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Conserved domains on  [gi|578817185|ref|XP_006717068|]
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fructose-1,6-bisphosphatase 1 isoform X1 [Homo sapiens]

Protein Classification

fructose-1,6-bisphosphatase (domain architecture ID 10086071)

class 1 fructose-1,6-bisphosphatase I catalyzes the conversion of D-fructose 1,6-bisphosphate to D-fructose 6-phosphate in gluconeogenesis and the Calvin cycle, which are both anabolic pathways

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
2-250 1.13e-150

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  Cd Length: 315  Bit Score: 422.35  E-value: 1.13e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   2 NMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAA 81
Cdd:cd00354   67 EALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  82 GYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGA 161
Cdd:cd00354  147 GYALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNL 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 162 RYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPD 241
Cdd:cd00354  227 RYIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKE 306

                 ....*....
gi 578817185 242 DVLEFLKVY 250
Cdd:cd00354  307 EVERVEEYL 315
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
2-250 1.13e-150

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  Cd Length: 315  Bit Score: 422.35  E-value: 1.13e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   2 NMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAA 81
Cdd:cd00354   67 EALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  82 GYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGA 161
Cdd:cd00354  147 GYALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNL 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 162 RYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPD 241
Cdd:cd00354  227 RYIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKE 306

                 ....*....
gi 578817185 242 DVLEFLKVY 250
Cdd:cd00354  307 EVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
1-250 9.32e-128

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 365.67  E-value: 9.32e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   1 MNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVA 80
Cdd:PLN02262  85 IKALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVA 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  81 AGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYG 160
Cdd:PLN02262 165 AGYCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKS 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 161 ARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSP 240
Cdd:PLN02262 245 LRYIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSY 324
                        250
                 ....*....|
gi 578817185 241 DDVLEFLKVY 250
Cdd:PLN02262 325 DDVEEIKALY 334
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
4-253 8.65e-110

Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 223236  Cd Length: 326  Bit Score: 319.26  E-value: 8.65e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   4 LKSSFATCVLVSEEdKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDePSEKDALQPGRNLVAAGY 83
Cdd:COG0158   77 LKARGNVAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  84 ALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYI---QRKKfpPDNSAPYG 160
Cdd:COG0158  155 VVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIkdcFAED--KGTRRPYN 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 161 ARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSP 240
Cdd:COG0158  233 MRYIGSMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSK 312
                        250
                 ....*....|...
gi 578817185 241 DDVLEFLKVYEKH 253
Cdd:COG0158  313 EEVEKLERFIKEF 325
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
1-114 1.95e-69

Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this protein family.


Pssm-ID: 395249  Cd Length: 189  Bit Score: 211.88  E-value: 1.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185    1 MNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVA 80
Cdd:pfam00316  73 KNALKASGIVAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVA 152
                          90       100       110
                  ....*....|....*....|....*....|....
gi 578817185   81 AGYALYGSATMLVLAMDCGVNCFMLDPAIGEFIL 114
Cdd:pfam00316 153 AGYVVYGSSTMLVLTTGCGVHGFTLDPSLGEFIL 186
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
2-250 1.13e-150

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  Cd Length: 315  Bit Score: 422.35  E-value: 1.13e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   2 NMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAA 81
Cdd:cd00354   67 EALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  82 GYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGA 161
Cdd:cd00354  147 GYALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNL 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 162 RYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPD 241
Cdd:cd00354  227 RYIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKE 306

                 ....*....
gi 578817185 242 DVLEFLKVY 250
Cdd:cd00354  307 EVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
1-250 9.32e-128

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 365.67  E-value: 9.32e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   1 MNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVA 80
Cdd:PLN02262  85 IKALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVA 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  81 AGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYG 160
Cdd:PLN02262 165 AGYCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKS 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 161 ARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSP 240
Cdd:PLN02262 245 LRYIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSY 324
                        250
                 ....*....|
gi 578817185 241 DDVLEFLKVY 250
Cdd:PLN02262 325 DDVEEIKALY 334
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
4-253 3.51e-118

class 1 fructose-bisphosphatase;


Pssm-ID: 236458  Cd Length: 327  Bit Score: 340.67  E-value: 3.51e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   4 LKSSFATCVLVSEEDKHAIIVePEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKStDEPSEKDALQPGRNLVAAGY 83
Cdd:PRK09293  78 LKARGHVAGLASEEEDEIVPI-PENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGY 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  84 ALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYI---QRKKFPPDnsAPYG 160
Cdd:PRK09293 156 VLYGPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIellAGKDGPRG--RPYN 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 161 ARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSP 240
Cdd:PRK09293 234 MRYIGSMVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSK 313
                        250
                 ....*....|...
gi 578817185 241 DDVLEFLKVYEKH 253
Cdd:PRK09293 314 EEVERVEEYHAEA 326
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
4-253 8.65e-110

Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 223236  Cd Length: 326  Bit Score: 319.26  E-value: 8.65e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   4 LKSSFATCVLVSEEdKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDePSEKDALQPGRNLVAAGY 83
Cdd:COG0158   77 LKARGNVAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  84 ALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYI---QRKKfpPDNSAPYG 160
Cdd:COG0158  155 VVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIkdcFAED--KGTRRPYN 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 161 ARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSP 240
Cdd:COG0158  233 MRYIGSMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSK 312
                        250
                 ....*....|...
gi 578817185 241 DDVLEFLKVYEKH 253
Cdd:COG0158  313 EEVEKLERFIKEF 325
PLN02542 PLN02542
fructose-1,6-bisphosphatase
2-243 1.98e-78

fructose-1,6-bisphosphatase


Pssm-ID: 215298  Cd Length: 412  Bit Score: 242.47  E-value: 1.98e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   2 NMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYR-----------KKSTDEPSEK- 69
Cdd:PLN02542 149 NCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSpndecladigdDSTLDSVEQRc 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  70 --DALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQ 147
Cdd:PLN02542 229 ivNVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYID 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 148 RKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPT 227
Cdd:PLN02542 309 DLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPT 388
                        250
                 ....*....|....*.
gi 578817185 228 DIHQRAPVILGSPDDV 243
Cdd:PLN02542 389 EIHQRVPLYIGSVEEV 404
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
1-114 1.95e-69

Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this protein family.


Pssm-ID: 395249  Cd Length: 189  Bit Score: 211.88  E-value: 1.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185    1 MNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVA 80
Cdd:pfam00316  73 KNALKASGIVAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVA 152
                          90       100       110
                  ....*....|....*....|....*....|....
gi 578817185   81 AGYALYGSATMLVLAMDCGVNCFMLDPAIGEFIL 114
Cdd:pfam00316 153 AGYVVYGSSTMLVLTTGCGVHGFTLDPSLGEFIL 186
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
4-245 9.33e-69

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337  Cd Length: 351  Bit Score: 215.82  E-value: 9.33e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   4 LKSSFATCVLVSEEDKHAIIVEPEkrGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKS------TDEPSEKDALQPGRN 77
Cdd:PLN02628  94 LRNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVeadhlpVEEKAQLNVLQRGSR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  78 LVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQR-KKFPPDNS 156
Cdd:PLN02628 172 LVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIDTvRQGKGQYP 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 157 APYGARYVGSMVADVHRTLVYGGIFLypankkSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVI 236
Cdd:PLN02628 252 KKYSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQRLPLF 325

                 ....*....
gi 578817185 237 LGSPDDVLE 245
Cdd:PLN02628 326 LGSSEDVLE 334
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
128-250 2.91e-61

Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of Fructose-1-6-bisphosphatase enzymes. According to ECOD this domain has a Rossmann-like fold.


Pssm-ID: 408683 [Multi-domain]  Cd Length: 125  Bit Score: 188.59  E-value: 2.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  128 YSLNEGYARDFDPAVTEYIQRKKFPPdnsAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVM 207
Cdd:pfam18913   5 YAINEGNARHWNAPYRAYIDDLKSGG---KGYTLRYVGSMVADVHRILLKGGIFLYPADKRAPNGKLRLLYECAPLAFLI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578817185  208 EKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVY 250
Cdd:pfam18913  82 EQAGGKASDGKQRILDIVPDSLHQRTPIFLGSREEVERVEAYL 124
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
4-246 1.08e-37

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256  Cd Length: 304  Bit Score: 134.09  E-value: 1.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   4 LKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYrkkstdePSEKDALQPGRNLVAAGY 83
Cdd:PLN02462  66 LKYSHVCKYACSEEVPEVQDMGGPVEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAM 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  84 ALYGSATMLVLAMDCGVNCFmldpaigEFILvdkdvkikkkgkiysLNEG---YARDfdpaVTEYIQRKKFPPDN----- 155
Cdd:PLN02462 139 GIYGPRTTYVVALKDGPGTH-------EFLL---------------LDDGkwqHVKE----TTEIGEGKIFSPGNlratf 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 156 -------------SAPYGARYVGSMVADVHRTLVY-GGIFLYPANKKSPnGKLRLLYECNPMAYVMEKAGGMATTGKEA- 220
Cdd:PLN02462 193 dnpgyeklinyyvSEKYTLRYTGGMVPDVYQIIVKeKGVFTNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGVQGg 271
                        250       260
                 ....*....|....*....|....*..
gi 578817185 221 -VLDVIPTDIHQRAPVILGSPDDVLEF 246
Cdd:PLN02462 272 sVLDKQINNLDQRTQVAYGSKNEVIRF 298
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
1-217 1.83e-27

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: 104.01  E-value: 1.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   1 MNMLKSSFATCVLVSEEDKHAIIVEpEKRGKYVVCFDPLDGSSNID-CLVSVGTIFGIYRkkstdepsekdalqpgrnlv 79
Cdd:cd01636   49 RNMLKSSFPDVKIVGEESGVAEEVM-GRRDEYTWVIDPIDGTKNFInGLPFVAVVIAVYV-------------------- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  80 aagyalygsatmlvlamdcgvncfmldpaigefilvdkdvkikkkgkIYSLNEGYARDFDPavteyiqrKKFPPDNSAPY 159
Cdd:cd01636  108 -----------------------------------------------ILILAEPSHKRVDE--------KKAELQLLAVY 132
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817185 160 GARYVGSMVADVHRTLV-YGGIFLYPANKkspngklRLLYECNPMAYVMEKAGGMATTG 217
Cdd:cd01636  133 RIRIVGSAVAKMCLVALgLADIYYEPGGK-------RRAWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
1-238 2.59e-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: 75.43  E-value: 2.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185   1 MNMLKSSFATCVLVSEEDKHAIIVEpekRGKYVVCFDPLDGSSN-IDCLVSVGTIFGIYRKKSTdepsekdalqpgrnlV 79
Cdd:cd01637   47 VDVLKALFPDDGILGEEGGGSGNVS---DGGRVWVIDPIDGTTNfVAGLPNFAVSIALYEDGKP---------------V 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185  80 AAGYALYGsATMLVLAM-DCGVNCFMLDPA------IGEFILvdkdvkikkkgkiySLNEGYARDFDPAVteyiqrkkFP 152
Cdd:cd01637  109 LGVIYDPM-LDELYYAGrGKGAFLNGKKLPlskdtpLNDALL--------------STNASMLRSNRAAV--------LA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817185 153 PDNSAPYGARYVGSMVADVHRTLVY-GGIFLYPANKkspngklrlLYECNPMAYVMEKAGGMATTGKEAVLdviptDIHQ 231
Cdd:cd01637  166 SLVNRALGIRIYGSAGLDLAYVAAGrLDAYLSSGLN---------PWDYAAGALIVEEAGGIVTDLDGEPL-----DTLN 231

                 ....*..
gi 578817185 232 RAPVILG 238
Cdd:cd01637  232 RSGIIAA 238
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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