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Conserved domains on  [gi|162312145|ref|NP_595083|]
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fructose-1,6-bisphosphatase Fbp1 [Schizosaccharomyces pombe]

Protein Classification

class 1 fructose-1,6-bisphosphatase (domain architecture ID 10000674)

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
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
12-347 9.69e-175

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


:

Pssm-ID: 223236  Cd Length: 326  Bit Score: 487.98  E-value: 9.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  12 IVTLSSFILQEQRRYNQKHkneegkpciiqeasGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLD 91
Cdd:COG0158    1 MKTLGRFLVEKQKEFKAAT--------------AELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLD 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  92 KICNDIFITAMKSNGCCKLIVSEEEEDLIVVDSN-GSYAVTCDPIDGSSNIDAGVSVGTIFGIYKlRPGSQGDISDVLRP 170
Cdd:COG0158   67 VFANEILIEALKARGNVAGIASEEEDEPVTFPENnGSYAVAYDPLDGSSNIDVNVSVGTIFSIYR-RPGSPGTEEDFLQP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 171 GKEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKESTP 250
Cdd:COG0158  146 GNKQVAAGYVVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDK 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 251 D-KKPYSARYIGSMVADMHRTILYGGLFAYPCSKGN-NGKLRLLYECFPMAFLVEQAGGIAVnDKGDRILDLVPKTLHGK 328
Cdd:COG0158  226 GtRRPYNMRYIGSMVADVHRILLKGGIFLYPSDKRApNGKLRLLYEANPMAFLVEQAGGKAT-DGKQRILDIVPEKLHQR 304
                        330
                 ....*....|....*....
gi 162312145 329 SSIWLGSKHEVEEYINFIK 347
Cdd:COG0158  305 VPLFLGSKEEVEKLERFIK 323
 
Name Accession Description Interval E-value
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
12-347 9.69e-175

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 487.98  E-value: 9.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  12 IVTLSSFILQEQRRYNQKHkneegkpciiqeasGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLD 91
Cdd:COG0158    1 MKTLGRFLVEKQKEFKAAT--------------AELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLD 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  92 KICNDIFITAMKSNGCCKLIVSEEEEDLIVVDSN-GSYAVTCDPIDGSSNIDAGVSVGTIFGIYKlRPGSQGDISDVLRP 170
Cdd:COG0158   67 VFANEILIEALKARGNVAGIASEEEDEPVTFPENnGSYAVAYDPLDGSSNIDVNVSVGTIFSIYR-RPGSPGTEEDFLQP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 171 GKEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKESTP 250
Cdd:COG0158  146 GNKQVAAGYVVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDK 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 251 D-KKPYSARYIGSMVADMHRTILYGGLFAYPCSKGN-NGKLRLLYECFPMAFLVEQAGGIAVnDKGDRILDLVPKTLHGK 328
Cdd:COG0158  226 GtRRPYNMRYIGSMVADVHRILLKGGIFLYPSDKRApNGKLRLLYEANPMAFLVEQAGGKAT-DGKQRILDIVPEKLHQR 304
                        330
                 ....*....|....*....
gi 162312145 329 SSIWLGSKHEVEEYINFIK 347
Cdd:COG0158  305 VPLFLGSKEEVEKLERFIK 323
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
42-346 2.30e-171

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: 478.97  E-value: 2.30e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  42 EASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIV 121
Cdd:cd00354    9 AATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASEEEEEPVP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 122 VDS--NGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRPGSQGDISDVLRPGKEMVAAGYTMYGASAHLLLTTGHRVNGF 199
Cdd:cd00354   89 VEEskDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLTLGQGVHGF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 200 TLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKESTPDKKPYSARYIGSMVADMHRTILYGGLFAY 279
Cdd:cd00354  169 TLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRILVRGGIFLY 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312145 280 PCSKGN-NGKLRLLYECFPMAFLVEQAGGIAVNDKGdRILDLVPKTLHGKSSIWLGSKHEVEEYINFI 346
Cdd:cd00354  249 PADKKSpKGKLRLLYEANPMAFLVEQAGGKATDGKE-RILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
1-341 5.10e-146

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 415.74  E-value: 5.10e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145   1 MKKDLDEIDTDIVTLSSFILQEQRRYnqkhkneegkpciiQEASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIV 80
Cdd:PLN02262   1 MDHAADAHRTDLMTITRFVLNEQSKH--------------PEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGET 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  81 NSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIVVDS--NGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRP 158
Cdd:PLN02262  67 NVQGEEQKKLDVLSNDVFIKALVSSGRTNVLVSEEDEEAIFVEPskRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 159 GSQGDISDVLRPGKEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKI 238
Cdd:PLN02262 147 GGEGTVEDVLQPGKEMVAAGYCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 239 ARFIAHLKESTPDKKPYSARYIGSMVADMHRTILYGGLFAYPC-SKGNNGKLRLLYECFPMAFLVEQAGGIAVNDKGdRI 317
Cdd:PLN02262 227 AKYVEKCKFPKDGSSPKSLRYIGSMVADVHRTLLYGGIFLYPAdKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQ-RA 305
                        330       340
                 ....*....|....*....|....
gi 162312145 318 LDLVPKTLHGKSSIWLGSKHEVEE 341
Cdd:PLN02262 306 LDLVPTKIHERSPIFLGSYDDVEE 329
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
14-212 1.12e-86

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: 259.26  E-value: 1.12e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145   14 TLSSFILQEQRRYnqkhkneegkpciiQEASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLDKI 93
Cdd:pfam00316   2 TLTRFIIEEQHEF--------------PNATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145   94 CNDIFITAMKSNGCCKLIVSEEEEDLIVVD--SNGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRPGSQGDISDVLRPG 171
Cdd:pfam00316  68 ADEILKNALKASGIVAVLVSEEEEELIVFEgnKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPG 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 162312145  172 KEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTH 212
Cdd:pfam00316 148 NEQVAAGYVVYGSSTMLVLTTGCGVHGFTLDPSLGEFILTH 188
 
Name Accession Description Interval E-value
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
12-347 9.69e-175

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


Pssm-ID: 223236  Cd Length: 326  Bit Score: 487.98  E-value: 9.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  12 IVTLSSFILQEQRRYNQKHkneegkpciiqeasGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLD 91
Cdd:COG0158    1 MKTLGRFLVEKQKEFKAAT--------------AELSAVLSSIALAGKEIAREINKAGLAGVLGYSGAENVQGDTQKKLD 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  92 KICNDIFITAMKSNGCCKLIVSEEEEDLIVVDSN-GSYAVTCDPIDGSSNIDAGVSVGTIFGIYKlRPGSQGDISDVLRP 170
Cdd:COG0158   67 VFANEILIEALKARGNVAGIASEEEDEPVTFPENnGSYAVAYDPLDGSSNIDVNVSVGTIFSIYR-RPGSPGTEEDFLQP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 171 GKEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKESTP 250
Cdd:COG0158  146 GNKQVAAGYVVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIKDCFAEDK 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 251 D-KKPYSARYIGSMVADMHRTILYGGLFAYPCSKGN-NGKLRLLYECFPMAFLVEQAGGIAVnDKGDRILDLVPKTLHGK 328
Cdd:COG0158  226 GtRRPYNMRYIGSMVADVHRILLKGGIFLYPSDKRApNGKLRLLYEANPMAFLVEQAGGKAT-DGKQRILDIVPEKLHQR 304
                        330
                 ....*....|....*....
gi 162312145 329 SSIWLGSKHEVEEYINFIK 347
Cdd:COG0158  305 VPLFLGSKEEVEKLERFIK 323
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
42-346 2.30e-171

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: 478.97  E-value: 2.30e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  42 EASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIV 121
Cdd:cd00354    9 AATGDLTDLLSSLALACKEISRAVRRAGLAGLLGLAGSVNVQGDEQKKLDVLANDIFIEALKSSGVVAVLASEEEEEPVP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 122 VDS--NGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRPGSQGDISDVLRPGKEMVAAGYTMYGASAHLLLTTGHRVNGF 199
Cdd:cd00354   89 VEEskDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAGYALYGPSTMLVLTLGQGVHGF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 200 TLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKESTPDKKPYSARYIGSMVADMHRTILYGGLFAY 279
Cdd:cd00354  169 TLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLRYIGSMVADVHRILVRGGIFLY 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312145 280 PCSKGN-NGKLRLLYECFPMAFLVEQAGGIAVNDKGdRILDLVPKTLHGKSSIWLGSKHEVEEYINFI 346
Cdd:cd00354  249 PADKKSpKGKLRLLYEANPMAFLVEQAGGKATDGKE-RILDIVPTSLHQRVPVILGSKEEVERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
1-341 5.10e-146

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 415.74  E-value: 5.10e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145   1 MKKDLDEIDTDIVTLSSFILQEQRRYnqkhkneegkpciiQEASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIV 80
Cdd:PLN02262   1 MDHAADAHRTDLMTITRFVLNEQSKH--------------PEARGDLTILLSHIVLGCKFVCSAVNKAGLAKLIGLAGET 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  81 NSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIVVDS--NGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRP 158
Cdd:PLN02262  67 NVQGEEQKKLDVLSNDVFIKALVSSGRTNVLVSEEDEEAIFVEPskRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 159 GSQGDISDVLRPGKEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKI 238
Cdd:PLN02262 147 GGEGTVEDVLQPGKEMVAAGYCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 239 ARFIAHLKESTPDKKPYSARYIGSMVADMHRTILYGGLFAYPC-SKGNNGKLRLLYECFPMAFLVEQAGGIAVNDKGdRI 317
Cdd:PLN02262 227 AKYVEKCKFPKDGSSPKSLRYIGSMVADVHRTLLYGGIFLYPAdKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQ-RA 305
                        330       340
                 ....*....|....*....|....
gi 162312145 318 LDLVPKTLHGKSSIWLGSKHEVEE 341
Cdd:PLN02262 306 LDLVPTKIHERSPIFLGSYDDVEE 329
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
13-344 6.03e-139

class 1 fructose-bisphosphatase;


Pssm-ID: 236458  Cd Length: 327  Bit Score: 397.30  E-value: 6.03e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  13 VTLSSFILQEQRRYnqkhkneegkpciiQEASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLDK 92
Cdd:PRK09293   3 KTLGEFLVEQQREF--------------PHATGELTALISAIALAAKIISRAINKGGLADILGAAGTENVQGETQKKLDV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  93 ICNDIFITAMKSNGCCKLIVSEEEEDLIVVDSN-GSYAVTCDPIDGSSNIDAGVSVGTIFGIYKlRPGSQGDISDVLRPG 171
Cdd:PRK09293  69 FANEILIEALKARGHVAGLASEEEDEIVPIPENeGKYLVAYDPLDGSSNIDVNVSVGTIFSIYR-APVGTPTEEDFLQPG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 172 KEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKEST-P 250
Cdd:PRK09293 148 NNQVAAGYVLYGPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIELLAGKDgP 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 251 DKKPYSARYIGSMVADMHRTILYGGLFAYPCSKGN-NGKLRLLYECFPMAFLVEQAGGIAVNDKgDRILDLVPKTLHGKS 329
Cdd:PRK09293 228 RGRPYNMRYIGSMVADVHRILLKGGIFLYPADEPYpNGKLRLLYEANPMAFLVEQAGGAASDGK-QRILDIEPESLHQRV 306
                        330
                 ....*....|....*...
gi 162312145 330 SIWLGSKHEV---EEYIN 344
Cdd:PRK09293 307 PLFLGSKEEVervEEYHA 324
PLN02542 PLN02542
fructose-1,6-bisphosphatase
45-346 3.32e-101

fructose-1,6-bisphosphatase


Pssm-ID: 215298  Cd Length: 412  Bit Score: 304.10  E-value: 3.32e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  45 GELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIVVDS 124
Cdd:PLN02542  94 AELTIVLSSISMACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEVFSNCLRSSGRTGIIASEEEDVPVAVEE 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 125 N--GSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRPGSQGDISD--------------VLRPGKEMVAAGYTMYGASAHL 188
Cdd:PLN02542 174 SysGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDECLADIGDdstldsveqrcivnVCQPGSNLLAAGYCMYSSSVIF 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 189 LLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHLKESTPDKKPYSARYIGSMVADMH 268
Cdd:PLN02542 254 VLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYIDDLKDPGPSGKPYSARYIGSLVGDFH 333
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312145 269 RTILYGGLFAYPC-SKGNNGKLRLLYECFPMAFLVEQAGGIAvNDKGDRILDLVPKTLHGKSSIWLGSKHEVEEYINFI 346
Cdd:PLN02542 334 RTLLYGGIYGYPRdKKSKNGKLRLLYECAPMSFIVEQAGGKG-SDGHQRILDIQPTEIHQRVPLYIGSVEEVEKLEKYL 411
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
14-212 1.12e-86

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: 259.26  E-value: 1.12e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145   14 TLSSFILQEQRRYnqkhkneegkpciiQEASGELSLLLNSLQFSFKFIANTIRKAELVNLIGLSGIVNSTGDEQKKLDKI 93
Cdd:pfam00316   2 TLTRFIIEEQHEF--------------PNATGELTGLLSALQLAAKFISRDIRKAGLANLLGLAGAENVQGDVQKKLDVL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145   94 CNDIFITAMKSNGCCKLIVSEEEEDLIVVD--SNGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKLRPGSQGDISDVLRPG 171
Cdd:pfam00316  68 ADEILKNALKASGIVAVLVSEEEEELIVFEgnKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPG 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 162312145  172 KEMVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTH 212
Cdd:pfam00316 148 NEQVAAGYVVYGSSTMLVLTTGCGVHGFTLDPSLGEFILTH 188
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
32-341 1.66e-73

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337  Cd Length: 351  Bit Score: 231.22  E-value: 1.66e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  32 NEEGKPCII----QEASG---ELSLLLNSLQFSFKFIANTI---RKAELVNLIGLSGIVNSTG-DEQKKLDKICNDIFIT 100
Cdd:PLN02628  13 GAEGVCTLMeflgTEGSNvgdDLVVLMAHIQAACKRIAALLaspFNSELGKTSSGASGASGSGrDAPKPLDIVSNEIILS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 101 AMKSNGCCKLIVSEEEEDLIVVDSNGSYAVTCDPIDGSSNIDAGVSVGTIFGIYKlR-------PGSQGDISDVLRPGKE 173
Cdd:PLN02628  93 SLRNSGKVAVMASEEDDAPIWIGDDGPYVVVFDPLDGSRNIDASIPTGTIFGIYN-RlveadhlPVEEKAQLNVLQRGSR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 174 MVAAGYTMYGASAHLLLTTGHRVNGFTLDTDIGEFILTHRNMKMPLQHSIYSINEGYTAFWDEKIARFIAHL---KESTP 250
Cdd:PLN02628 172 LVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIDTVrqgKGQYP 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 251 dkKPYSARYIGSMVADMHRTILYGGLFAYPCSkgnngKLRLLYECFPMAFLVEQAGGIAVNDKgDRILDLVPKTLHGKSS 330
Cdd:PLN02628 252 --KKYSARYICSLVADLHRTILYGGIAMNPRS-----HLRLVYEANPLSFLVEQAGGRGSDGK-RRILSIQPVKLHQRLP 323
                        330
                 ....*....|.
gi 162312145 331 IWLGSKHEVEE 341
Cdd:PLN02628 324 LFLGSSEDVLE 334
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
222-347 9.58e-56

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: 177.80  E-value: 9.58e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  222 SIYSINEGYTAFWDEKIARFIAHLKEStpdKKPYSARYIGSMVADMHRTILYGGLFAYPCSKGN-NGKLRLLYECFPMAF 300
Cdd:pfam18913   3 KIYAINEGNARHWNAPYRAYIDDLKSG---GKGYTLRYVGSMVADVHRILLKGGIFLYPADKRApNGKLRLLYECAPLAF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 162312145  301 LVEQAGGIAVNDKGdRILDLVPKTLHGKSSIWLGSKHEVEEYINFIK 347
Cdd:pfam18913  80 LIEQAGGKASDGKQ-RILDIVPDSLHQRTPIFLGSREEVERVEAYLK 125
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
61-346 6.85e-40

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256  Cd Length: 304  Bit Score: 142.56  E-value: 6.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  61 IANTIRKAelvnLIGLSGIVNSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIVVDSN--GSYAVTCDPIDGS 138
Cdd:PLN02462  29 IAFKVRTA----SCTGTACVNSFGDEQLAVDMLADKLLFEALKYSHVCKYACSEEVPEVQDMGGPveGGFSVAFDPLDGS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 139 SNIDAGVSVGTIFGIYklrPGsqgdisDVL--RPGKEMVAAGYTMYGASAHLL--LTTGHRVNGFTLDTDiGEFIltHRN 214
Cdd:PLN02462 105 SIVDTNFAVGTIFGVW---PG------DKLtgVTGRDQVAAAMGIYGPRTTYVvaLKDGPGTHEFLLLDD-GKWQ--HVK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 215 MKMPLQHS-IYSINEGYTAFWDEKIARFIAH-LKEStpdkkpYSARYIGSMVADMHRTILY-GGLFAYPCSKGNNGKLRL 291
Cdd:PLN02462 173 ETTEIGEGkIFSPGNLRATFDNPGYEKLINYyVSEK------YTLRYTGGMVPDVYQIIVKeKGVFTNVTSPKSKAKLRL 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162312145 292 LYECFPMAFLVEQAGGIAVND-KGDRILDLVPKTLHGKSSIWLGSKHEVEEYINFI 346
Cdd:PLN02462 247 LFEVAPLGLLVEKAGGKSSDGvQGGSVLDKQINNLDQRTQVAYGSKNEVIRFEETL 302
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
61-311 8.01e-13

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: 65.88  E-value: 8.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  61 IANTIRKAELVNLIGLSGIVNSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEE-EEDLIVVDSNGSYAVTCDPIDGSS 139
Cdd:cd01636   11 AGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEEsGVAEEVMGRRDEYTWVIDPIDGTK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 140 NIDAG-VSVGTIFGIYKLrpgsqgdisdvlrpgkemvaagYTMYGASahlllttghrvngftldtdigefILTHRNMKMP 218
Cdd:cd01636   91 NFINGlPFVAVVIAVYVI----------------------LILAEPS-----------------------HKRVDEKKAE 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 219 LQHSiysinegytafwdekiarfiahlkestpdkKPYSARYIGSMVADMHRTIL-YGGLFAYPcskgnnGKLRLLYECFP 297
Cdd:cd01636  126 LQLL------------------------------AVYRIRIVGSAVAKMCLVALgLADIYYEP------GGKRRAWDVAA 169
                        250
                 ....*....|....
gi 162312145 298 MAFLVEQAGGIAVN 311
Cdd:cd01636  170 SAAIVREAGGIMTD 183
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
81-325 4.28e-12

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: 65.03  E-value: 4.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145  81 NSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEDLIVVDSNGSYAVTcDPIDGSSNIDAG-VSVGTIFGIYKLRPG 159
Cdd:cd01637   29 KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVI-DPIDGTTNFVAGlPNFAVSIALYEDGKP 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 160 SQGDISDvlrpgkemVAAGYTMYGASahlllttghrvngftldtDIGEFILTHRnMKMPLQHSIYSINEGYTAFW-DEKI 238
Cdd:cd01637  108 VLGVIYD--------PMLDELYYAGR------------------GKGAFLNGKK-LPLSKDTPLNDALLSTNASMlRSNR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312145 239 ARFIAHLKestpdKKPYSARYIGSMVADMHRTILyGGLFAYpCSKGNNgklrlLYECFPMAFLVEQAGGIAVNDKGDRIL 318
Cdd:cd01637  161 AAVLASLV-----NRALGIRIYGSAGLDLAYVAA-GRLDAY-LSSGLN-----PWDYAAGALIVEEAGGIVTDLDGEPLD 228

                 ....*..
gi 162312145 319 DLVPKTL 325
Cdd:cd01637  229 TLNRSGI 235
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
84-145 8.24e-08

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673  Cd Length: 263  Bit Score: 52.60  E-value: 8.24e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312145  84 GDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEdlIVVDSNGSYAVTCDPIDGSSNIDAGV 145
Cdd:PRK12676  40 GTPTKLIDKVAEDIILEVLKPLGRCVNIISEELG--EIVGNGPEYTVVLDPLDGTYNAINGI 99
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
69-145 1.26e-04

Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. These are Mg++ dependent phosphatases. Members in this family may have fructose-1,6-bisphosphatase and/or inositol-monophosphatase activity. Fructose-1,6-bisphosphatase catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway.


Pssm-ID: 238820  Cd Length: 244  Bit Score: 42.82  E-value: 1.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312145  69 ELVNLIGLSGIVNSTGDEQKKLDKICNDIFITAMKSNGCCKLIVSEEEEdlIVVDSNGSYAVTCDPIDGSSNIDAGV 145
Cdd:cd01642   18 EKNRQGLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESG--EIRKGSGEYIAVLDPLDGSTNYLSGI 92
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
84-145 1.99e-04

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: 42.36  E-value: 1.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162312145  84 GDEQKKLDKICNDIFITAMKSNGCCKLIvsEEEEDLIVVDSNGSYAVTCDPIDGSSNIDAGV 145
Cdd:cd01515   35 GTPTKLIDKVAEDAAIEILKKLGSVNIV--SEEIGVIDNGDEPEYTVVLDPLDGTYNAINGI 94
 
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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