGAVNIQGEDQ---KKLDVISNEVFSNCLRSSGRTGIIASEEEDVPVAV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 168 KDD--GPYVVVVDPLDGSRNIDASIPTGTIFGIYNR----LVELDHLP----VEEKAELNSLQRGSRLVASGYVLYSSAT 237
Cdd:PLN02542 172 EESysGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPndecLADIGDDStldsVEQRCIVNVCQPGSNLLAAGYCMYSSSV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 238 IFCVTLGSGTHAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWPEGLRKYIDTVRQgKGQNPKKYSARYICSLVA 317
Cdd:PLN02542 252 IFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKD-PGPSGKPYSARYIGSLVG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 318 DLHRTLLYGGVAMNPRDH------LRLVYEGNPLAFLVEQAGGKSSDGKRGILSIQPVKLHQRLPLFLGSLEDVAELESY 391
Cdd:PLN02542 331 DFHRTLLYGGIYGYPRDKkskngkLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRVPLYIGSVEEVEKLEKY 410
|
|
| PLN02262 |
PLN02262 |
fructose-1,6-bisphosphatase |
89-390 |
6.17e-96 |
|
fructose-1,6-bisphosphatase
Pssm-ID: 215147 [Multi-domain] Cd Length: 340 Bit Score: 290.55 E-value: 6.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 89 DLVVLLYHLQHACKRIASLVAspfNSSLGKLS-VNSSSGSDRDAPKPLDIVSNDIVLSSLRNSGKVAVMASEENDSPTWI 167
Cdd:PLN02262 32 DLTILLSHIVLGCKFVCSAVN---KAGLAKLIgLAGETNVQGEEQKKLDVLSNDVFIKALVSSGRTNVLVSEEDEEAIFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 168 KDD--GPYVVVVDPLDGSRNIDASIPTGTIFGIYnrLVELDHLPVEEkaelNSLQRGSRLVASGYVLYSSATIFCVTLGS 245
Cdd:PLN02262 109 EPSkrGRYCVVFDPLDGSSNIDCGVSIGTIFGIY--MLKDGGEGTVE----DVLQPGKEMVAAGYCMYGSSCTLVLSTGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 246 GTHAFTLDHSTGEFVLTHQNIKIPTRGQIYSVNDARYFDWPEGLRKYIDTVRQGKGQNPKKySARYICSLVADLHRTLLY 325
Cdd:PLN02262 183 GVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPK-SLRYIGSMVADVHRTLLY 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15237685 326 GGVAMNPRDH------LRLVYEGNPLAFLVEQAGGKSSDGKRGILSIQPVKLHQRLPLFLGSLEDVAELES 390
Cdd:PLN02262 262 GGIFLYPADKkspngkLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEEIKA 332
|
|
| FBPase_C |
pfam18913 |
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ... |
271-391 |
7.51e-49 |
|
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: 161.63 E-value: 7.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 271 RGQIYSVNDARYFDWPEGLRKYIDTVRQGKGqnpkkYSARYICSLVADLHRTLLYGGVAMNPRDH------LRLVYEGNP 344
Cdd:pfam18913 2 EGKIYAINEGNARFWNAPYRAYIDDLVSGKG-----YTLRYIGSMVADVHRILLKGGIFLYPADRrspygkLRLLYECAP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15237685 345 LAFLVEQAGGKSSDGKRGILSIQPVKLHQRLPLFLGSLEDVAELESY 391
Cdd:pfam18913 77 LAFLIEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAY 123
|
|
| FBPase |
pfam00316 |
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ... |
71-264 |
8.60e-40 |
|
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: 140.29 E-value: 8.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 71 TLIDFAGSGGGEGKNVGEDLVVLLYHLQHACKRIASLV--ASPFNSSLGKLSVNSSSgsdrDAPKPLDIVSNDIVLSSLR 148
Cdd:pfam00316 2 TLTRFIIEQQHEFPNATGELTTLLSAIQLAAKFISRDIrkAGLVNLLGLAGAENVQG----DQQKKLDVLADELLKNALK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 149 NSGKVAVMASEENDSPTWIK--DDGPYVVVVDPLDGSRNIDASIPTGTIFGIYNRlvelDHLPVEEKAELNSLQRGSRLV 226
Cdd:pfam00316 78 ASGIVKVLVSEEEEELIVFEppKRGKYVVCFDPLDGSSNIDVNVSVGTIFSIYRR----VSPTDSPTTIEDVLQPGNEQV 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 15237685 227 ASGYVLYSSATIFCVTLGSGTHAFTLDHSTGEFVLTHQ 264
Cdd:pfam00316 154 AAGYAMYGSSTMLVLTTGCGVHGFTLDPSLGEFILTHE 191
|
|
| PLN02462 |
PLN02462 |
sedoheptulose-1,7-bisphosphatase |
88-391 |
1.35e-30 |
|
sedoheptulose-1,7-bisphosphatase
Pssm-ID: 215256 [Multi-domain] Cd Length: 304 Bit Score: 119.06 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 88 EDLVVLLYHLQHACKRIASLVASPfnSSLGKLSVNSSSgsdrDAPKPLDIVSNDIVLSSLRNSGKVAVMASEEndSPTWI 167
Cdd:PLN02462 13 KKLRRLIMCMGEACRTIAFKVRTA--SCTGTACVNSFG----DEQLAVDMLADKLLFEALKYSHVCKYACSEE--VPEVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 168 KDDGP----YVVVVDPLDGSRNIDASIPTGTIFGIY--NRLVELDhlpveekaelnslqrGSRLVASGYVLYSSATIFCV 241
Cdd:PLN02462 85 DMGGPveggFSVAFDPLDGSSIVDTNFAVGTIFGVWpgDKLTGVT---------------GRDQVAAAMGIYGPRTTYVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 242 TL--GSGTHAFTLdHSTGEFVLTHQNIKIpTRGQIYSVNDARY-FDWPeGLRKYIDTVRQgkgqnpKKYSARYICSLVAD 318
Cdd:PLN02462 150 ALkdGPGTHEFLL-LDDGKWQHVKETTEI-GEGKIFSPGNLRAtFDNP-GYEKLINYYVS------EKYTLRYTGGMVPD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 319 LHRTLLY-GGVAMNP-----RDHLRLVYEGNPLAFLVEQAGGKSSDGKRG--ILSIQPVKLHQRLPLFLGSLEDVAELES 390
Cdd:PLN02462 221 VYQIIVKeKGVFTNVtspksKAKLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEVIRFEE 300
|
.
gi 15237685 391 Y 391
Cdd:PLN02462 301 T 301
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
97-225 |
2.20e-10 |
|
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: 59.33 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 97 LQHACK--RIASLVASPFNSSLGKLSVNSSSgSDRDAPKPLDIVSNDIVLSSLRNSGKVAVMASEEnDSPTWIKD--DGP 172
Cdd:cd01636 1 LEELCRvaKEAGLAILKAFGRELSGKVKITK-SDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEE-SGVAEEVMgrRDE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15237685 173 YVVVVDPLDGSRNIDASIP-TGTIFGIYN--RLVELDHLPVEEKAELNSLQRGSRL 225
Cdd:cd01636 79 YTWVIDPIDGTKNFINGLPfVAVVIAVYVilILAEPSHKRVDEKKAELQLLAVYRI 134
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
100-198 |
7.02e-08 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 53.37 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 100 ACKRIASLVASPFNSSLG--KLSVNSSSGSDRDAPKPLDIVSNDIVLSSLRNSGKVAVMASEENDSptwIKDDGP-YVVV 176
Cdd:PRK12676 9 ICDDMAKEVEKAIMPLFGtpDAGETVGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGE---IVGNGPeYTVV 85
|
90 100
....*....|....*....|..
gi 15237685 177 VDPLDGSRNIDASIPtgtIFGI 198
Cdd:PRK12676 86 LDPLDGTYNAINGIP---FYAI 104
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
99-191 |
5.13e-07 |
|
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: 50.52 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 99 HACKRIASLVASPFNSSLGKLSVNSSSGSDRDAPKPLDIVSNDIVLSSLRNSGKVAVMASEEndSPTWIKDDGPYVVVVD 178
Cdd:cd01642 3 EVLEKITKEIILLLNEKNRQGLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEE--SGEIRKGSGEYIAVLD 80
|
90
....*....|...
gi 15237685 179 PLDGSRNIDASIP 191
Cdd:cd01642 81 PLDGSTNYLSGIP 93
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
102-191 |
3.30e-06 |
|
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: 48.14 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 102 KRIASLVASPFNSSLGKLsvnsssGSDRDAPKPLDIVSNDIVLSSLRNSGKVAVMaSEE------NDSPTWIkddgpyvV 175
Cdd:cd01515 14 KAIKPLFGTEDASEVVKI------GADGTPTKLIDKVAEDAAIEILKKLGSVNIV-SEEigvidnGDEPEYT-------V 79
|
90
....*....|....*.
gi 15237685 176 VVDPLDGSRNIDASIP 191
Cdd:cd01515 80 VLDPLDGTYNAINGIP 95
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
126-191 |
1.51e-04 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 43.95 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237685 126 GSDRDAPKPLDIVSNDIVLSSLRNSGKvAVMASEENDSPTWIKDDGPYVVVVDPLDGSRNIDASIP 191
Cdd:PRK14076 36 GADGTPTKRIDLIAENIAINSLEKFCS-GILISEEIGFKKIGKNKPEYIFVLDPIDGTYNALKDIP 100
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
122-201 |
4.28e-04 |
|
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: 41.53 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237685 122 NSSSGSDRDAPKPLDIVSNDIVLSSLRNSG-KVAVMAsEEnDSPTWIKDDGPYVVVVDPLDGSRNIDASIPT-GTIFGIY 199
Cdd:cd01637 25 VETKKGDGDLVTEADLAAEELIVDVLKALFpDDGILG-EE-GGGSGNVSDGGRVWVIDPIDGTTNFVAGLPNfAVSIALY 102
|
..
gi 15237685 200 NR 201
Cdd:cd01637 103 ED 104
|
|
| |
