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Conserved domains on  [gi|61679846|pdb|1S2O|A]
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Chain A, sucrose-phosphatase

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPP_plant-cyano super family cl30869
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 3-243 4.95e-149

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


The actual alignment was detected with superfamily member TIGR01485:

Pssm-ID: 130549  Cd Length: 249  Bit Score: 415.37  E-value: 4.95e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          3 QLLLISDLDNTWV----GDQQALEHLQEYLGDRRGNF-YLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHP--E 75
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhtdGDNQALLRLNALLEDHRGEDsLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGgaE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         76 GLDQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSGKDVD 155
Cdd:TIGR01485  81 VPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTEMLKETGLDVKLIYSSGKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        156 LLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFET-SARGVIVRNAQPELLHWYDQWGDSRHYRAQSSHAGAIL 234
Cdd:TIGR01485 161 ILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIgSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGII 240


                  ....*....
1S2O_A        235 EAIAHFDFL 243
Cdd:TIGR01485 241 EAIAHFDLL 249
 
Name Accession Description Interval E-value
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 3-243 4.95e-149

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 415.37  E-value: 4.95e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          3 QLLLISDLDNTWV----GDQQALEHLQEYLGDRRGNF-YLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHP--E 75
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhtdGDNQALLRLNALLEDHRGEDsLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGgaE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         76 GLDQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSGKDVD 155
Cdd:TIGR01485  81 VPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTEMLKETGLDVKLIYSSGKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        156 LLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFET-SARGVIVRNAQPELLHWYDQWGDSRHYRAQSSHAGAIL 234
Cdd:TIGR01485 161 ILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIgSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGII 240


                  ....*....
1S2O_A        235 EAIAHFDFL 243
Cdd:TIGR01485 241 EAIAHFDLL 249
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 2-242 2.45e-119

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 340.01  E-value: 2.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          2 RQLLLISDLDNTWV-GDQQALEHLQEYLGDRRGNFYLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHPEGL--D 78
Cdd:pfam05116   1 PPLLLVSDLDNTLVdGDNEALARLNQLLEAYRPDVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGPSLvpD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         79 QHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSGKDVDLLP 158
Cdd:pfam05116  81 QSWQEHLDYHWDRQAVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLAELEQLLRKRGLDVKVIYSSGRDLDILP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        159 QRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDQWGDSRH--YRAQSSHAGAILEA 236
Cdd:pfam05116 161 LRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQWYLENARDNPriYFASGRCAGGILEG 240


                  ....*.
1S2O_A        237 IAHFDF 242
Cdd:pfam05116 241 IRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-240 1.17e-104

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 302.73  E-value: 1.17e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        5 LLISDLDNTWVGD---QQALEHLQEYLGDRR--GNFYLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHPEG--- 76
Cdd:cd02605   1 LLVSDLDETLVGHdtnLQALERLQDLLEQLTadNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYGESgyl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       77 -LDQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSG--KD 153
Cdd:cd02605  81 ePDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGlaYD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A      154 VDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDQWGDSRHyrAQSSHAGAI 233
Cdd:cd02605 161 LDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRL--AKGPYAGGI 238


                ....*..
1S2O_A      234 LEAIAHF 240
Cdd:cd02605 239 LEGLAHF 245
PLN02382 PLN02382
probable sucrose-phosphatase
 4-241 2.65e-62

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 200.60  E-value: 2.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         4 LLLISDLDNTWVgDQQALEHLQ----------EYlgdrRGNFYLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYH 73
Cdd:PLN02382  10 LMIVSDLDHTMV-DHHDPENLSllrfnalweaEY----RHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIAY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        74 PEGL--DQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSG 151
Cdd:PLN02382  85 GESMvpDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVDKKKAQEVIKELSERLEKRGLDVKIIYSGG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       152 KDVDLLPQRSNKGNATQYLQQHLAME---PSQTLVCGDSGNDIGLFET-SARGVIVRNAQPELLHWY-DQWGDSRH-YRA 225
Cdd:PLN02382 165 IDLDVLPQGAGKGQALAYLLKKLKAEgkaPVNTLVCGDSGNDAELFSVpDVYGVMVSNAQEELLQWYaENAKDNPKiIHA 244

                        250
                 ....*....|....*.
1S2O_A       226 QSSHAGAILEAIAHFD 241
Cdd:PLN02382 245 TERCAAGIIQAIGHFN 260
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 5-240 8.97e-38

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 130.64  E-value: 8.97e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        5 LLISDLDNTWVGDQ--------QALEHLQEylgdrRGnFYLAYATGRSYHSARELQKQVGLmePDYWLTAVGSEIYHPEG 76
Cdd:COG0561   4 LIALDLDGTLLNDDgeisprtkEALRRLRE-----KG-IKVVIATGRPLRSALPLLEELGL--DDPLITSNGALIYDPDG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       77 ldqhwadylsehwqrdilqaiadgfealkpqSPLEQNPwkisyhLDPQacptVIDQLTEMLKETGIPVQVIFSSGKD-VD 155
Cdd:COG0561  76 -------------------------------EVLYERP------LDPE----DVREILELLREHGLHLQVVVRSGPGfLE 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A      156 LLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDqwgdsrhYRAQSSHAGAILE 235
Cdd:COG0561 115 ILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAAD-------YVTGSNDEDGVAE 187


                ....*
1S2O_A      236 AIAHF 240
Cdd:COG0561 188 ALEKL 192
 
Name Accession Description Interval E-value
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 3-243 4.95e-149

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 415.37  E-value: 4.95e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          3 QLLLISDLDNTWV----GDQQALEHLQEYLGDRRGNF-YLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHP--E 75
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhtdGDNQALLRLNALLEDHRGEDsLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGgaE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         76 GLDQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSGKDVD 155
Cdd:TIGR01485  81 VPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTEMLKETGLDVKLIYSSGKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        156 LLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFET-SARGVIVRNAQPELLHWYDQWGDSRHYRAQSSHAGAIL 234
Cdd:TIGR01485 161 ILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIgSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGII 240


                  ....*....
1S2O_A        235 EAIAHFDFL 243
Cdd:TIGR01485 241 EAIAHFDLL 249
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 2-242 2.45e-119

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 340.01  E-value: 2.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          2 RQLLLISDLDNTWV-GDQQALEHLQEYLGDRRGNFYLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHPEGL--D 78
Cdd:pfam05116   1 PPLLLVSDLDNTLVdGDNEALARLNQLLEAYRPDVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGPSLvpD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         79 QHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSGKDVDLLP 158
Cdd:pfam05116  81 QSWQEHLDYHWDRQAVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLAELEQLLRKRGLDVKVIYSSGRDLDILP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        159 QRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDQWGDSRH--YRAQSSHAGAILEA 236
Cdd:pfam05116 161 LRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQWYLENARDNPriYFASGRCAGGILEG 240


                  ....*.
1S2O_A        237 IAHFDF 242
Cdd:pfam05116 241 IRHFGL 246
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-238 9.89e-115

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 327.50  E-value: 9.89e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          6 LISDLDNTWVGDQQALEHLQEYLGDRRGNFY--LAYATGRSYHSARELQKQVGlmEPDYWLTAVGSEIYHPEGLDQHWAD 83
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGipVVLVTGNSVQFARALAKLIG--TPDPVIAENGGEISYNEGLDDIFLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         84 YLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETgipvqvifSSGKDVDLLPQRSNK 163
Cdd:TIGR01482  79 YLEEEWFLDIVIAKTFPFSRLKVQYPRRASLVKMRYGIDVDTVREIIKELGLNLVAV--------DSGFDIHILPQGVNK 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1S2O_A        164 GNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDQWGDSRHYRAQSSHAGAILEAIA 238
Cdd:TIGR01482 151 GVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADYVTESPYGEGGAEAIGEILQAIG 225
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-240 1.17e-104

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 302.73  E-value: 1.17e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        5 LLISDLDNTWVGD---QQALEHLQEYLGDRR--GNFYLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHPEG--- 76
Cdd:cd02605   1 LLVSDLDETLVGHdtnLQALERLQDLLEQLTadNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYGESgyl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       77 -LDQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSG--KD 153
Cdd:cd02605  81 ePDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGlaYD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A      154 VDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDQWGDSRHyrAQSSHAGAI 233
Cdd:cd02605 161 LDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRL--AKGPYAGGI 238


                ....*..
1S2O_A      234 LEAIAHF 240
Cdd:cd02605 239 LEGLAHF 245
PLN02382 PLN02382
probable sucrose-phosphatase
 4-241 2.65e-62

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 200.60  E-value: 2.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         4 LLLISDLDNTWVgDQQALEHLQ----------EYlgdrRGNFYLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYH 73
Cdd:PLN02382  10 LMIVSDLDHTMV-DHHDPENLSllrfnalweaEY----RHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIAY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        74 PEGL--DQHWADYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSSG 151
Cdd:PLN02382  85 GESMvpDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVDKKKAQEVIKELSERLEKRGLDVKIIYSGG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       152 KDVDLLPQRSNKGNATQYLQQHLAME---PSQTLVCGDSGNDIGLFET-SARGVIVRNAQPELLHWY-DQWGDSRH-YRA 225
Cdd:PLN02382 165 IDLDVLPQGAGKGQALAYLLKKLKAEgkaPVNTLVCGDSGNDAELFSVpDVYGVMVSNAQEELLQWYaENAKDNPKiIHA 244

                        250
                 ....*....|....*.
1S2O_A       226 QSSHAGAILEAIAHFD 241
Cdd:PLN02382 245 TERCAAGIIQAIGHFN 260
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 5-242 6.44e-51

sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472.


Pssm-ID: 131524  Cd Length: 236  Bit Score: 165.71  E-value: 6.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          5 LLISDLDNTWVGDQQALEHLQEYLGDRRGNFYLAYATGRSYHSARELQKQVGLMEPDYWLTAVGSEIYHPEGL--DQHWA 82
Cdd:TIGR02471   1 LIITDLDNTLLGDDEGLASFVELLRGSGDAVGFGIATGRSVESAKSRYAKLNLPSPDVLIARVGTEIYYGPELqpDRFWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         83 DYLSEHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTViDQLTEMLKETGIPVQVIFSSGKDVDLLPQRSN 162
Cdd:TIGR02471  81 KHIDHDWRRQAVVEALADIPGLTLQDDQEQGPFKISYLLDPEGEPIL-PQIRQRLRQQSQAAKVILSCGWFLDVLPLRAS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        163 KGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDQwgdSRHYRAQSSHAGAILEAIAHFDF 242
Cdd:TIGR02471 160 KGLALRYLSYRWGLPLEQILVAGDSGNDEEMLRGLTLGVVVGNHDPELEGLRHQ---QRIYFANNPHAFGILEGINHYDF 236
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 5-240 8.97e-38

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 130.64  E-value: 8.97e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        5 LLISDLDNTWVGDQ--------QALEHLQEylgdrRGnFYLAYATGRSYHSARELQKQVGLmePDYWLTAVGSEIYHPEG 76
Cdd:COG0561   4 LIALDLDGTLLNDDgeisprtkEALRRLRE-----KG-IKVVIATGRPLRSALPLLEELGL--DDPLITSNGALIYDPDG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       77 ldqhwadylsehwqrdilqaiadgfealkpqSPLEQNPwkisyhLDPQacptVIDQLTEMLKETGIPVQVIFSSGKD-VD 155
Cdd:COG0561  76 -------------------------------EVLYERP------LDPE----DVREILELLREHGLHLQVVVRSGPGfLE 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A      156 LLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDqwgdsrhYRAQSSHAGAILE 235
Cdd:COG0561 115 ILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAAD-------YVTGSNDEDGVAE 187


                ....*
1S2O_A      236 AIAHF 240
Cdd:COG0561 188 ALEKL 192
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-211 5.98e-21

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 88.45  E-value: 5.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          6 LISDLDNTWVGD--------QQALEHLQEylgdrrGNFYLAYATGRSYHSARELQKQVGLmePDYWLTAVGSEIYHPEG- 76
Cdd:pfam08282   1 IASDLDGTLLNSdkkisektKEAIKKLKE------KGIKFVIATGRPYRAILPVIKELGL--DDPVICYNGALIYDENGk 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         77 ------LD----QHWADYLSEHwQRDILQAIADG-----------------------FEALKPQSPLEQNPWKISYHLDP 123
Cdd:pfam08282  73 ilysnpISkeavKEIIEYLKEN-NLEILLYTDDGvyilndnelekilkelnytksfvPEIDDFELLEDEDINKILILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        124 QacptVIDQLTEMLKETGIPVQVIFSSGKD-VDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVI 202
Cdd:pfam08282 152 E----DLDELEKELKELFGSLITITSSGPGyLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVA 227


                  ....*....
1S2O_A        203 VRNAQPELL 211
Cdd:pfam08282 228 MGNASPEVK 236
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-203 5.60e-20

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 84.74  E-value: 5.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          5 LLISDLDNTWVGDQ------QALEHLQEYlgdRRGNFYLAYATGRSYHSARELQKQVGLmePDYWLTAVGSEIYHPEGld 78
Cdd:TIGR01484   1 LLFFDLDGTLLDPNahelspETIEALERL---REAGVKVVIVTGRSLAEIKELLKQLNL--PLPLIAENGALIFYPGE-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         79 QHWADYLS-----EHWQRDILQAIADGFEALKPQSPLEQNPWKISYHLDPQACPTVIDQ-LTEMLKETGIP---VQVIFS 149
Cdd:TIGR01484  74 ILYIEPSDvfeeiLGIKFEEIGAELKSLSEHYVGTFIEDKAIAVAIHYVGAELGQELDSkMRERLEKIGRNdleLEAIYS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
1S2O_A        150 SGKDVDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIV 203
Cdd:TIGR01484 154 GKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-210 2.89e-17

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 78.46  E-value: 2.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A          5 LLISDLDNTWVGD--------QQALEHLQEylgdrRG-NFYLAyaTGRSYHSARELQKQVGLmePDYWLTAVGSEIYHPE 75
Cdd:TIGR00099   1 LIFIDLDGTLLNDdhtispstKEALAKLRE-----KGiKVVLA--TGRPYKEVKNILKELGL--DTPFITANGAAVIDDQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A         76 G-------LDQHWADYLSEHWQRDILQAIADG----------------FEALKPQSPLEQNPWKISYH---------LDP 123
Cdd:TIGR00099  72 GeilykkpLDLDLVEEILNFLKKHGLDVILYGddsiyaskndpeyftiFKKFLGEPKLEVVDIQYLPDdilkilllfLDP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        124 QACPTVIDQLTEMLKETGIPVQviFSSGKDVDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIV 203
Cdd:TIGR00099 152 EDLDLLIEALNKLELEENVSVV--SSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAM 229


                  ....*..
1S2O_A        204 RNAQPEL 210
Cdd:TIGR00099 230 GNADEEL 236
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 116-211 3.99e-16

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 73.77  E-value: 3.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A      116 KISYHLDPQACPTVIDQLTEMLKETgipvQVIFSSGKD-VDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLF 194
Cdd:cd07518  72 KFTLNVPDEAAPDIIDELNQKFGGI----LRAVTSGFGsIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEML 147

                        90
                ....*....|....*..
1S2O_A      195 ETSARGVIVRNAQPELL 211
Cdd:cd07518 148 KYAGYSYAMENAPEEVK 164
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-210 8.83e-16

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 74.17  E-value: 8.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        5 LLISDLDNTWVGDQ--------QALEHLQEylgdrRGnFYLAYATGRSYHSARELQKQVGLmePDYWLTAVGSEIYHPEG 76
Cdd:cd07516   1 LIALDLDGTLLNSDkeisprtkEAIKKAKE-----KG-IKVVIATGRPLRGAQPYLEELGL--DSPLITFNGALVYDPTG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       77 ------------------------------LDQHWADYL-SEHWQRDILQAIADGFEALKPQSpleQNPWKISYHLDPQA 125
Cdd:cd07516  73 keilerliskedvkeleeflrklgiginiyTNDDWADTIyEENEDDEIIKPAEILDDLLLPPD---EDITKILFVGEDEE 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A      126 cptVIDQLTEMLKETGIPVQVIFSSGKDVDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRN 205
Cdd:cd07516 150 ---LDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGN 226


                ....*
1S2O_A      206 AQPEL 210
Cdd:cd07516 227 AIDEV 231
PRK15126 PRK15126
HMP-PP phosphatase;
37-210 7.54e-10

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 57.78  E-value: 7.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        37 LAYATGRSYHSARELQKQVGLmePDYWLTAVGSEIYHPEG----------------LDQHWADYLSEHWQRD-------- 92
Cdd:PRK15126  38 LTFATGRHVLEMQHILGALSL--DAYLITGNGTRVHSLEGellhrqdlpadvaelvLHQQWDTRASMHVFNDdgwftgke 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        93 ---ILQA-IADGFE----ALKpQSPLEQNPwKISYHLDPQACPTVIDQLTEMLketGIPVQVIFSSGKDVDLLPQRSNKG 164
Cdd:PRK15126 116 ipaLLQAhVYSGFRyqliDLK-RLPAHGVT-KICFCGDHDDLTRLQIQLNEAL---GERAHLCFSATDCLEVLPVGCNKG 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
1S2O_A       165 NATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPEL 210
Cdd:PRK15126 191 AALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNAMPQL 236
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 130-242 2.23e-09

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 55.75  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       130 IDQLTEMLKETGIPVqVIFSSGKDVDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPE 209
Cdd:PRK01158 126 VEEVRELLEELGLDL-EIVDSGFAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEE 204

                         90       100       110
                 ....*....|....*....|....*....|...
1S2O_A       210 LLHWYDqwgdsrhYRAQSSHAGAILEAIAHFDF 242
Cdd:PRK01158 205 LKEAAD-------YVTEKSYGEGVAEAIEHLLL 230
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 130-210 2.08e-08

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 52.82  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        130 IDQLTEMLKETGIpvqVIFSSGKDVDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPE 209
Cdd:TIGR01487 118 VDEVREIIKERGL---NLVASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQ 194


                  .
1S2O_A        210 L 210
Cdd:TIGR01487 195 L 195
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 162-240 3.01e-08

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 51.05  E-value: 3.01e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1S2O_A      162 NKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDqwgdsrhYRAQSSHAGAILEAIAHF 240
Cdd:cd07514  67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAAD-------YVTDASYGDGVLEAIDKL 138
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 153-210 8.26e-08

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 51.07  E-value: 8.26e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
1S2O_A      153 DVDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPEL 210
Cdd:cd07517 132 STDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEEL 189
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 155-211 1.99e-05

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 44.68  E-value: 1.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
1S2O_A       155 DLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELL 211
Cdd:PRK10513 189 EILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVK 245
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 161-237 3.61e-05

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 43.78  E-value: 3.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1S2O_A       161 SNKGNATQYLQQHLA-MEPSQTLVCGDSGNDIGLFETSARGVIVRNAQPELLHWYDQWGDSRHYRAQSSHAGAILEAI 237
Cdd:PRK00192 189 GDKGKAVRWLKELYRrQDGVETIALGDSPNDLPMLEAADIAVVVPGPDGPNPPLLPGIADGEFILASAPGPEGWAEAI 266
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 5-186 3.08e-04

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 40.74  E-value: 3.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A        5 LLISDLDNT---WVGDQQALEHLQEY------LGDRRGNFyLAYATGRSyhsARELQKQVGLmePDYWLTAV-GSEIYHP 74
Cdd:cd01627   1 LLFLDYDGTlapIVPDPDAAVPSPELlealkkLAADPKNA-VAIVSGRD---LDDLDKWLGL--PGIGLAGEhGAEIRLP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A       75 EGldQHWaDYLSEH----WQRDILqAIADGFEALKPQSPLEQNPWKISYHL---DPQACPTVIDQLtEMLKETGIPVQVI 147
Cdd:cd01627  75 GG--GEW-VTLAPKadleWKEEVE-AIFKYFTERTPGSLVEDKGASLAWHYrnaDPEGARAALELA-LHLASDLLKALEV 149

                       170       180       190
                ....*....|....*....|....*....|....*....
1S2O_A      148 FSSGKDVDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGD 186
Cdd:cd01627 150 VPGKKVVEVRPVGVNKGEAVERILGELPFAGDFVLCAGD 188
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 135-211 3.15e-04

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 39.81  E-value: 3.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1S2O_A      135 EMLKETGIPVQVIfsSGKDVDLLPQR-------------SNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGV 201
Cdd:cd01630  38 KLLQKSGIEVAII--TGRQSEAVRRRakelgiedlfqgvKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSV 115

                        90
                ....*....|
1S2O_A      202 IVRNAQPELL 211
Cdd:cd01630 116 APADAHPEVR 125
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-76 1.91e-03

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 36.99  E-value: 1.91e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1S2O_A        5 LLISDLDNTWVgdqqALEHLQEYlgdRRGNFYLAYATGRSYHSARELQKQVGLME-PDYWLTAVGSEIYHPEG 76
Cdd:cd01427   1 AVLFDLDGTLL----AVELLKRL---RAAGIKLAIVTNRSREALRALLEKLGLGDlFDGIIGSDGGGTPKPKP 66
PLN02887 PLN02887
hydrolase family protein
 154-205 2.82e-03

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 38.70  E-value: 2.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
1S2O_A       154 VDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARGVIVRN 205
Cdd:PLN02887 499 LEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSN 550
 
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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