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Conserved domains on  [gi|16579888|ref|NP_000498|]
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fructose-1,6-bisphosphatase 1 [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, ...
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  Cd Length: 315  Bit Score: 519.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  18 VMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  98 EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 178 MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16579888 258 VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVY 332
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
 
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  Cd Length: 315  Bit Score: 519.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  18 VMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  98 EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 178 MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16579888 258 VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVY 332
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-332 8.85e-158

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 445.02  E-value: 8.85e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888    9 TDVNTLTRFVM-EEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLK 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   88 SSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  168 YGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  248 SMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329

                 ....*
gi 16579888  328 FLKVY 332
Cdd:PLN02262 330 IKALY 334
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
13-335 3.15e-133

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 382.43  E-value: 3.15e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  13 TLTRFVMEEGRKARG-TGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFA 91
Cdd:COG0158   3 TLGRFLVEKQKEFKAaTAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKARGN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  92 TCVLVSEEdKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDePSEKDALQPGRNLVAAGYALYGSA 171
Cdd:COG0158  83 VAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYGPS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 172 TMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYI---QRKKfpPDNSAPYGARYVGS 248
Cdd:COG0158 161 TMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIkdcFAED--KGTRRPYNMRYIGS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 249 MVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEF 328
Cdd:COG0158 239 MVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEKL 318

                ....*..
gi 16579888 329 LKVYEKH 335
Cdd:COG0158 319 ERFIKEF 325
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
13-196 1.03e-107

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: 312.42  E-value: 1.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888    13 TLTRFVMEEGRKAR-GTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFA 91
Cdd:pfam00316   2 TLTRFIIEEQHEFPnATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVLADEILKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888    92 TCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSA 171
Cdd:pfam00316  82 VAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAGYVVYGSS 161
                         170       180
                  ....*....|....*....|....*
gi 16579888   172 TMLVLAMDCGVNCFMLDPAIGEFIL 196
Cdd:pfam00316 162 TMLVLTTGCGVHGFTLDPSLGEFIL 186
 
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  Cd Length: 315  Bit Score: 519.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  18 VMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVS 97
Cdd:cd00354   1 LLEQLRKGAATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  98 EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA 177
Cdd:cd00354  81 EEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 178 MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL 257
Cdd:cd00354 161 LGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRIL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16579888 258 VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVY 332
Cdd:cd00354 241 VRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
9-332 8.85e-158

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 445.02  E-value: 8.85e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888    9 TDVNTLTRFVM-EEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLK 87
Cdd:PLN02262  10 TDLMTITRFVLnEQSKHPEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGETNVQGEEQKKLDVLSNDVFIKALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   88 SSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYAL 167
Cdd:PLN02262  90 SSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAGYCM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  168 YGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVG 247
Cdd:PLN02262 170 YGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLRYIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  248 SMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLE 327
Cdd:PLN02262 250 SMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDDVEE 329

                 ....*
gi 16579888  328 FLKVY 332
Cdd:PLN02262 330 IKALY 334
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
13-335 7.63e-146

class 1 fructose-bisphosphatase;


Pssm-ID: 236458  Cd Length: 327  Bit Score: 414.25  E-value: 7.63e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   13 TLTRFVMEEGRKARG-TGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFA 91
Cdd:PRK09293   4 TLGEFLVEQQREFPHaTGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDVFANEILIEALKARGH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   92 TCVLVSEEDKHAIIVePEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKStDEPSEKDALQPGRNLVAAGYALYGSA 171
Cdd:PRK09293  84 VAGLASEEEDEIVPI-PENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGYVLYGPS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  172 TMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYI---QRKKFPPDnsAPYGARYVGS 248
Cdd:PRK09293 162 TMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIellAGKDGPRG--RPYNMRYIGS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  249 MVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEF 328
Cdd:PRK09293 240 MVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSKEEVERV 319

                 ....*..
gi 16579888  329 LKVYEKH 335
Cdd:PRK09293 320 EEYHAEA 326
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
13-335 3.15e-133

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 382.43  E-value: 3.15e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  13 TLTRFVMEEGRKARG-TGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFA 91
Cdd:COG0158   3 TLGRFLVEKQKEFKAaTAELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLDVFANEILIEALKARGN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  92 TCVLVSEEdKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDePSEKDALQPGRNLVAAGYALYGSA 171
Cdd:COG0158  83 VAGIASEE-EDEPVTFPENNGSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGSP-GTEEDFLQPGNKQVAAGYVVYGPS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 172 TMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYI---QRKKfpPDNSAPYGARYVGS 248
Cdd:COG0158 161 TMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIkdcFAED--KGTRRPYNMRYIGS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 249 MVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEF 328
Cdd:COG0158 239 MVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSKEEVEKL 318

                ....*..
gi 16579888 329 LKVYEKH 335
Cdd:COG0158 319 ERFIKEF 325
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
13-196 1.03e-107

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: 312.42  E-value: 1.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888    13 TLTRFVMEEGRKAR-GTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFA 91
Cdd:pfam00316   2 TLTRFIIEEQHEFPnATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVLADEILKNALKASGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888    92 TCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSA 171
Cdd:pfam00316  82 VAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAGYVVYGSS 161
                         170       180
                  ....*....|....*....|....*
gi 16579888   172 TMLVLAMDCGVNCFMLDPAIGEFIL 196
Cdd:pfam00316 162 TMLVLTTGCGVHGFTLDPSLGEFIL 186
PLN02542 PLN02542
fructose-1,6-bisphosphatase
10-325 1.37e-99

fructose-1,6-bisphosphatase


Pssm-ID: 215298  Cd Length: 412  Bit Score: 299.87  E-value: 1.37e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   10 DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSS 89
Cdd:PLN02542  75 EIQTLTTWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEVFSNCLRSS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   90 FATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYR-----------KKSTDEPSEK---DALQ 155
Cdd:PLN02542 155 GRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSpndecladigdDSTLDSVEQRcivNVCQ 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  156 PGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPP 235
Cdd:PLN02542 235 PGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKDPG 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  236 DNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRA 315
Cdd:PLN02542 315 PSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRV 394
                        330
                 ....*....|
gi 16579888  316 PVILGSPDDV 325
Cdd:PLN02542 395 PLYIGSVEEV 404
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
8-327 1.85e-76

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337  Cd Length: 351  Bit Score: 238.54  E-value: 1.85e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888    8 DTDVNTLTRFVMEEGRKArgTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTG----DQVKKLDVLSNDLVM 83
Cdd:PLN02628  14 AEGVCTLMEFLGTEGSNV--GDDLVVLMAHIQAACKRIAALLASPFNSELGKTSSGASGASgsgrDAPKPLDIVSNEIIL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   84 NMLKSSFATCVLVSEEDKHAIIVEPEkrGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKS------TDEPSEKDALQPG 157
Cdd:PLN02628  92 SSLRNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVeadhlpVEEKAQLNVLQRG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  158 RNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQR-KKFPPD 236
Cdd:PLN02628 170 SRLVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIDTvRQGKGQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  237 NSAPYGARYVGSMVADVHRTLVYGGIFLypankkSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAP 316
Cdd:PLN02628 250 YPKKYSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQRLP 323
                        330
                 ....*....|.
gi 16579888  317 VILGSPDDVLE 327
Cdd:PLN02628 324 LFLGSSEDVLE 334
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
210-332 7.89e-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: 190.51  E-value: 7.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   210 YSLNEGYARDFDPAVTEYIQRKKFPPdnsAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVM 289
Cdd:pfam18913   5 YAINEGNARHWNAPYRAYIDDLKSGG---KGYTLRYVGSMVADVHRILLKGGIFLYPADKRAPNGKLRLLYECAPLAFLI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 16579888   290 EKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVY 332
Cdd:pfam18913  82 EQAGGKASDGKQRILDIVPDSLHQRTPIFLGSREEVERVEAYL 124
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
30-328 7.37e-46

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256  Cd Length: 304  Bit Score: 157.97  E-value: 7.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   30 ELTQLLNSLCTAVKAISSAVRKAgiahLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPE 109
Cdd:PLN02462  14 KLRRLIMCMGEACRTIAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  110 KRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYrkkstdePSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFmldp 189
Cdd:PLN02462  90 VEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAMGIYGPRTTYVVALKDGPGTH---- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  190 aigEFILvdkdvkikkkgkiysLNEG---YARDfdpaVTEYIQRKKFPPDN------------------SAPYGARYVGS 248
Cdd:PLN02462 159 ---EFLL---------------LDDGkwqHVKE----TTEIGEGKIFSPGNlratfdnpgyeklinyyvSEKYTLRYTGG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  249 MVADVHRTLVY-GGIFLYPANKKSPnGKLRLLYECNPMAYVMEKAGGMATTGKEA--VLDVIPTDIHQRAPVILGSPDDV 325
Cdd:PLN02462 217 MVPDVYQIIVKeKGVFTNVTSPKSK-AKLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQINNLDQRTQVAYGSKNEV 295

                 ...
gi 16579888  326 LEF 328
Cdd:PLN02462 296 IRF 298
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
35-299 4.44e-45

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: 152.16  E-value: 4.44e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  35 LNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEpEKRGKY 114
Cdd:cd01636   1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVM-GRRDEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 115 VVCFDPLDGSSNID-CLVSVGTIFGIYRkkstdepsekdalqpgrnlvaagyalygsatmlvlamdcgvncfmldpaige 193
Cdd:cd01636  80 TWVIDPIDGTKNFInGLPFVAVVIAVYV---------------------------------------------------- 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 194 filvdkdvkikkkgkIYSLNEGYARDFDPavteyiqrKKFPPDNSAPYGARYVGSMVADVHRTLV-YGGIFLYPANKksp 272
Cdd:cd01636 108 ---------------ILILAEPSHKRVDE--------KKAELQLLAVYRIRIVGSAVAKMCLVALgLADIYYEPGGK--- 161
                       250       260
                ....*....|....*....|....*..
gi 16579888 273 ngklRLLYECNPMAYVMEKAGGMATTG 299
Cdd:cd01636 162 ----RRAWDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
35-320 9.12e-26

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: 103.16  E-value: 9.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  35 LNSLCTAVKAISSAVRKAGIAHLYgiAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEpekRGKY 114
Cdd:cd01637   1 LELALKAVREAGALILEAFGEELT--VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVS---DGGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 115 VVCFDPLDGSSN-IDCLVSVGTIFGIYRKKSTdepsekdalqpgrnlVAAGYALYGsATMLVLAM-DCGVNCFMLDPA-- 190
Cdd:cd01637  76 VWVIDPIDGTTNfVAGLPNFAVSIALYEDGKP---------------VLGVIYDPM-LDELYYAGrGKGAFLNGKKLPls 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888 191 ----IGEFILvdkdvkikkkgkiySLNEGYARDFDPAVteyiqrkkFPPDNSAPYGARYVGSMVADVHRTLVY-GGIFLY 265
Cdd:cd01637 140 kdtpLNDALL--------------STNASMLRSNRAAV--------LASLVNRALGIRIYGSAGLDLAYVAAGrLDAYLS 197
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16579888 266 PANKkspngklrlLYECNPMAYVMEKAGGMATTGKEAVLdviptDIHQRAPVILG 320
Cdd:cd01637 198 SGLN---------PWDYAAGALIVEEAGGIVTDLDGEPL-----DTLNRSGIIAA 238
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
45-126 1.25e-05

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673  Cd Length: 263  Bit Score: 46.05  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888   45 ISSAVRKAgIAHLYGI--AGST---NVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEkrgkYVVCFD 119
Cdd:PRK12676  13 MAKEVEKA-IMPLFGTpdAGETvgmGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPE----YTVVLD 87

                 ....*..
gi 16579888  120 PLDGSSN 126
Cdd:PRK12676  88 PLDGTYN 94
Inositol_P pfam00459
Inositol monophosphatase family;
30-134 7.51e-04

Inositol monophosphatase family;


Pssm-ID: 395369 [Multi-domain]  Cd Length: 270  Bit Score: 40.40  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888    30 ELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPE 109
Cdd:pfam00459   1 DLEEVLKVAVELAAKAGEVLREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQSEL 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 16579888   110 KRGKYVVCFDPLDGSSN----IDCL-VSVG 134
Cdd:pfam00459  81 TDDGPTWIIDPIDGTTNfvhgIPQFaVSIG 110
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
34-147 1.21e-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  Cd Length: 244  Bit Score: 39.74  E-value: 1.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16579888  34 LLNSLCTAVKAISSAVR---KAGIAHLYGIAGstnvtGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEdkhAIIVEPEK 110
Cdd:cd01642   1 MLEVLEKITKEIILLLNeknRQGLVKLIRGAG-----GDVTRVADLKAEEIILKLLREEGVFGQIISEE---SGEIRKGS 72
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 16579888 111 rGKYVVCFDPLDGSSN-IDCLVSVGTIFGIYRKKSTDE 147
Cdd:cd01642  73 -GEYIAVLDPLDGSTNyLSGIPFYSVSVALADPRSKVK 109
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
68-126 2.49e-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  Cd Length: 257  Bit Score: 38.90  E-value: 2.49e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16579888  68 GDQVKKLDVLSNDLVMNMLKSsFATCVLVSEEDkhAIIVEpEKRGKYVVCFDPLDGSSN 126
Cdd:cd01515  35 GTPTKLIDKVAEDAAIEILKK-LGSVNIVSEEI--GVIDN-GDEPEYTVVLDPLDGTYN 89
 
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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