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Conserved domains on  [gi|255718083|ref|XP_002555322|]
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KLTH0G06556p [Lachancea thermotolerans CBS 6340]

Protein Classification

inositol monophosphatase family protein( domain architecture ID 10108155)

inositol monophosphatase family protein such as inositol monophosphatase, which catalyzes the hydrolysis of several inositol monophosphates and the artificial substrate p-nitrophenyl-phosphate to inorganic phosphate and inositol

CATH:  3.40.190.80
EC:  3.1.3.-
Gene Ontology:  GO:0008934|GO:0006020|GO:0046872
PubMed:  7890024

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 19-269 1.92e-101

IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.


:

Pssm-ID: 238817 [Multi-domain]  Cd Length: 244  Bit Score: 296.76  E-value: 1.92e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  19 ASKEVGPLLKEKAGTQFDAFDDKANQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGttEIGKEPTFIVDPIDG 98
Cdd:cd01639    8 AARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG--GLTDEPTWIIDPLDG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  99 TTNFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDlTLQQSIIALEagsersSGSSG 178
Cdd:cd01639   86 TTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK-ELKDALVATG------FPYDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 179 DDNFDIKQATYKNLLSDKGgyiHGSRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMVVGGNPNAWev 258
Cdd:cd01639  159 GDNFDRYLNNFAKLLAKAV---RGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPF-- 233

                        250
                 ....*....|.
gi 255718083 259 PVDERCYLAVR 269
Cdd:cd01639  234 DLMSGNILAGN 244
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 19-269 1.92e-101

IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.


Pssm-ID: 238817 [Multi-domain]  Cd Length: 244  Bit Score: 296.76  E-value: 1.92e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  19 ASKEVGPLLKEKAGTQFDAFDDKANQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGttEIGKEPTFIVDPIDG 98
Cdd:cd01639    8 AARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG--GLTDEPTWIIDPLDG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  99 TTNFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDlTLQQSIIALEagsersSGSSG 178
Cdd:cd01639   86 TTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK-ELKDALVATG------FPYDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 179 DDNFDIKQATYKNLLSDKGgyiHGSRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMVVGGNPNAWev 258
Cdd:cd01639  159 GDNFDRYLNNFAKLLAKAV---RGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPF-- 233

                        250
                 ....*....|.
gi 255718083 259 PVDERCYLAVR 269
Cdd:cd01639  234 DLMSGNILAGN 244
Inositol_P pfam00459
Inositol monophosphatase family;
19-277 2.50e-80

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 244.18  E-value: 2.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   19 ASKEVGPLLKEKAGTQFDAFDD-KANQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPG-TTEIGKE-PTFIVDP 95
Cdd:pfam00459  12 LAAKAGEILREAFSNKLTIEEKgKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGdQTELTDDgPTWIIDP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   96 IDGTTNFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDLTLQQSIIALEAgserssg 175
Cdd:pfam00459  92 IDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVTLFG------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  176 ssGDDNFDIKQA-TYKNLLSDKggYIHGSRSCGSAAMNMCLVATGKLDAYWEGG-CWAWDVCAGWCIVTECGGMVVGGNP 253
Cdd:pfam00459 165 --VSSRKDTSEAsFLAKLLKLV--RAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADG 240

                         250       260
                  ....*....|....*....|....
gi 255718083  254 NawevpvdERCYLAVRGGCTNPSQ 277
Cdd:pfam00459 241 G-------PFDLLAGRVIAANPKV 257
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 15-258 1.10e-76

Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family [Carbohydrate transport and metabolism]; Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440251 [Multi-domain]  Cd Length: 255  Bit Score: 234.35  E-value: 1.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  15 LVDLAsKEVGPLLKEKAGTQFDAFDDKANQvDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETyqPGTTEIGKEPTFIVD 94
Cdd:COG0483    7 ALRAA-RAAGALILRRFRELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEES--GASEGRDSGYVWVID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  95 PIDGTTNFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDlTLQQSIIALeagserss 174
Cdd:COG0483   83 PIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSART-DLEDALVAT-------- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 175 gssgDDNFDIKQATYKNLLSDKGGYIHGSRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMVVGGNPN 254
Cdd:COG0483  154 ----GFPYLRDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGE 229


                 ....
gi 255718083 255 AWEV 258
Cdd:COG0483  230 PLDL 233
PLN02553 PLN02553
inositol-phosphate phosphatase
 43-282 1.41e-69

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 216.48  E-value: 1.41e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  43 NQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQP-GTTEIGKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVP 121
Cdd:PLN02553  39 GQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAAsGGTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVP 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 122 VVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDlTLQQSIIALEAgSERSSGSSGDDNFD-IKQATYKnllsdkggyI 200
Cdd:PLN02553 119 VVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQS-ELGKALLATEV-GTKRDKATVDATTNrINALLYK---------V 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 201 HGSRSCGSAAMNMCLVATGKLDAYWE---GGCwaWDVCAGWCIVTECGGMVVGGNPNAWEVpvdercyLAVRGGCTNPSQ 277
Cdd:PLN02553 188 RSLRMSGSCALNLCGVACGRLDIFYEigfGGP--WDVAAGAVIVKEAGGLVFDPSGGPFDI-------MSRRVAASNGHL 258


                 ....*.
gi 255718083 278 K-TFVE 282
Cdd:PLN02553 259 KdAFVE 264
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 48-248 2.96e-29

3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 130398 [Multi-domain]  Cd Length: 249  Bit Score: 111.77  E-value: 2.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   48 VTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTTEIGKEPTF-IVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGVV 126
Cdd:TIGR01331  35 VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFwLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  127 YNPHLNMMFHASKDNGARLngepiKVPERDLTLQQSIIALEAGSERSSGSSGDDNFDIKQatyknLLSDKGGYIHgsrSC 206
Cdd:TIGR01331 115 YAPATGVTYFATAGKAAKR-----EGDGQALKAPIHVRPWPSGPLLVVISRSHAEEKTTE-----YLANLGYDLR---TS 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 255718083  207 GSAAMNMCLVATGKLDAYWEGGCWA-WDVCAGWCIVTECGGMV 248
Cdd:TIGR01331 182 GGSSLKFCLVAEGSADIYPRLGPTGeWDTAAGHAVLAAAGGAI 224
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 19-269 1.92e-101

IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.


Pssm-ID: 238817 [Multi-domain]  Cd Length: 244  Bit Score: 296.76  E-value: 1.92e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  19 ASKEVGPLLKEKAGTQFDAFDDKANQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGttEIGKEPTFIVDPIDG 98
Cdd:cd01639    8 AARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG--GLTDEPTWIIDPLDG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  99 TTNFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDlTLQQSIIALEagsersSGSSG 178
Cdd:cd01639   86 TTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK-ELKDALVATG------FPYDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 179 DDNFDIKQATYKNLLSDKGgyiHGSRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMVVGGNPNAWev 258
Cdd:cd01639  159 GDNFDRYLNNFAKLLAKAV---RGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPF-- 233

                        250
                 ....*....|.
gi 255718083 259 PVDERCYLAVR 269
Cdd:cd01639  234 DLMSGNILAGN 244
Inositol_P pfam00459
Inositol monophosphatase family;
19-277 2.50e-80

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 244.18  E-value: 2.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   19 ASKEVGPLLKEKAGTQFDAFDD-KANQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPG-TTEIGKE-PTFIVDP 95
Cdd:pfam00459  12 LAAKAGEILREAFSNKLTIEEKgKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGdQTELTDDgPTWIIDP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   96 IDGTTNFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDLTLQQSIIALEAgserssg 175
Cdd:pfam00459  92 IDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVTLFG------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  176 ssGDDNFDIKQA-TYKNLLSDKggYIHGSRSCGSAAMNMCLVATGKLDAYWEGG-CWAWDVCAGWCIVTECGGMVVGGNP 253
Cdd:pfam00459 165 --VSSRKDTSEAsFLAKLLKLV--RAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADG 240

                         250       260
                  ....*....|....*....|....
gi 255718083  254 NawevpvdERCYLAVRGGCTNPSQ 277
Cdd:pfam00459 241 G-------PFDLLAGRVIAANPKV 257
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 15-258 1.10e-76

Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family [Carbohydrate transport and metabolism]; Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440251 [Multi-domain]  Cd Length: 255  Bit Score: 234.35  E-value: 1.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  15 LVDLAsKEVGPLLKEKAGTQFDAFDDKANQvDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETyqPGTTEIGKEPTFIVD 94
Cdd:COG0483    7 ALRAA-RAAGALILRRFRELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEES--GASEGRDSGYVWVID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  95 PIDGTTNFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDlTLQQSIIALeagserss 174
Cdd:COG0483   83 PIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSART-DLEDALVAT-------- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 175 gssgDDNFDIKQATYKNLLSDKGGYIHGSRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMVVGGNPN 254
Cdd:COG0483  154 ----GFPYLRDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGE 229


                 ....
gi 255718083 255 AWEV 258
Cdd:COG0483  230 PLDL 233
PLN02553 PLN02553
inositol-phosphate phosphatase
 43-282 1.41e-69

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 216.48  E-value: 1.41e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  43 NQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQP-GTTEIGKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVP 121
Cdd:PLN02553  39 GQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAAsGGTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVP 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 122 VVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDlTLQQSIIALEAgSERSSGSSGDDNFD-IKQATYKnllsdkggyI 200
Cdd:PLN02553 119 VVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQS-ELGKALLATEV-GTKRDKATVDATTNrINALLYK---------V 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 201 HGSRSCGSAAMNMCLVATGKLDAYWE---GGCwaWDVCAGWCIVTECGGMVVGGNPNAWEVpvdercyLAVRGGCTNPSQ 277
Cdd:PLN02553 188 RSLRMSGSCALNLCGVACGRLDIFYEigfGGP--WDVAAGAVIVKEAGGLVFDPSGGPFDI-------MSRRVAASNGHL 258


                 ....*.
gi 255718083 278 K-TFVE 282
Cdd:PLN02553 259 KdAFVE 264
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 19-256 6.66e-57

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: 183.28  E-value: 6.66e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  19 ASKEVGPLLKEKAGTQFDAfDDKANQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTTEIGkEPTFIVDPIDG 98
Cdd:cd01637    7 AVREAGALILEAFGEELTV-ETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDG-GRVWVIDPIDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  99 TTNFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPErDLTLQQSIIALEAGSERSSGSSG 178
Cdd:cd01637   85 TTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSK-DTPLNDALLSTNASMLRSNRAAV 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255718083 179 DDnfDIKQATYknllsdkggyihGSRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMVVGGNPNAW 256
Cdd:cd01637  164 LA--SLVNRAL------------GIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPL 227
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 21-246 5.39e-48

Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate inositol monophosphate or similar substrates.


Pssm-ID: 238821 [Multi-domain]  Cd Length: 242  Bit Score: 160.19  E-value: 5.39e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  21 KEVGPLLKEKAGTQFDAfDDKANQvDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETyqpGTTEIGKEPTFIVDPIDGTT 100
Cdd:cd01643    9 QEAGDRALADFGNSLSA-ETKADG-SLVTAADRWVEQLIRARLAAQFPDDGVLGEEG---GGIFPSSGWYWVIDPIDGTT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 101 NFIHGYPYSCTSLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVpERDLTLQQSIIALeagserssgssgdd 180
Cdd:cd01643   84 NFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLAL-HPPLQLPDCNVGF-------------- 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255718083 181 NFDIK---QATYKNLLSDKGGYIhgsRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGG 246
Cdd:cd01643  149 NRSSRasaRAVLRVILRRFPGKI---RMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGG 214
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 48-253 3.33e-38

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 135.29  E-value: 3.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  48 VTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTTEIGKEPTF-IVDPIDGTTNFIHG---YpysCTSLGLVENGVPVV 123
Cdd:COG1218   38 VTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFwLVDPLDGTKEFIKRngeF---TVNIALIEDGRPVL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 124 GVVYNPHLNMMFHASKDNGARL---NGEPIKVPERDLTLQQSIIALEAGSErssgssgddnfdiKQATYKNLLSDKGgyI 200
Cdd:COG1218  115 GVVYAPALGRLYYAAKGQGAFKetgGGERQPIRVRDRPPAEPLRVVASRSH-------------RDEETEALLARLG--V 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255718083 201 HGSRSCGSAAmNMCLVATGKLDAYWE-GGCWAWDVCAGWCIVTECGGMVVG--GNP 253
Cdd:COG1218  180 AELVSVGSSL-KFCLVAEGEADLYPRlGPTMEWDTAAGQAILEAAGGRVTDldGKP 234
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 46-249 1.79e-37

CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).


Pssm-ID: 238816 [Multi-domain]  Cd Length: 242  Bit Score: 133.12  E-value: 1.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  46 DLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTtEIGKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGV 125
Cdd:cd01638   33 SPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL-RLGWDRFWLVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 126 VYNPHLNMMFHASKDNGARLNGEPIKV--PERDLTLQQSIIAleagserssgssgddnfdIKQATYKNLLSD--KGGYIH 201
Cdd:cd01638  112 VYAPALGELYYALRGGGAYKNGRPGAVslQARPPPLQPLRVV------------------ASRSHPDEELEAllAALGVA 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 255718083 202 GSRSCGSAAmNMCLVATGKLDAYWE-GGCWAWDVCAGWCIVTECGGMVV 249
Cdd:cd01638  174 EVVSIGSSL-KFCLVAEGEADIYPRlGPTMEWDTAAGDAVLRAAGGAVS 221
PLN02737 PLN02737
inositol monophosphatase family protein
 46-248 8.25e-33

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 123.76  E-value: 8.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  46 DLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTTEigKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGV 125
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSS--SDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAAT 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 126 VYN----PHL--NMMFHASKDNGARLNGEPIKVPERDLtLQQSIIALEAGSERssgssgDDNFdikqATYKNLLSDKGGY 199
Cdd:PLN02737 189 VVEfvggPMCwnTRTFSASAGGGAFCNGQKIHVSQTDK-VERSLLVTGFGYEH------DDAW----ATNIELFKEFTDV 257

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 255718083 200 IHGSRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMV 248
Cdd:PLN02737 258 SRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTV 306
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 9-253 9.06e-30

PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set.


Pssm-ID: 238775 [Multi-domain]  Cd Length: 274  Bit Score: 113.56  E-value: 9.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   9 KDIETSLVDLASKEVGPLLKEKAgtQFDAFDDKANQvDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPgtteigKE 88
Cdd:cd01517    2 LEVAILAVRAAASLTLPVFRNLG--AGDVVWKKSDK-SPVTVADYGAQALITAALARLFPSDPIVGEEDSAA------LG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  89 PTFIVDPIDGTTNFIHGYPYsCTSLGLVENGVPVVGVVYNPHLNM-------MFHASKDNGARL----NGEPIKVPERDL 157
Cdd:cd01517   73 RFWVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWLrpldGSSLQPLSVRQL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 158 TLQQSIIALEAGSERSSGSSgddnfdiKQATYKNLLSDKggyihGSRSCGSAAmNMCLVATGKLDAY---------WEGg 228
Cdd:cd01517  152 TNAARASFCESVESAHSSHR-------LQAAIKALGGTP-----QPVRLDSQA-KYAAVARGAADFYlrlplsmsyREK- 217

                        250       260
                 ....*....|....*....|....*..
gi 255718083 229 cwAWDVCAGWCIVTECGGMV--VGGNP 253
Cdd:cd01517  218 --IWDHAAGVLIVEEAGGKVtdADGKP 242
PRK10757 PRK10757
inositol-1-monophosphatase;
46-252 1.84e-29

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 112.59  E-value: 1.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  46 DLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTTEigKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGV 125
Cdd:PRK10757  38 DFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGED--QDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 126 VYNPHLNMMFHASKDNGARLNGEPIK-VPERDltLQQSIIALEAGserssgssgddnFDIKQ--ATYKNLLSDKGGYIHG 202
Cdd:PRK10757 116 VYDPMRNELFTATRGQGAQLNGYRLRgSTARD--LDGTILATGFP------------FKAKQhaTTYINIVGKLFTECAD 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255718083 203 SRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMV---VGGN 252
Cdd:PRK10757 182 FRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVsdfTGGH 234
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 48-248 2.96e-29

3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 130398 [Multi-domain]  Cd Length: 249  Bit Score: 111.77  E-value: 2.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   48 VTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTTEIGKEPTF-IVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGVV 126
Cdd:TIGR01331  35 VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFwLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  127 YNPHLNMMFHASKDNGARLngepiKVPERDLTLQQSIIALEAGSERSSGSSGDDNFDIKQatyknLLSDKGGYIHgsrSC 206
Cdd:TIGR01331 115 YAPATGVTYFATAGKAAKR-----EGDGQALKAPIHVRPWPSGPLLVVISRSHAEEKTTE-----YLANLGYDLR---TS 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 255718083  207 GSAAMNMCLVATGKLDAYWEGGCWA-WDVCAGWCIVTECGGMV 248
Cdd:TIGR01331 182 GGSSLKFCLVAEGSADIYPRLGPTGeWDTAAGHAVLAAAGGAI 224
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 19-251 8.90e-28

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: 105.94  E-value: 8.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  19 ASKEVGPL-LKEKAGTQFDAFDDKANQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTTEI-GKEPTFIVDPI 96
Cdd:cd01636    7 VAKEAGLAiLKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGrRDEYTWVIDPI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  97 DGTTNFIHGYPYSCTSLGlvengvpvVGVVYnphlnmmfhaskdngaRLNGEPIK-VPERDLTLQQSiialeagserssg 175
Cdd:cd01636   87 DGTKNFINGLPFVAVVIA--------VYVIL----------------ILAEPSHKrVDEKKAELQLL------------- 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255718083 176 ssgddnfdikqatyknllsdkggYIHGSRSCGSAAMNMCLVATGKLDAYWE--GGCWAWDVCAGWCIVTECGGMVVGG 251
Cdd:cd01636  130 -----------------------AVYRIRIVGSAVAKMCLVALGLADIYYEpgGKRRAWDVAASAAIVREAGGIMTDW 184
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 48-248 9.53e-27

histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273949 [Multi-domain]  Cd Length: 251  Bit Score: 105.08  E-value: 9.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   48 VTAVDKKIEAIIKESLNKLYPDFKFVGEETyqPGTTEIGKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGVVY 127
Cdd:TIGR02067  36 VTEADRAAEEAMRELIAAFFPDHGILGEEF--GHNEEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIF 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  128 NPHLNMMFHASKDNGARLNGEPIKVperdltlqQSIIALEAGSERSSGSSGDDNFDIKQATykNLLSDKGGYIHGSRSCG 207
Cdd:TIGR02067 114 QPATGERWWAAGGGAAFLGGRRLRV--------SSCANLSDAVLFTTSPDLLDDPGNRPAF--ERLRRAARLTRYGGDCY 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 255718083  208 saamNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMV 248
Cdd:TIGR02067 184 ----AYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCF 220
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
49-270 4.43e-26

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 103.45  E-value: 4.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  49 TAVDKKIEAIIKESLNKLYPDFKFVGEETyqpGTTEI-GKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGVVY 127
Cdd:PRK12676  44 KLIDKVAEDIILEVLKPLGRCVNIISEEL---GEIVGnGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVY 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 128 NPHLNMMFHASKDNGARLNGEPIKVPE-RDLtlqqsiialeagserssgssgdDNFDIKQATY---KNLLSDKGGYIHGS 203
Cdd:PRK12676 121 NLATGDFYEAIPGKGAYLNGKPIKVSKtSEL----------------------NESAVSIYGYrrgKERTVKLGRKVRRV 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255718083 204 RSCGSAAMNMCLVATGKLDAYWE--GGCWAWDVCAGWCIVTECGGMVVGGNPNAWEVP---VDERCYLAVRG 270
Cdd:PRK12676 179 RILGAIALELCYVASGRLDAFVDvrNYLRVTDIAAGKLICEEAGGIVTDEDGNELKLPlnvTERTNLIAANG 250
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 39-248 4.81e-25

Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate fructose-1,6-bisphosphate, inositol monophospate, 3'-phosphoadenosine-5'-phosphate, or similar substrates.


Pssm-ID: 238819 [Multi-domain]  Cd Length: 248  Bit Score: 100.41  E-value: 4.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  39 DDKANQvDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETyqpGTTEIGKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVEN 118
Cdd:cd01641   27 ETKADF-SPVTEADRAAEAAMRELIAAAFPDHGILGEEF---GNEGGDAGYVWVLDPIDGTKSFIRGLPVWGTLIALLHD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 119 GVPVVGVVYNPHLNMMFHASKDNGARLN---GEPIKVpeRDLT-LQQSIIALEAgserssgssGDDNFDIKQATYKNLLS 194
Cdd:cd01641  103 GRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRV--RACAdLAEAVLSTTD---------PHFFTPGDRAAFERLAR 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255718083 195 DkggyiHGSRSCGSAAMNMCLVATGKLDAYWEGGCWAWDVCAGWCIVTECGGMV 248
Cdd:cd01641  172 A-----VRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVI 220
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 49-275 8.84e-24

Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles.


Pssm-ID: 238773 [Multi-domain]  Cd Length: 257  Bit Score: 97.06  E-value: 8.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  49 TAVDKKIEAIIKESLNKLYPdFKFVGEETyqpGTTEIGKEP--TFIVDPIDGTTNFIHGYPYSCTSLGLVEN--GVPVVG 124
Cdd:cd01515   39 KLIDKVAEDAAIEILKKLGS-VNIVSEEI---GVIDNGDEPeyTVVLDPLDGTYNAINGIPFYSVSVAVFKIdkSDPYYG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 125 VVYNPHLNMMFHASKDNGARLNGEPIKVPERDLTLQQSIIAleagserssgSSGDDNFDIKQATYKNllsdkggyIHGSR 204
Cdd:cd01515  115 YVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSY----------YIYGKNHDRTFKICRK--------VRRVR 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255718083 205 SCGSAAMNMCLVATGKLDAYWE--GGCWAWDVCAGWCIVTECGGMVVGGNPNAWEVPVD--ERCYLAVRGGCTNP 275
Cdd:cd01515  177 IFGSVALELCYVASGALDAFVDvrENLRLVDIAAGYLIAEEAGGIVTDENGKELKLKLNvtERVNIIAANSELHK 251
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 15-255 3.72e-14

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


Pssm-ID: 238820 [Multi-domain]  Cd Length: 244  Bit Score: 70.55  E-value: 3.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  15 LVDLASKEVGPLLKEKAGTQFDAFDDKANQvDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETyqpgtTEIGK---EPTF 91
Cdd:cd01642    4 VLEKITKEIILLLNEKNRQGLVKLIRGAGG-DVTRVADLKAEEIILKLLREEGVFGQIISEES-----GEIRKgsgEYIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  92 IVDPIDGTTNFIHGYPYSCTSLGLVENGVPV-VGVVYNphlnmmfHASKDNGARLNGEPI-KVPERDLTLQQSIIalEAG 169
Cdd:cd01642   78 VLDPLDGSTNYLSGIPFYSVSVALADPRSKVkAATLDN-------FVSGEGGLKVYSPPTrFSYISVPKLGPPLV--PEV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 170 SERSSGSSGDDNFdikqATYKNLLSDKGGYIhgsRSCGSAAMNMCLVATGKLDAYWE--GGCWAWDVCAGwciVTECGGM 247
Cdd:cd01642  149 PSKIGIYEGSSRN----PEKFLLLSRNGLKF---RSLGSAALELAYTCEGSFVLFLDlrGKLRNFDVAAA---LGACKRL 218


                 ....*...
gi 255718083 248 VVGGNPNA 255
Cdd:cd01642  219 GLHGDPSN 226
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 48-248 8.21e-13

adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 66.64  E-value: 8.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  48 VTAVDKKIEAIIKESLNKLYPDFKFVGEEtyQPGTTEIGK--EPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGV 125
Cdd:PRK10931  37 VTAADIAAHTVIKDGLRTLTPDIPVLSEE--DPPAWEVRQhwQRYWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 126 VYNPHLNMMFHASK------DNGARLngePIKVpeRDLTLQQSIIALEAGserssgssgddnfdikQATYKNLLSDKGGy 199
Cdd:PRK10931 115 VYAPVMNVMYSAAEgkawkeECGVRK---QIQV--RDARPPLVVISRSHA----------------DAELKEYLQQLGE- 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 255718083 200 iHGSRSCGSaAMNMCLVATGKLDAYWE-GGCWAWDVCAGWCIVTECGGMV 248
Cdd:PRK10931 173 -HQTTSIGS-SLKFCLVAEGQAQLYPRfGPTNIWDTAAGHAVAIAAGAHV 220
PLN02911 PLN02911
inositol-phosphate phosphatase
 48-152 4.38e-12

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 65.13  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  48 VTAVDKKIEAIIKESLNKLYPDFKFVGEETyqpGTT--EIGKEPTFIVDPIDGTTNFIHGYPYSCTSLGLVENGVPVVGV 125
Cdd:PLN02911  70 VTIADRAAEEAMRSIILENFPSHAIFGEEH---GLRcgEGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGI 146

                         90       100
                 ....*....|....*....|....*..
gi 255718083 126 VYNPHLNMMFHASKDNGARLNGEPIKV 152
Cdd:PLN02911 147 IDQPVLKERWVGVAGRATTLNGEEIST 173
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 41-246 9.72e-12

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 64.27  E-value: 9.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  41 KANQVDLVTAVDKKIEAIIKESLNKLYPDFKFVGEETYQPGTTEIGKEPTFI------------------------VDPI 96
Cdd:cd01640   35 KEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDVDLdeeileescpspskdlpeedlgvwVDPL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  97 DGTTNFIHG-YPYSCTSLGLVENGVPVVGVVYNP----------HLNMMFHASKDNGARLNGEPIKVPERDLTLQQSiia 165
Cdd:cd01640  115 DATQEYTEGlLEYVTVLIGVAVKGKPIAGVIHQPfyektagagaWLGRTIWGLSGLGAHSSDFKEREDAGKIIVSTS--- 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 166 leagserssgssgdDNFDIKQATYKNL-LSDKGGYIHGsrscgsAAMNMCLVATGKLDAYW--EGGCWAWDVCAGWCIVT 242
Cdd:cd01640  192 --------------HSHSVKEVQLITAgNKDEVLRAGG------AGYKVLQVLEGLADAYVhsTGGIKKWDICAPEAILR 251


                 ....
gi 255718083 243 ECGG 246
Cdd:cd01640  252 ALGG 255
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
9-252 1.63e-09

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 58.20  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   9 KDIETSLVDLASKEVGPLL-KEKAG--TQFDAFDDKANQVDLVTavdkkiEAIIKESLNKlYPDFKFVGEETyqpGTTEI 85
Cdd:PRK14076   6 LKIALKVAKEIEKKIKPLIgWEKAGevVKIGADGTPTKRIDLIA------ENIAINSLEK-FCSGILISEEI---GFKKI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  86 GKEP---TFIVDPIDGTTNFIHGYPYSCTSLGLVE-NGVPV----------------VGVVYNPHLNMMFHASKDNGARL 145
Cdd:PRK14076  76 GKNKpeyIFVLDPIDGTYNALKDIPIYSASIAIAKiDGFDKkikefigknltindleVGVVKNIATGDTYYAEKGEGAYL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083 146 --NGEPIKVPERDLT-LQQSIIALEAgserssgssgddnFDIKQATYKNLlsdKGGYIHGSRSCGSAAMNMCLVATGKLD 222
Cdd:PRK14076 156 lkKGEKKKIEISNISnLKDASIGLFA-------------YGLSLDTLKFI---KDRKVRRIRLFGSIALEMCYVASGALD 219

                        250       260       270
                 ....*....|....*....|....*....|..
gi 255718083 223 AYWE--GGCWAWDVCAGWCIVTECGGMVVGGN 252
Cdd:PRK14076 220 AFINvnETTRLCDIAAGYVICKEAGGIITNKN 251
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 2-261 2.77e-08

3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.


Pssm-ID: 273558 [Multi-domain]  Cd Length: 353  Bit Score: 54.10  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083    2 ALTKEqlKDIETSLVDLAS----KEVGPLLKEKAGTQFDAFDDKAnqvdlVTAVDKKIEAIIKESLNKLYPDFKFVGEET 77
Cdd:TIGR01330   1 ALERE--LDVATQAVRLASlltkKVQSELISHKDSTVITKDDKSP-----VTVGDYGAQAIVINVLKSNFPDDPIVGEED 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083   78 ---------------------------------YQP------------GTTEIGKEPTF-IVDPIDGTTNFIHGYPYScT 111
Cdd:TIGR01330  74 ssglseadftlgrvnelvnetlvyaknykkddqFPLksledvlqiidfGNYEGGRKGRHwVLDPIDGTKGFLRGDQYA-V 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  112 SLGLVENGVPVVGVVYNPHLNMMFHASKDNGARLNGEPIKVPERDL-TLQQSIIALEAGSERSSGSSGDDNFDIK----- 185
Cdd:TIGR01330 153 CLALIENGKVVLGVIGCPNLPLSSYGAQNLKGSESKGCIFRAVRGSgAFMYSLSSDAESPTKVHVSSVKDTKDAIfcegv 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255718083  186 ---------QATYKNLLSDKGGYIH-------GSRSCGSAAMNMCLVATGkldAYWEGgcwAWDVCAGWCIVTECGGMVV 249
Cdd:TIGR01330 233 ekghsshdeQTAIANKLGISKSPLRldsqakyAALARGDADVYLRLPIKL---SYQEK---IWDHAAGNVIVEEAGGIVT 306

                         330
                  ....*....|..
gi 255718083  250 ggnpNAWEVPVD 261
Cdd:TIGR01330 307 ----DAMGKPLD 314
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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