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Conserved domains on  [gi|32307558|gb|AAP79184|]
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sedoheptulose-1,7 bisphosphatase, partial [Bigelowiella natans]

Protein Classification

FIG domain-containing protein( domain architecture ID 299)

FIG (FBPase/IMPase/glpX-like) domain-containing protein belongs to a superfamily of metal-dependent phosphatases with various substrates; such as fructose-1,6-bisphosphatase (both the major and the glpX-encoded variant), inositol-monophosphatases and inositol polyphosphatases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FIG super family cl00289
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
109-409 9.84e-143

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+.


The actual alignment was detected with superfamily member PLN02462:

Pssm-ID: 469707 [Multi-domain]  Cd Length: 304  Bit Score: 408.73  E-value: 9.84e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  109 TIEEFL--ANTEPKLQKAIMGMFSACKEIGYKIRTASCDKQACFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEE 186
Cdd:PLN02462   1 SLEEFLakATPDKKLRRLIMCMGEACRTIAFKVRTASCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  187 PTEVPLGGE---GYSVAFDPLDGSSIIDTNFAVGTIFGnLGLDPRLTGIKGTEQKAAGLGVYGPRTTITLAVDGIQGAHE 263
Cdd:PLN02462  81 PEVQDMGGPvegGFSVAFDPLDGSSIVDTNFAVGTIFG-VWPGDKLTGVTGRDQVAAAMGIYGPRTTYVVALKDGPGTHE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  264 FLLIDDysakhGQWVLSQSFMSIGESKLFAPGNLRATKDNKGYEELFNYWYDNQYQLRYTGGMVPDVNQIMVKGKGVFVN 343
Cdd:PLN02462 160 FLLLDD-----GKWQHVKETTEIGEGKIFSPGNLRATFDNPGYEKLINYYVSEKYTLRYTGGMVPDVYQIIVKEKGVFTN 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32307558  344 AESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQ--SVLNIEVVGTEDRTQVAYGSAAEVDRFEQMV 409
Cdd:PLN02462 235 VTSPKSKAKLRLLFEVAPLGLLVEKAGGKSSDGVQggSVLDKQINNLDQRTQVAYGSKNEVIRFEETL 302
 
Name Accession Description Interval E-value
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
109-409 9.84e-143

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256 [Multi-domain]  Cd Length: 304  Bit Score: 408.73  E-value: 9.84e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  109 TIEEFL--ANTEPKLQKAIMGMFSACKEIGYKIRTASCDKQACFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEE 186
Cdd:PLN02462   1 SLEEFLakATPDKKLRRLIMCMGEACRTIAFKVRTASCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  187 PTEVPLGGE---GYSVAFDPLDGSSIIDTNFAVGTIFGnLGLDPRLTGIKGTEQKAAGLGVYGPRTTITLAVDGIQGAHE 263
Cdd:PLN02462  81 PEVQDMGGPvegGFSVAFDPLDGSSIVDTNFAVGTIFG-VWPGDKLTGVTGRDQVAAAMGIYGPRTTYVVALKDGPGTHE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  264 FLLIDDysakhGQWVLSQSFMSIGESKLFAPGNLRATKDNKGYEELFNYWYDNQYQLRYTGGMVPDVNQIMVKGKGVFVN 343
Cdd:PLN02462 160 FLLLDD-----GKWQHVKETTEIGEGKIFSPGNLRATFDNPGYEKLINYYVSEKYTLRYTGGMVPDVYQIIVKEKGVFTN 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32307558  344 AESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQ--SVLNIEVVGTEDRTQVAYGSAAEVDRFEQMV 409
Cdd:PLN02462 235 VTSPKSKAKLRLLFEVAPLGLLVEKAGGKSSDGVQggSVLDKQINNLDQRTQVAYGSKNEVIRFEETL 302
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
111-408 1.69e-111

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: 329.51  E-value: 1.69e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 111 EEFLANTEPKLQKAIMGMFSACKEIGYKIRTA----SCDKQACFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEE 186
Cdd:cd00354   4 QLRKGAATGDLTDLLSSLALACKEISRAVRRAglagLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASEEE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 187 PTEVPLG---GEGYSVAFDPLDGSSIIDTNFAVGTIFGNLGLDPRLTG------IKGTEQKAAGLGVYGPRTTITLAVDg 257
Cdd:cd00354  84 EEPVPVEeskDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADAtekdflQPGRNQVAAGYALYGPSTMLVLTLG- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 258 iQGAHEFLLIDDysakHGQWVLSQSFMSI-GESKLFAP--GNLRATkDNKGYEELFNYWYDN----QYQLRYTGGMVPDV 330
Cdd:cd00354 163 -QGVHGFTLDPS----LGEFILTHPNVKIpKKGKIYSIneGNYRYW-DEPVKKYIDDCKAGEdggkPYNLRYIGSMVADV 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32307558 331 NQIMVKGkGVFVN-AESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQSVLNIEVVGTEDRTQVAYGSAAEVDRFEQM 408
Cdd:cd00354 237 HRILVRG-GIFLYpADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEY 314
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
106-408 8.19e-54

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: 181.85  E-value: 8.19e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 106 QSTTIEEFLANTEPKLQKA-------IMGMFSACKEIGYKIRtascdkQACF----------NAFGDEQLAIDVLADNVI 168
Cdd:COG0158   3 KGTTLTQFLIEQQRRFPGAtgelsalLNAIALAAKIISREVN------KGGLagilgaagseNVQGETQKKLDVIANEIF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 169 FENLRASGAVATASSEEEPTEVPLGGEG----YSVAFDPLDGSSIIDTNFAVGTIFGNLgldPRLTGI----------KG 234
Cdd:COG0158  77 IEALEWGGHVAAMASEEMDDPIPIPEQYprgkYLVLFDPLDGSSNIDVNVSVGTIFSIL---RRPSGGgpvteedflqPG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 235 TEQKAAGLGVYGPRTTITLAVdGiQGAHEFLLidDYSakHGQWVLSQSFMSIGES-KLFA--PGNLR----ATKD----- 302
Cdd:COG0158 154 SEQVAAGYVLYGPSTMLVLTT-G-NGVHGFTL--DPS--IGEFLLTHPNMRIPEDtKEYAinESNYRhwepPVRRyidec 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 303 NKGYEELFNywydNQYQLRYTGGMVPDVNQIMVKGkGVFV---NAESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQS 379
Cdd:COG0158 228 LAGKEGPRG----RDFNMRWIGSLVADVHRILLRG-GIFLypaDSRDGYPPGKLRLLYEANPMAFLVEQAGGAATDGRQR 302
                       330       340
                ....*....|....*....|....*....
gi 32307558 380 VLNIEVVGTEDRTQVAYGSAAEVDRFEQM 408
Cdd:COG0158 303 ILDIVPTSLHQRVPLILGSKEEVERVERY 331
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
288-408 1.02e-44

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: 151.23  E-value: 1.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558   288 ESKLFAPGNLRATKDNKGYEELFNYWYDNQ-YQLRYTGGMVPDVNQIMVKGkGVFVNAESKAAK-AKLRLLYEVAPIGYV 365
Cdd:pfam18913   2 EGKIYAINEGNARFWNAPYRAYIDDLVSGKgYTLRYIGSMVADVHRILLKG-GIFLYPADRRSPyGKLRLLYECAPLAFL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 32307558   366 IEKAGGKSSDGEQSVLNIEVVGTEDRTQVAYGSAAEVDRFEQM 408
Cdd:pfam18913  81 IEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAY 123
 
Name Accession Description Interval E-value
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
109-409 9.84e-143

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256 [Multi-domain]  Cd Length: 304  Bit Score: 408.73  E-value: 9.84e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  109 TIEEFL--ANTEPKLQKAIMGMFSACKEIGYKIRTASCDKQACFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEE 186
Cdd:PLN02462   1 SLEEFLakATPDKKLRRLIMCMGEACRTIAFKVRTASCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  187 PTEVPLGGE---GYSVAFDPLDGSSIIDTNFAVGTIFGnLGLDPRLTGIKGTEQKAAGLGVYGPRTTITLAVDGIQGAHE 263
Cdd:PLN02462  81 PEVQDMGGPvegGFSVAFDPLDGSSIVDTNFAVGTIFG-VWPGDKLTGVTGRDQVAAAMGIYGPRTTYVVALKDGPGTHE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  264 FLLIDDysakhGQWVLSQSFMSIGESKLFAPGNLRATKDNKGYEELFNYWYDNQYQLRYTGGMVPDVNQIMVKGKGVFVN 343
Cdd:PLN02462 160 FLLLDD-----GKWQHVKETTEIGEGKIFSPGNLRATFDNPGYEKLINYYVSEKYTLRYTGGMVPDVYQIIVKEKGVFTN 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32307558  344 AESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQ--SVLNIEVVGTEDRTQVAYGSAAEVDRFEQMV 409
Cdd:PLN02462 235 VTSPKSKAKLRLLFEVAPLGLLVEKAGGKSSDGVQggSVLDKQINNLDQRTQVAYGSKNEVIRFEETL 302
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
111-408 1.69e-111

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: 329.51  E-value: 1.69e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 111 EEFLANTEPKLQKAIMGMFSACKEIGYKIRTA----SCDKQACFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEE 186
Cdd:cd00354   4 QLRKGAATGDLTDLLSSLALACKEISRAVRRAglagLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASEEE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 187 PTEVPLG---GEGYSVAFDPLDGSSIIDTNFAVGTIFGNLGLDPRLTG------IKGTEQKAAGLGVYGPRTTITLAVDg 257
Cdd:cd00354  84 EEPVPVEeskDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADAtekdflQPGRNQVAAGYALYGPSTMLVLTLG- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 258 iQGAHEFLLIDDysakHGQWVLSQSFMSI-GESKLFAP--GNLRATkDNKGYEELFNYWYDN----QYQLRYTGGMVPDV 330
Cdd:cd00354 163 -QGVHGFTLDPS----LGEFILTHPNVKIpKKGKIYSIneGNYRYW-DEPVKKYIDDCKAGEdggkPYNLRYIGSMVADV 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32307558 331 NQIMVKGkGVFVN-AESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQSVLNIEVVGTEDRTQVAYGSAAEVDRFEQM 408
Cdd:cd00354 237 HRILVRG-GIFLYpADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEY 314
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
106-413 1.69e-76

class 1 fructose-bisphosphatase;


Pssm-ID: 236458 [Multi-domain]  Cd Length: 327  Bit Score: 240.52  E-value: 1.69e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  106 QSTTIEEFLAnTEPKLQKAIMGMFS--------ACKEIGYKIRTASCDKQACF----NAFGDEQLAIDVLADNVIFENLR 173
Cdd:PRK09293   1 SMKTLGEFLV-EQQREFPHATGELTalisaialAAKIISRAINKGGLADILGAagteNVQGETQKKLDVFANEILIEALK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  174 ASGAVATASSEEEPTEVPLGGE--GYSVAFDPLDGSSIIDTNFAVGTIFG-------NLGLDPRLTgiKGTEQKAAGLGV 244
Cdd:PRK09293  80 ARGHVAGLASEEEDEIVPIPENegKYLVAYDPLDGSSNIDVNVSVGTIFSiyrapvgTPTEEDFLQ--PGNNQVAAGYVL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  245 YGPRTTITLAVDgiQGAHEFLLIDDysakHGQWVLSQSFM---------SIGES--KLFAPGNLRATKDNKGYEELFNyw 313
Cdd:PRK09293 158 YGPSTMLVLTTG--DGVHGFTLDPS----LGEFVLTHENIripedgkeyAINEGnqRHWEPGVKKYIELLAGKDGPRG-- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  314 ydNQYQLRYTGGMVPDVNQIMVKGkGVFV-NAESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQSVLNIEVVGTEDRT 392
Cdd:PRK09293 230 --RPYNMRYIGSMVADVHRILLKG-GIFLyPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRV 306
                        330       340
                 ....*....|....*....|.
gi 32307558  393 QVAYGSAAEVDRFEQMVGKKY 413
Cdd:PRK09293 307 PLFLGSKEEVERVEEYHAEAP 327
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism]; Fructose-1, ...
106-408 8.19e-54

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: 181.85  E-value: 8.19e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 106 QSTTIEEFLANTEPKLQKA-------IMGMFSACKEIGYKIRtascdkQACF----------NAFGDEQLAIDVLADNVI 168
Cdd:COG0158   3 KGTTLTQFLIEQQRRFPGAtgelsalLNAIALAAKIISREVN------KGGLagilgaagseNVQGETQKKLDVIANEIF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 169 FENLRASGAVATASSEEEPTEVPLGGEG----YSVAFDPLDGSSIIDTNFAVGTIFGNLgldPRLTGI----------KG 234
Cdd:COG0158  77 IEALEWGGHVAAMASEEMDDPIPIPEQYprgkYLVLFDPLDGSSNIDVNVSVGTIFSIL---RRPSGGgpvteedflqPG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 235 TEQKAAGLGVYGPRTTITLAVdGiQGAHEFLLidDYSakHGQWVLSQSFMSIGES-KLFA--PGNLR----ATKD----- 302
Cdd:COG0158 154 SEQVAAGYVLYGPSTMLVLTT-G-NGVHGFTL--DPS--IGEFLLTHPNMRIPEDtKEYAinESNYRhwepPVRRyidec 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 303 NKGYEELFNywydNQYQLRYTGGMVPDVNQIMVKGkGVFV---NAESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQS 379
Cdd:COG0158 228 LAGKEGPRG----RDFNMRWIGSLVADVHRILLRG-GIFLypaDSRDGYPPGKLRLLYEANPMAFLVEQAGGAATDGRQR 302
                       330       340
                ....*....|....*....|....*....
gi 32307558 380 VLNIEVVGTEDRTQVAYGSAAEVDRFEQM 408
Cdd:COG0158 303 ILDIVPTSLHQRVPLILGSKEEVERVERY 331
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
288-408 1.02e-44

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: 151.23  E-value: 1.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558   288 ESKLFAPGNLRATKDNKGYEELFNYWYDNQ-YQLRYTGGMVPDVNQIMVKGkGVFVNAESKAAK-AKLRLLYEVAPIGYV 365
Cdd:pfam18913   2 EGKIYAINEGNARFWNAPYRAYIDDLVSGKgYTLRYIGSMVADVHRILLKG-GIFLYPADRRSPyGKLRLLYECAPLAFL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 32307558   366 IEKAGGKSSDGEQSVLNIEVVGTEDRTQVAYGSAAEVDRFEQM 408
Cdd:pfam18913  81 IEQAGGKASDGTQRILDIVPDSLHQRTPIFLGSRDEVARVEAY 123
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
125-281 3.45e-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: 141.83  E-value: 3.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558   125 IMGMFSACKEIGYKIRTAS----CDKQACFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEEPTEVPLGGE---GY 197
Cdd:pfam00316  25 LSAIQLAAKFISRDIRKAGlvnlLGLAGAENVQGDQQKKLDVLADELLKNALKASGIVKVLVSEEEEELIVFEPPkrgKY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558   198 SVAFDPLDGSSIIDTNFAVGTIFG---NLGLDPRLTGIK-----GTEQKAAGLGVYGPRTTITLAVDGiqGAHEFLLIDD 269
Cdd:pfam00316 105 VVCFDPLDGSSNIDVNVSVGTIFSiyrRVSPTDSPTTIEdvlqpGNEQVAAGYAMYGSSTMLVLTTGC--GVHGFTLDPS 182
                         170
                  ....*....|..
gi 32307558   270 YsakhGQWVLSQ 281
Cdd:pfam00316 183 L----GEFILTH 190
PLN02262 PLN02262
fructose-1,6-bisphosphatase
151-408 2.97e-35

fructose-1,6-bisphosphatase


Pssm-ID: 215147 [Multi-domain]  Cd Length: 340  Bit Score: 133.01  E-value: 2.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  151 NAFGDEQLAIDVLADNVIFENLRASGAVATASSEE--EPTEVPLGGEG-YSVAFDPLDGSSIIDTNFAVGTIFG----NL 223
Cdd:PLN02262  67 NVQGEEQKKLDVLSNDVFIKALVSSGRTNVLVSEEdeEAIFVEPSKRGrYCVVFDPLDGSSNIDCGVSIGTIFGiymlKD 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  224 GLDPRLTGI--KGTEQKAAGLGVYGPRTTITLAVDGiqGAHEFLLidDYSAkhGQWVLSQSFMSIGES-KLFA--PGNLR 298
Cdd:PLN02262 147 GGEGTVEDVlqPGKEMVAAGYCMYGSSCTLVLSTGG--GVNGFTL--DPSL--GEFILTHPDIKIPKKgKIYSvnEGNAK 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  299 ATKD-NKGYEELFNYWYDNQ--YQLRYTGGMVPDVNQIMVKGkGVFV-NAESKAAKAKLRLLYEVAPIGYVIEKAGGKSS 374
Cdd:PLN02262 221 NWDGpTAKYVEKCKFPKDGSspKSLRYIGSMVADVHRTLLYG-GIFLyPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAF 299
                        250       260       270
                 ....*....|....*....|....*....|....
gi 32307558  375 DGEQSVLNIEVVGTEDRTQVAYGSAAEVDRFEQM 408
Cdd:PLN02262 300 TGKQRALDLVPTKIHERSPIFLGSYDDVEEIKAL 333
PLN02542 PLN02542
fructose-1,6-bisphosphatase
131-407 1.19e-31

fructose-1,6-bisphosphatase


Pssm-ID: 215298 [Multi-domain]  Cd Length: 412  Bit Score: 124.60  E-value: 1.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  131 ACKEIGYKIRTASCDK----QACFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEEPTEVPLGgEGYS----VAFD 202
Cdd:PLN02542 106 ACKQIASLVQRAGISNltgvQGAVNIQGEDQKKLDVISNEVFSNCLRSSGRTGIIASEEEDVPVAVE-ESYSgnyiVVFD 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  203 PLDGSSIIDTNFAVGTIFG----------NLGLDPRLTGIK----------GTEQKAAGLGVYGPRTTITLAVDgiQGAH 262
Cdd:PLN02542 185 PLDGSSNIDAAVSTGSIFGiyspndeclaDIGDDSTLDSVEqrcivnvcqpGSNLLAAGYCMYSSSVIFVLTIG--TGVF 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  263 EFLLIDDYsakhGQWVLSQSFMSI---GESKLFAPGNLRATKDNkgyeeLFNYWYD--------NQYQLRYTGGMVPDVN 331
Cdd:PLN02542 263 SFTLDPMY----GEFVLTQENIQIpkaGKIYSFNEGNYQLWDDK-----LKKYIDDlkdpgpsgKPYSARYIGSLVGDFH 333
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32307558  332 QIMVKGKGVFVNAESKAAKAKLRLLYEVAPIGYVIEKAGGKSSDGEQSVLNIEVVGTEDRTQVAYGSAAEVDRFEQ 407
Cdd:PLN02542 334 RTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRVPLYIGSVEEVEKLEK 409
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
100-406 2.55e-30

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337 [Multi-domain]  Cd Length: 351  Bit Score: 119.52  E-value: 2.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  100 SSVATEQSTTIEEFL----ANTEPKLQKAIMGMFSACKEIGYKIRTASCDKQACFNAFG--------DEQLAIDVLADNV 167
Cdd:PLN02628  10 AARGAEGVCTLMEFLgtegSNVGDDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGAsgasgsgrDAPKPLDIVSNEI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  168 IFENLRASGAVATASSEEEPTEVPLGGEG-YSVAFDPLDGSSIIDTNFAVGTIFG---------NLGLDPRLTG---IKG 234
Cdd:PLN02628  90 ILSSLRNSGKVAVMASEEDDAPIWIGDDGpYVVVFDPLDGSRNIDASIPTGTIFGiynrlveadHLPVEEKAQLnvlQRG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  235 TEQKAAGLGVYGPRTTITLAVDgiQGAHEFLLidDYSAkhGQWVLSQ---------SFMSIGESKLFA-PGNLRATKDN- 303
Cdd:PLN02628 170 SRLVAAGYVLYSSATILCISFG--SGTHGFTL--DHST--GEFVLTHpdikipergQIYSVNDARYFDwPEGLRKYIDTv 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  304 ---KGYeelfnywYDNQYQLRYTGGMVPDVNQIMVKGkGVFVNAESKaakakLRLLYEVAPIGYVIEKAGGKSSDGEQSV 380
Cdd:PLN02628 244 rqgKGQ-------YPKKYSARYICSLVADLHRTILYG-GIAMNPRSH-----LRLVYEANPLSFLVEQAGGRGSDGKRRI 310
                        330       340
                 ....*....|....*....|....*.
gi 32307558  381 LNIEVVGTEDRTQVAYGSAAEVDRFE 406
Cdd:PLN02628 311 LSIQPVKLHQRLPLFLGSSEDVLELE 336
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
125-220 3.28e-07

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 51.45  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558  125 IMGMFSACKEIGYKIRTASCD----KQA----CFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEEpTEVPLGGEG 196
Cdd:PRK12676   3 IMEWLEICDDMAKEVEKAIMPlfgtPDAgetvGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEEL-GEIVGNGPE 81
                         90       100
                 ....*....|....*....|....
gi 32307558  197 YSVAFDPLDGSSiidtNFAVGTIF 220
Cdd:PRK12676  82 YTVVLDPLDGTY----NAINGIPF 101
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
154-221 1.60e-05

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: 45.08  E-value: 1.60e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32307558 154 GDEQLAIDVLADNVIFENLRASGAVATASSEEEP--TEVPLGGEGYSVAFDPLDGSSIIDTNFA-VGTIFG 221
Cdd:cd01636  34 NDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGvaEEVMGRRDEYTWVIDPIDGTKNFINGLPfVAVVIA 104
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
128-220 2.44e-05

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: 45.45  E-value: 2.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32307558 128 MFSACKEIGYKIRTASCD--------KQACFNAFGDEQLAIDVLADNVIFENLRASGAVATASseEEPTEVPLGGE-GYS 198
Cdd:cd01515   1 WLEIARNIAKEIEKAIKPlfgtedasEVVKIGADGTPTKLIDKVAEDAAIEILKKLGSVNIVS--EEIGVIDNGDEpEYT 78
                        90       100
                ....*....|....*....|..
gi 32307558 199 VAFDPLDGSSiidtNFAVGTIF 220
Cdd:cd01515  79 VVLDPLDGTY----NAINGIPF 96
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
144-217 1.78e-03

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: 39.74  E-value: 1.78e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32307558 144 CDKQACFNAFGDEQLAIDVLADNVIFENLRASGAVATASSEEEPTEVPLGGEgYSVAFDPLDGSsiidTNFAVG 217
Cdd:cd01642  23 GLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGE-YIAVLDPLDGS----TNYLSG 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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