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Conserved domains on  [gi|16605555|emb|CAC87815|]
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putative sucrose-phosphate phosphatase [Nostoc punctiforme PCC 73102]

Protein Classification

SPP_plant-cyano family protein( domain architecture ID 11492701)

SPP_plant-cyano family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 3-252 4.91e-159

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: 441.17  E-value: 4.91e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     3 PFLFVTDLDDTLVYRTTGDDSALPELNQLLKRHRQEYGtKIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNGA 82
Cdd:TIGR01485   1 RLLLVSDLDNTLVDHTDGDNQALLRLNALLEDHRGEDS-LLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    83 DTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSGIDL 162
Cdd:TIGR01485  80 EVPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTEMLKETGLDVKLIYSSGKDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   163 DIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGNERGIIVGNARKELLQWHNEHPAEHRYLASCFCAGGI 242
Cdd:TIGR01485 160 DILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGI 239

                         250
                  ....*....|
gi 16605555   243 IEGLNYFGLL 252
Cdd:TIGR01485 240 IEAIAHFDLL 249
 
Name Accession Description Interval E-value
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 3-252 4.91e-159

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: 441.17  E-value: 4.91e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     3 PFLFVTDLDDTLVYRTTGDDSALPELNQLLKRHRQEYGtKIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNGA 82
Cdd:TIGR01485   1 RLLLVSDLDNTLVDHTDGDNQALLRLNALLEDHRGEDS-LLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    83 DTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSGIDL 162
Cdd:TIGR01485  80 EVPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTEMLKETGLDVKLIYSSGKDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   163 DIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGNERGIIVGNARKELLQWHNEHPAEHRYLASCFCAGGI 242
Cdd:TIGR01485 160 DILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGI 239

                         250
                  ....*....|
gi 16605555   243 IEGLNYFGLL 252
Cdd:TIGR01485 240 IEAIAHFDLL 249
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 2-251 1.38e-123

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: 351.18  E-value: 1.38e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     2 KPFLFVTDLDDTLVYrttGDDSALPELNQLLKRHRQEYGtkIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNG 81
Cdd:pfam05116   1 PPLLLVSDLDNTLVD---GDNEALARLNQLLEAYRPDVG--LVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    82 ADTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSGID 161
Cdd:pfam05116  76 SLVPDQSWQEHLDYHWDRQAVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLAELEQLLRKRGLDVKVIYSSGRD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   162 LDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFaVGNERGIIVGNARKELLQWHNEHPAEHR--YLASCFCA 239
Cdd:pfam05116 156 LDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELF-IGGTRGVVVGNAQPELLQWYLENARDNPriYFASGRCA 234

                         250
                  ....*....|..
gi 16605555   240 GGIIEGLNYFGL 251
Cdd:pfam05116 235 GGILEGIRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-249 1.45e-93

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: 275.00  E-value: 1.45e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   5 LFVTDLDDTLVyRTTGDDSALPELNQLLKRHRQEYGTKIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYL--NGA 82
Cdd:cd02605   1 LLVSDLDETLV-GHDTNLQALERLQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYgeSGY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  83 DTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSG--I 160
Cdd:cd02605  80 LEPDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGlaY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 161 DLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGnERGIIVGNARKELLQWHNEHPAEHryLASCFCAG 240
Cdd:cd02605 160 DLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTG-TRGVIVGNAQPELLKWADRVTRSR--LAKGPYAG 236


                ....*....
gi 16605555 241 GIIEGLNYF 249
Cdd:cd02605 237 GILEGLAHF 245
PLN02382 PLN02382
probable sucrose-phosphatase
 5-251 3.65e-84

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 256.84  E-value: 3.65e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    5 LFVTDLDDTLVYRTTGDDSALPELNQLLKRH-RQEygTKIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNGAD 83
Cdd:PLN02382  11 MIVSDLDHTMVDHHDPENLSLLRFNALWEAEyRHD--SLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIAYGESM 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   84 TPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSGIDLD 163
Cdd:PLN02382  89 VPDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVDKKKAQEVIKELSERLEKRGLDVKIIYSGGIDLD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  164 IVPHSSDKGQAMQFLRQKWKF---AAEQTVVCGDSGNDIALFAVGNERGIIVGNARKELLQWHNEHPAE--HRYLASCFC 238
Cdd:PLN02382 169 VLPQGAGKGQALAYLLKKLKAegkAPVNTLVCGDSGNDAELFSVPDVYGVMVSNAQEELLQWYAENAKDnpKIIHATERC 248

                        250
                 ....*....|...
gi 16605555  239 AGGIIEGLNYFGL 251
Cdd:PLN02382 249 AAGIIQAIGHFNL 261
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 5-249 1.64e-30

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: 112.15  E-value: 1.64e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   5 LFVTDLDDTLVyrttGDDSALPELN-QLLKRHRQEyGTKIVYSTGRSPVLYKELQAQKNLlqPDALVLSVGTEIYlngad 83
Cdd:COG0561   4 LIALDLDGTLL----NDDGEISPRTkEALRRLREK-GIKVVIATGRPLRSALPLLEELGL--DDPLITSNGALIY----- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  84 tpDSDWSEILSPGWEREVVLSITRKYRELvrqpdseqrafkvsffleqeasaNVLPQLeaelqksklnvkLIYSSGIDLD 163
Cdd:COG0561  72 --DPDGEVLYERPLDPEDVREILELLREH-----------------------GLHLQV------------VVRSGPGFLE 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 164 IVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALF-AVGneRGIIVGNARKELLQWHNehpaehrYLASCFCAGGI 242
Cdd:COG0561 115 ILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLeAAG--LGVAMGNAPPEVKAAAD-------YVTGSNDEDGV 185


                ....*..
gi 16605555 243 IEGLNYF 249
Cdd:COG0561 186 AEALEKL 192
 
Name Accession Description Interval E-value
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 3-252 4.91e-159

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: 441.17  E-value: 4.91e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     3 PFLFVTDLDDTLVYRTTGDDSALPELNQLLKRHRQEYGtKIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNGA 82
Cdd:TIGR01485   1 RLLLVSDLDNTLVDHTDGDNQALLRLNALLEDHRGEDS-LLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    83 DTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSGIDL 162
Cdd:TIGR01485  80 EVPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTEMLKETGLDVKLIYSSGKDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   163 DIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGNERGIIVGNARKELLQWHNEHPAEHRYLASCFCAGGI 242
Cdd:TIGR01485 160 DILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGI 239

                         250
                  ....*....|
gi 16605555   243 IEGLNYFGLL 252
Cdd:TIGR01485 240 IEAIAHFDLL 249
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 2-251 1.38e-123

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: 351.18  E-value: 1.38e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     2 KPFLFVTDLDDTLVYrttGDDSALPELNQLLKRHRQEYGtkIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNG 81
Cdd:pfam05116   1 PPLLLVSDLDNTLVD---GDNEALARLNQLLEAYRPDVG--LVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    82 ADTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSGID 161
Cdd:pfam05116  76 SLVPDQSWQEHLDYHWDRQAVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLAELEQLLRKRGLDVKVIYSSGRD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   162 LDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFaVGNERGIIVGNARKELLQWHNEHPAEHR--YLASCFCA 239
Cdd:pfam05116 156 LDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELF-IGGTRGVVVGNAQPELLQWYLENARDNPriYFASGRCA 234

                         250
                  ....*....|..
gi 16605555   240 GGIIEGLNYFGL 251
Cdd:pfam05116 235 GGILEGIRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-249 1.45e-93

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: 275.00  E-value: 1.45e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   5 LFVTDLDDTLVyRTTGDDSALPELNQLLKRHRQEYGTKIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYL--NGA 82
Cdd:cd02605   1 LLVSDLDETLV-GHDTNLQALERLQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYgeSGY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  83 DTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSG--I 160
Cdd:cd02605  80 LEPDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGlaY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 161 DLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGnERGIIVGNARKELLQWHNEHPAEHryLASCFCAG 240
Cdd:cd02605 160 DLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTG-TRGVIVGNAQPELLKWADRVTRSR--LAKGPYAG 236


                ....*....
gi 16605555 241 GIIEGLNYF 249
Cdd:cd02605 237 GILEGLAHF 245
PLN02382 PLN02382
probable sucrose-phosphatase
 5-251 3.65e-84

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 256.84  E-value: 3.65e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    5 LFVTDLDDTLVYRTTGDDSALPELNQLLKRH-RQEygTKIVYSTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNGAD 83
Cdd:PLN02382  11 MIVSDLDHTMVDHHDPENLSLLRFNALWEAEyRHD--SLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIAYGESM 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   84 TPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSKLNVKLIYSSGIDLD 163
Cdd:PLN02382  89 VPDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVDKKKAQEVIKELSERLEKRGLDVKIIYSGGIDLD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  164 IVPHSSDKGQAMQFLRQKWKF---AAEQTVVCGDSGNDIALFAVGNERGIIVGNARKELLQWHNEHPAE--HRYLASCFC 238
Cdd:PLN02382 169 VLPQGAGKGQALAYLLKKLKAegkAPVNTLVCGDSGNDAELFSVPDVYGVMVSNAQEELLQWYAENAKDnpKIIHATERC 248

                        250
                 ....*....|...
gi 16605555  239 AGGIIEGLNYFGL 251
Cdd:PLN02382 249 AAGIIQAIGHFNL 261
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 5-249 7.49e-47

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: 155.69  E-value: 7.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     5 LFVTDLDDTLvyrtTGDDSALPELNQLLKRHRQEYGTKIvySTGRSPVLYKELQAQKNLLQPDALVLSVGTEIYLNGADT 84
Cdd:TIGR02471   1 LIITDLDNTL----LGDDEGLASFVELLRGSGDAVGFGI--ATGRSVESAKSRYAKLNLPSPDVLIARVGTEIYYGPELQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    85 PDSDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASAnVLPQLEAELQKSKLNVKLIYSSGIDLDI 164
Cdd:TIGR02471  75 PDRFWQKHIDHDWRRQAVVEALADIPGLTLQDDQEQGPFKISYLLDPEGEP-ILPQIRQRLRQQSQAAKVILSCGWFLDV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   165 VPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFaVGNERGIIVGNARKELLQWHNEhpaEHRYLASCFCAGGIIE 244
Cdd:TIGR02471 154 LPLRASKGLALRYLSYRWGLPLEQILVAGDSGNDEEML-RGLTLGVVVGNHDPELEGLRHQ---QRIYFANNPHAFGILE 229


                  ....*
gi 16605555   245 GLNYF 249
Cdd:TIGR02471 230 GINHY 234
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 7-247 1.28e-41

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: 141.83  E-value: 1.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     7 VTDLDDTLVYrttgDDSALPELNQLLKRHRQEYGTKIVYSTGRSPVLYKELQAQKNllQPDALVLSVGTEIYLNgaDTPD 86
Cdd:TIGR01482   2 ASDIDGTLTD----PNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIG--TPDPVIAENGGEISYN--EGLD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    87 SDWSEILSPGWEREVVLSITRKYRELVRQPDSEQRAFKVSFFLEQEASANVLPQLEAELQKSklnvkliySSGIDLDIVP 166
Cdd:TIGR01482  74 DIFLAYLEEEWFLDIVIAKTFPFSRLKVQYPRRASLVKMRYGIDVDTVREIIKELGLNLVAV--------DSGFDIHILP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   167 HSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGNeRGIIVGNARKELLQWHNEHPAEHRYLASCFCAGGIIEGL 246
Cdd:TIGR01482 146 QGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPG-FGVAVANAQPELKEWADYVTESPYGEGGAEAIGEILQAI 224


                  .
gi 16605555   247 N 247
Cdd:TIGR01482 225 G 225
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 5-249 1.64e-30

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: 112.15  E-value: 1.64e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   5 LFVTDLDDTLVyrttGDDSALPELN-QLLKRHRQEyGTKIVYSTGRSPVLYKELQAQKNLlqPDALVLSVGTEIYlngad 83
Cdd:COG0561   4 LIALDLDGTLL----NDDGEISPRTkEALRRLREK-GIKVVIATGRPLRSALPLLEELGL--DDPLITSNGALIY----- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  84 tpDSDWSEILSPGWEREVVLSITRKYRELvrqpdseqrafkvsffleqeasaNVLPQLeaelqksklnvkLIYSSGIDLD 163
Cdd:COG0561  72 --DPDGEVLYERPLDPEDVREILELLREH-----------------------GLHLQV------------VVRSGPGFLE 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 164 IVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALF-AVGneRGIIVGNARKELLQWHNehpaehrYLASCFCAGGI 242
Cdd:COG0561 115 ILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLeAAG--LGVAMGNAPPEVKAAAD-------YVTGSNDEDGV 185


                ....*..
gi 16605555 243 IEGLNYF 249
Cdd:COG0561 186 AEALEKL 192
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-211 4.14e-28

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: 106.31  E-value: 4.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     5 LFVTDLDDTLVyrTTGDDSALPELNQLLKRHRQEyGTKIVYSTGRSP----VLYKELQAQKNLLQPDALVLSVGTEIYLN 80
Cdd:TIGR01484   1 LLFFDLDGTLL--DPNAHELSPETIEALERLREA-GVKVVIVTGRSLaeikELLKQLNLPLPLIAENGALIFYPGEILYI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    81 gadTPDSDWSEILSPGWERevVLSITRKYRELVRQPDSEQRAFKVSF-FLEQEASANVLPQLEAELQKSKLN---VKLIY 156
Cdd:TIGR01484  78 ---EPSDVFEEILGIKFEE--IGAELKSLSEHYVGTFIEDKAIAVAIhYVGAELGQELDSKMRERLEKIGRNdleLEAIY 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16605555   157 SSGIDLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGNERGII 211
Cdd:TIGR01484 153 SGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-226 3.42e-19

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: 83.86  E-value: 3.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     5 LFVTDLDDTLVyrttGDDSALPELN-QLLKRHRQEyGTKIVYSTGRSPVLYKELQAQKNLLQP-----DALVLSVGTEI- 77
Cdd:TIGR00099   1 LIFIDLDGTLL----NDDHTISPSTkEALAKLREK-GIKVVLATGRPYKEVKNILKELGLDTPfitanGAAVIDDQGEIl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    78 ---YLNGADTP---------------DSDWSE-ILSPGWEREVVLSITRKYRELVRQP---DSEQRAFKVSFFLEQEasa 135
Cdd:TIGR00099  76 ykkPLDLDLVEeilnflkkhgldvilYGDDSIyASKNDPEYFTIFKKFLGEPKLEVVDiqyLPDDILKILLLFLDPE--- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   136 nVLPQLEAELQKS--KLNVKLIYSSGIDLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALF-AVGneRGIIV 212
Cdd:TIGR00099 153 -DLDLLIEALNKLelEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLeAAG--YGVAM 229

                         250
                  ....*....|....
gi 16605555   213 GNARKELLQWHNEH 226
Cdd:TIGR00099 230 GNADEELKALADYV 243
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-221 3.26e-15

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 72.66  E-value: 3.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555     6 FVTDLDDTLVyrttGDDSALPELNQ-LLKRHRQEyGTKIVYSTGRSPV----LYKELQaqknllqpdaLVLSVgteIYLN 80
Cdd:pfam08282   1 IASDLDGTLL----NSDKKISEKTKeAIKKLKEK-GIKFVIATGRPYRailpVIKELG----------LDDPV---ICYN 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    81 GADTPDSDWSEILSPGWEREVVLSITRKYREL-----------------VRQPDSEQRAFKVSFFLEQEASANVLP---- 139
Cdd:pfam08282  63 GALIYDENGKILYSNPISKEAVKEIIEYLKENnleillytddgvyilndNELEKILKELNYTKSFVPEIDDFELLEdedi 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   140 -------------QLEAELQKSKLNVKLIYSSGID-LDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALF-AV 204
Cdd:pfam08282 143 nkililldeedldELEKELKELFGSLITITSSGPGyLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLeAA 222

                         250
                  ....*....|....*..
gi 16605555   205 GNerGIIVGNARKELLQ 221
Cdd:pfam08282 223 GL--GVAMGNASPEVKA 237
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-226 7.72e-13

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: 66.08  E-value: 7.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   5 LFVTDLDDTLVYrttgDDSALPELN-QLLKRHRQEyGTKIVYSTGRSPV----LYKELQ----------------AQKNL 63
Cdd:cd07516   1 LIALDLDGTLLN----SDKEISPRTkEAIKKAKEK-GIKVVIATGRPLRgaqpYLEELGldsplitfngalvydpTGKEI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  64 LQP-----DALVL-------SVGTEIYlngadTPDSDWSEILSPGWEREVVLSITRKYRELVRQPDSeqrAFKVSFFLEQ 131
Cdd:cd07516  76 LERliskeDVKELeeflrklGIGINIY-----TNDDWADTIYEENEDDEIIKPAEILDDLLLPPDED---ITKILFVGED 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 132 EASANVLPQLEAELqKSKLNVklIYSSGIDLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALF-AVGNerGI 210
Cdd:cd07516 148 EELDELIAKLPEEF-FDDLSV--VRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLeYAGL--GV 222

                       250       260
                ....*....|....*....|..
gi 16605555 211 IVGNAR---KELLQW---HNEH 226
Cdd:cd07516 223 AMGNAIdevKEAADYvtlTNNE 244
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 123-206 5.75e-12

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: 62.60  E-value: 5.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 123 FKVSFFLEQEASANVLPQLEAELQKsklNVKLIYSSGIDLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIAL- 201
Cdd:cd07518  71 FKFTLNVPDEAAPDIIDELNQKFGG---ILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMl 147

                        90
                ....*....|.
gi 16605555 202 ------FAVGN 206
Cdd:cd07518 148 kyagysYAMEN 158
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 9-250 1.68e-10

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: 58.77  E-value: 1.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   9 DLDDTLVYRTTG-DDSALPELNQLlkrhrQEYGTKIVYSTGRSPVlykELQAQKNLLQPDALVLSVGTEIYLNGadtpds 87
Cdd:cd07517   6 DIDGTLLDEDTTiPESTKEAIAAL-----KEKGILVVIATGRAPF---EIQPIVKALGIDSYVSYNGQYVFFEG------ 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  88 dwsEILspgweREVVLSiTRKYRELVRQPDSEQRAfkVSFFLEQEASANvlPQLEAELQKSKLNVKLIYSSGIDLDIVPH 167
Cdd:cd07517  72 ---EVI-----YKNPLP-QELVERLTEFAKEQGHP--VSFYGQLLLFED--EEEEQKYEELRPELRFVRWHPLSTDVIPK 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 168 SSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALF-AVGNerGIIVGNARKELLQwhnehpaehryLASCFCA----GGI 242
Cdd:cd07517 139 GGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLeAVGI--GIAMGNAHEELKE-----------IADYVTKdvdeDGI 205


                ....*...
gi 16605555 243 IEGLNYFG 250
Cdd:cd07517 206 LKALKHFG 213
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-215 9.46e-08

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 51.48  E-value: 9.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555    1 MKPFLFVTDLDDTLVYRTTGD-DSALPELNQLlkrhrQEYGTKIVYSTG--RSPVLYkeLQAQKNLlqPDALVLSVGTEI 77
Cdd:PRK00192   2 MMKLLVFTDLDGTLLDHHTYSyEPAKPALKAL-----KEKGIPVIPCTSktAAEVEV--LRKELGL--EDPFIVENGAAI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   78 YL---------NGADTPDSDWSEILSPGWE--REVVLSITRKYR------------ELVR----QPDS----EQRAFKVS 126
Cdd:PRK00192  73 YIpknyfpfqpDGERLKGDYWVIELGPPYEelREILDEISDELGyplkgfgdlsaeEVAEltglSGESarlaKDREFSEP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  127 FFLEQeaSANVLPQLEAELQKSKLNV----KLIYSSGidldivphSSDKGQAMQFLRQKWKFAAE-QTVVCGDSGNDIAL 201
Cdd:PRK00192 153 FLWNG--SEAAKERFEEALKRLGLKVtrggRFLHLLG--------GGDKGKAVRWLKELYRRQDGvETIALGDSPNDLPM 222

                        250
                 ....*....|....
gi 16605555  202 FAVGNeRGIIVGNA 215
Cdd:PRK00192 223 LEAAD-IAVVVPGP 235
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 149-219 5.70e-06

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: 45.89  E-value: 5.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16605555   149 KLNVKLIYSsGIDLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGNERgIIVGNARKEL 219
Cdd:TIGR01487 127 ERGLNLVAS-GFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFK-VAVANADDQL 195
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 5-218 6.37e-06

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. 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: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 46.20  E-value: 6.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   5 LFVTDLDDTLVYRTTGD-DSALPELNQLlkrhrQEYGTKIVYSTGRSpvlYKELQA-QKNLLQPDALVLSVGTEIYLnga 82
Cdd:cd07507   1 VIFTDLDGTLLDHHTYSfDPARPALERL-----KERGIPVVPCTSKT---RAEVEYlRKELGIEDPFIVENGGAIFI--- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  83 dtpDSDWSEIlsPGWEREV----VLSITRKYRELVRQPDS--EQRAFKVSFFLEQEASANV----LPQLEAELQKSKL-N 151
Cdd:cd07507  70 ---PRGYFKF--PGRCKSEggyeVIELGKPYREIRAALEKirEETGFKITGFGDLTEEEIAeltgLPRERAALAKEREyS 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 152 VKLIYSSGIDLD----------------------IVPHSSDKGQAMQFLRQKWK--FAAEQTVVCGDSGNDIALFAVGnE 207
Cdd:cd07507 145 ETIILRSDEEEDekvlealeerglkitkggrfyhVLGAGADKGKAVAILAALYRqlYEAIVTVGLGDSPNDLPMLEAV-D 223

                       250
                ....*....|.
gi 16605555 208 RGIIVGNARKE 218
Cdd:cd07507 224 IAFVVKSLNGK 234
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 105-219 6.85e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 42.65  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  105 ITRKYREL---VRQPDSEQR----AFKVSFFLEQeasanvlpqLEAELQKSKLNVKLIYSsGIDLDIVPHSSDKGQAMQF 177
Cdd:PRK01158  95 LKKRFPEAstsLTKLDPDYRktevALRRTVPVEE---------VRELLEELGLDLEIVDS-GFAIHIKSPGVNKGTGLKK 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 16605555  178 LRQKWKFAAEQTVVCGDSGNDIALFAVGNeRGIIVGNARKEL 219
Cdd:PRK01158 165 LAELMGIDPEEVAAIGDSENDLEMFEVAG-FGVAVANADEEL 205
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 133-212 4.45e-04

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: 38.53  E-value: 4.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555 133 ASANVLPQLEAELQKSKLNVKLIYssGIDLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGNERGIIV 212
Cdd:cd01427  29 VTNRSREALRALLEKLGLGDLFDG--IIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTVAV 106
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 169-221 1.09e-03

Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 39.43  E-value: 1.09e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16605555 169 SDKGQAMQFLRQKWKFAAEQTVVC---GDSGNDIALFAVGNeRGIIVGNARKELLQ 221
Cdd:COG3769 187 ADKGKAVRWLVEQYRQRFGKNVVTialGDSPNDIPMLEAAD-IAVVIRSPHGAPPE 241
HAD_SPS cd16419
sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; ...
 5-196 1.71e-03

sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; Sucrose phosphate synthase (SPS; EC 2.4.1.14) also known as UDP-glucose-fructose-phosphate glucosyltransferase, catalyzes the transfer of a hexosyl group from UDP-glucose to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate, this is the rate limiting step of sucrose synthesis. 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319856  Cd Length: 174  Bit Score: 37.99  E-value: 1.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555   5 LFVTDLDDTLvyrtTGDDSALPELNQLLKRHRQEYGTKI---VYSTGRS-PVLYKELQ-AQKNLLQPDALVLSVGTEIYL 79
Cdd:cd16419   1 LFVIAVDCYD----SSGLPALRVIKNILKAVRSDSGGGStgfVLSTSLTlSETVSLLKsAGISVTDFDALICNSGSELYY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16605555  80 NGADTPDsdwseilsPGWEREVVLSItRKYRELVRqpdseQRAFkvsffleqeaSANvlpqleaelqksklnvkLIYSS- 158
Cdd:cd16419  77 PSPSGDD--------DSDYELIPDPV-KELRKLLR-----MRGL----------RCH-----------------LVYCRn 115

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 16605555 159 GIDLDIVPHSSDKGQAMQFLRQKWKFAAEQTVVC-GDSG 196
Cdd:cd16419 116 GTRLHVLPLLASRSQALRYLFVRWGIDLSNMVVFvGESG 154
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 171-203 6.31e-03

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 36.37  E-value: 6.31e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 16605555 171 KGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFA 203
Cdd:cd07500 138 KAETLQELAARLGIPLEQTVAVGDGANDLPMLK 170
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 170-219 7.49e-03

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: 35.64  E-value: 7.49e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16605555 170 DKGQAMQFLRQKWKFAAEQTVVCGDSGNDIALFAVGNErGIIVGNARKEL 219
Cdd:cd07514  67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGF-KVAVANADEEL 115
 
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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