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Conserved domains on  [gi|2198613519|gb|ULP70456|]
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Mannosylfructose-phosphate phosphatase [Nodularia sphaerocarpa UHCC 0038]

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 ...
 3-247 3.85e-125

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: 355.27  E-value: 3.85e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   3 PFLFVSDLDNTFV----GDDDALTALTQSLSQHRQVYgSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYLDGQ 78
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhtdGDNQALLRLNALLEDHRGED-SLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  79 DTPDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEVA-NILPQLEAELLKSKLNVKLIYSSGIDL 157
Cdd:TIGR01485  80 EVPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAApEVIKQLTEMLKETGLDVKLIYSSGKDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 158 DIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGEERGIIVGNARPELLKWHSEYPANYRYLAQAVCAGGI 237
Cdd:TIGR01485 160 DILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGI 239

                         250
                  ....*....|
gi 2198613519 238 LEGLKYFGFL 247
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 ...
 3-247 3.85e-125

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: 355.27  E-value: 3.85e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   3 PFLFVSDLDNTFV----GDDDALTALTQSLSQHRQVYgSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYLDGQ 78
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhtdGDNQALLRLNALLEDHRGED-SLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  79 DTPDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEVA-NILPQLEAELLKSKLNVKLIYSSGIDL 157
Cdd:TIGR01485  80 EVPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAApEVIKQLTEMLKETGLDVKLIYSSGKDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 158 DIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGEERGIIVGNARPELLKWHSEYPANYRYLAQAVCAGGI 237
Cdd:TIGR01485 160 DILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGI 239

                         250
                  ....*....|
gi 2198613519 238 LEGLKYFGFL 247
Cdd:TIGR01485 240 IEAIAHFDLL 249
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 2-246 2.37e-110

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: 317.67  E-value: 2.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   2 KPFLFVSDLDNTFV-GDDDALTALTQSLSQHRQvyGSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYLDGQDT 80
Cdd:pfam05116   1 PPLLLVSDLDNTLVdGDNEALARLNQLLEAYRP--DVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGPSLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  81 PDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEVA-NILPQLEAELLKSKLNVKLIYSSGIDLDI 159
Cdd:pfam05116  79 PDQSWQEHLDYHWDRQAVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAaAVLAELEQLLRKRGLDVKVIYSSGRDLDI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 160 VPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFaVGEERGIIVGNARPELLKWHSEYPANYR--YLAQAVCAGGI 237
Cdd:pfam05116 159 LPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELF-IGGTRGVVVGNAQPELLQWYLENARDNPriYFASGRCAGGI 237


                  ....*....
gi 2198613519 238 LEGLKYFGF 246
Cdd:pfam05116 238 LEGIRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-244 1.17e-95

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: 280.39  E-value: 1.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFVGDDD------ALTALTQSLSQHRqvyGSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYL--D 76
Cdd:cd02605     1 LLVSDLDETLVGHDTnlqaleRLQDLLEQLTADN---DVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYgeS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  77 GQDTPDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEV-ANILPQLEAELLKSKLNVKLIYSSG- 154
Cdd:cd02605    78 GYLEPDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNdAAVIEQLEEMLLKAGLTVRIIYSSGl 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 155 -IDLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGeERGIIVGNARPELLKWHSEYPANyrYLAQAVC 233
Cdd:cd02605   158 aYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTG-TRGVIVGNAQPELLKWADRVTRS--RLAKGPY 234

                         250
                  ....*....|.
gi 2198613519 234 AGGILEGLKYF 244
Cdd:cd02605   235 AGGILEGLAHF 245
PLN02382 PLN02382
probable sucrose-phosphatase
 5-245 1.68e-81

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 249.90  E-value: 1.68e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFV--GDDDALTALT-QSLSQHRQVYGSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYLDGQDTP 81
Cdd:PLN02382   11 MIVSDLDHTMVdhHDPENLSLLRfNALWEAEYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIAYGESMVP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  82 DAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFL-KQEVANILPQLEAELLKSKLNVKLIYSSGIDLDIV 160
Cdd:PLN02382   91 DHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVdKKKAQEVIKELSERLEKRGLDVKIIYSGGIDLDVL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 161 PLTSDKGQAMQFLRQKwsFAAE-----QTVVCGDSGNDIALFAVGEERGIIVGNARPELLKWHSEYPAN--YRYLAQAVC 233
Cdd:PLN02382  171 PQGAGKGQALAYLLKK--LKAEgkapvNTLVCGDSGNDAELFSVPDVYGVMVSNAQEELLQWYAENAKDnpKIIHATERC 248

                         250
                  ....*....|..
gi 2198613519 234 AGGILEGLKYFG 245
Cdd:PLN02382  249 AAGIIQAIGHFN 260
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 5-244 4.18e-33

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: 118.70  E-value: 4.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFVGDDDALTALT-QSLSQHRQvYGSKIVYATGRSPILYRELQTEKNLmePDALVLSVGTEIYldgqdtpDA 83
Cdd:COG0561     4 LIALDLDGTLLNDDGEISPRTkEALRRLRE-KGIKVVIATGRPLRSALPLLEELGL--DDPLITSNGALIY-------DP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  84 AWSEILSSGWDNELVLKIAQSFPELemqpdseqrafkvsfflkqevaNILPQLeaellksklnvkLIYSSGIDLDIVPLT 163
Cdd:COG0561    74 DGEVLYERPLDPEDVREILELLREH----------------------GLHLQV------------VVRSGPGFLEILPKG 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 164 SDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALF-AVGeeRGIIVGNARPELLKWHseypanyRYLAQAVCAGGILEGLK 242
Cdd:COG0561   120 VSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLeAAG--LGVAMGNAPPEVKAAA-------DYVTGSNDEDGVAEALE 190


                  ..
gi 2198613519 243 YF 244
Cdd:COG0561   191 KL 192
 
Name Accession Description Interval E-value
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 3-247 3.85e-125

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: 355.27  E-value: 3.85e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   3 PFLFVSDLDNTFV----GDDDALTALTQSLSQHRQVYgSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYLDGQ 78
Cdd:TIGR01485   1 RLLLVSDLDNTLVdhtdGDNQALLRLNALLEDHRGED-SLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  79 DTPDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEVA-NILPQLEAELLKSKLNVKLIYSSGIDL 157
Cdd:TIGR01485  80 EVPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAApEVIKQLTEMLKETGLDVKLIYSSGKDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 158 DIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGEERGIIVGNARPELLKWHSEYPANYRYLAQAVCAGGI 237
Cdd:TIGR01485 160 DILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSVRGVIVSNAQEELLQWYDENAKDKIYHASERCAGGI 239

                         250
                  ....*....|
gi 2198613519 238 LEGLKYFGFL 247
Cdd:TIGR01485 240 IEAIAHFDLL 249
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 2-246 2.37e-110

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: 317.67  E-value: 2.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   2 KPFLFVSDLDNTFV-GDDDALTALTQSLSQHRQvyGSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYLDGQDT 80
Cdd:pfam05116   1 PPLLLVSDLDNTLVdGDNEALARLNQLLEAYRP--DVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGPSLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  81 PDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEVA-NILPQLEAELLKSKLNVKLIYSSGIDLDI 159
Cdd:pfam05116  79 PDQSWQEHLDYHWDRQAVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAaAVLAELEQLLRKRGLDVKVIYSSGRDLDI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 160 VPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFaVGEERGIIVGNARPELLKWHSEYPANYR--YLAQAVCAGGI 237
Cdd:pfam05116 159 LPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELF-IGGTRGVVVGNAQPELLQWYLENARDNPriYFASGRCAGGI 237


                  ....*....
gi 2198613519 238 LEGLKYFGF 246
Cdd:pfam05116 238 LEGIRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-244 1.17e-95

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: 280.39  E-value: 1.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFVGDDD------ALTALTQSLSQHRqvyGSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYL--D 76
Cdd:cd02605     1 LLVSDLDETLVGHDTnlqaleRLQDLLEQLTADN---DVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYgeS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  77 GQDTPDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEV-ANILPQLEAELLKSKLNVKLIYSSG- 154
Cdd:cd02605    78 GYLEPDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNdAAVIEQLEEMLLKAGLTVRIIYSSGl 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 155 -IDLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGeERGIIVGNARPELLKWHSEYPANyrYLAQAVC 233
Cdd:cd02605   158 aYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTG-TRGVIVGNAQPELLKWADRVTRS--RLAKGPY 234

                         250
                  ....*....|.
gi 2198613519 234 AGGILEGLKYF 244
Cdd:cd02605   235 AGGILEGLAHF 245
PLN02382 PLN02382
probable sucrose-phosphatase
 5-245 1.68e-81

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 249.90  E-value: 1.68e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFV--GDDDALTALT-QSLSQHRQVYGSKIVYATGRSPILYRELQTEKNLMEPDALVLSVGTEIYLDGQDTP 81
Cdd:PLN02382   11 MIVSDLDHTMVdhHDPENLSLLRfNALWEAEYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEIAYGESMVP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  82 DAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFL-KQEVANILPQLEAELLKSKLNVKLIYSSGIDLDIV 160
Cdd:PLN02382   91 DHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVdKKKAQEVIKELSERLEKRGLDVKIIYSGGIDLDVL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 161 PLTSDKGQAMQFLRQKwsFAAE-----QTVVCGDSGNDIALFAVGEERGIIVGNARPELLKWHSEYPAN--YRYLAQAVC 233
Cdd:PLN02382  171 PQGAGKGQALAYLLKK--LKAEgkapvNTLVCGDSGNDAELFSVPDVYGVMVSNAQEELLQWYAENAKDnpKIIHATERC 248

                         250
                  ....*....|..
gi 2198613519 234 AGGILEGLKYFG 245
Cdd:PLN02382  249 AAGIIQAIGHFN 260
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 5-246 1.83e-53

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: 172.64  E-value: 1.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFVGDDDALTALTQSLSQHRQVYGSKIvyATGRSPILYRELQTEKNLMEPDALVLSVGTEIYLDGQDTPDAA 84
Cdd:TIGR02471   1 LIITDLDNTLLGDDEGLASFVELLRGSGDAVGFGI--ATGRSVESAKSRYAKLNLPSPDVLIARVGTEIYYGPELQPDRF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  85 WSEILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEVANILPQLEAELLKSKLNVKLIYSSGIDLDIVPLTS 164
Cdd:TIGR02471  79 WQKHIDHDWRRQAVVEALADIPGLTLQDDQEQGPFKISYLLDPEGEPILPQIRQRLRQQSQAAKVILSCGWFLDVLPLRA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 165 DKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFaVGEERGIIVGNARPELLKWHSEypaNYRYLAQAVCAGGILEGLKYF 244
Cdd:TIGR02471 159 SKGLALRYLSYRWGLPLEQILVAGDSGNDEEML-RGLTLGVVVGNHDPELEGLRHQ---QRIYFANNPHAFGILEGINHY 234


                  ..
gi 2198613519 245 GF 246
Cdd:TIGR02471 235 DF 236
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 7-239 8.36e-48

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: 157.62  E-value: 8.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   7 VSDLDNTFVGDDDALTALTQSLSQHRQVYGSKIVYATGRSPILYRELQTEKNlmEPDALVLSVGTEIYLdgQDTPDAAWS 86
Cdd:TIGR01482   2 ASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIG--TPDPVIAENGGEISY--NEGLDDIFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  87 EILSSGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEVANilpqleaELLKsKLNVKLIY-SSGIDLDIVPLTSD 165
Cdd:TIGR01482  78 AYLEEEWFLDIVIAKTFPFSRLKVQYPRRASLVKMRYGIDVDTVR-------EIIK-ELGLNLVAvDSGFDIHILPQGVN 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2198613519 166 KGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGeERGIIVGNARPELLKWHSEYPANYRYLAQAVCAGGILE 239
Cdd:TIGR01482 150 KGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVP-GFGVAVANAQPELKEWADYVTESPYGEGGAEAIGEILQ 222
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 5-244 4.18e-33

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: 118.70  E-value: 4.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFVGDDDALTALT-QSLSQHRQvYGSKIVYATGRSPILYRELQTEKNLmePDALVLSVGTEIYldgqdtpDA 83
Cdd:COG0561     4 LIALDLDGTLLNDDGEISPRTkEALRRLRE-KGIKVVIATGRPLRSALPLLEELGL--DDPLITSNGALIY-------DP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  84 AWSEILSSGWDNELVLKIAQSFPELemqpdseqrafkvsfflkqevaNILPQLeaellksklnvkLIYSSGIDLDIVPLT 163
Cdd:COG0561    74 DGEVLYERPLDPEDVREILELLREH----------------------GLHLQV------------VVRSGPGFLEILPKG 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 164 SDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALF-AVGeeRGIIVGNARPELLKWHseypanyRYLAQAVCAGGILEGLK 242
Cdd:COG0561   120 VSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLeAAG--LGVAMGNAPPEVKAAA-------DYVTGSNDEDGVAEALE 190


                  ..
gi 2198613519 243 YF 244
Cdd:COG0561   191 KL 192
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-206 4.24e-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: 85.12  E-value: 4.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFVGDDD--ALTALTQSLSQHRQVyGSKIVYATGRSPILYRELQTEKNLMEPdaLVLSVGTEIYLDGQD--- 79
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAheLSPETIEALERLREA-GVKVVIVTGRSLAEIKELLKQLNLPLP--LIAENGALIFYPGEIlyi 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  80 TPDAAWSEILssGWDNELVLKIAQSFPELEMQPDSEQRAFKVSFFLKQEVAN--ILPQLEAELLKSKLN---VKLIYSSG 154
Cdd:TIGR01484  78 EPSDVFEEIL--GIKFEEIGAELKSLSEHYVGTFIEDKAIAVAIHYVGAELGqeLDSKMRERLEKIGRNdleLEAIYSGK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2198613519 155 IDLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGEERGII 206
Cdd:TIGR01484 156 TDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-241 2.94e-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: 2.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFVGDDD-----ALTALTQSLSQhrqvyGSKIVYATGRSPI----LYRELQTE------------------- 56
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHtispsTKEALAKLREK-----GIKVVLATGRPYKevknILKELGLDtpfitangaaviddqgeil 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  57 -KNLMEPDAL------VLSVGTEIYLDGQDTPDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSEQraFKVSFFLKQEV 129
Cdd:TIGR00099  76 yKKPLDLDLVeeilnfLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDIL--KILLLFLDPED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 130 ANILP-QLEAELLKSKLNVkLIYSSGIdLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALF-AVGeeRGIIV 207
Cdd:TIGR00099 154 LDLLIeALNKLELEENVSV-VSSGPYS-IEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLeAAG--YGVAM 229

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2198613519 208 GNARPELLKWHseypanyRYLAQAVCAGGILEGL 241
Cdd:TIGR00099 230 GNADEELKALA-------DYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-216 1.65e-16

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 76.12  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   6 FVSDLDNTFVGDDDALT-----ALTQSLSQhrqvyGSKIVYATGRSpilYRE-LQTEKNLMEPDALVLSVGTEIYldgqd 79
Cdd:pfam08282   1 IASDLDGTLLNSDKKISektkeAIKKLKEK-----GIKFVIATGRP---YRAiLPVIKELGLDDPVICYNGALIY----- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  80 tpDAAWSEILSSGWDNELVLKIAQSFPEL-----------------EMQPDSEQRAFKVSFF----------LKQEVANI 132
Cdd:pfam08282  68 --DENGKILYSNPISKEAVKEIIEYLKENnleillytddgvyilndNELEKILKELNYTKSFvpeiddfellEDEDINKI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 133 LPQLEAEL-------LKSKLNVKLIY--SSGIDLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALF-AVGee 202
Cdd:pfam08282 146 LILLDEEDldelekeLKELFGSLITItsSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLeAAG-- 223

                         250
                  ....*....|....
gi 2198613519 203 RGIIVGNARPELLK 216
Cdd:pfam08282 224 LGVAMGNASPEVKA 237
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-214 4.82e-14

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: 69.55  E-value: 4.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   5 LFVSDLDNTFVGDD--------DALTALTQSlsqhrqvyGSKIVYATGRSPI----LYRELQ----------------TE 56
Cdd:cd07516     1 LIALDLDGTLLNSDkeisprtkEAIKKAKEK--------GIKVVIATGRPLRgaqpYLEELGldsplitfngalvydpTG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  57 KNLMEP-----DALVL-------SVGTEIYldgqdTPDAAWSEILSSGWDNELVLKIAQSFPELEMQPDSeqrAFKVSFF 124
Cdd:cd07516    73 KEILERliskeDVKELeeflrklGIGINIY-----TNDDWADTIYEENEDDEIIKPAEILDDLLLPPDED---ITKILFV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 125 LKQEvaNILPQLEAELLKSKLNVKLIYSSGIDLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALF-AVGeeR 203
Cdd:cd07516   145 GEDE--ELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLeYAG--L 220

                         250
                  ....*....|.
gi 2198613519 204 GIIVGNARPEL 214
Cdd:cd07516   221 GVAMGNAIDEV 231
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 9-245 5.46e-12

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: 63.01  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   9 DLDNTFVGDDDALTALTQSLSQHRQVYGSKIVYATGRSPIlyrELQTEKNLMEPDALVLSVGTEIYLDGQdtpdaawsEI 88
Cdd:cd07517     6 DIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPF---EIQPIVKALGIDSYVSYNGQYVFFEGE--------VI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  89 LSSGWDNELVLKIAQsfpelemQPDSEQRAfkVSFFLkQEVANILPQLEAELLKSKLNVKLIYSSGIDLDIVPLTSDKGQ 168
Cdd:cd07517    75 YKNPLPQELVERLTE-------FAKEQGHP--VSFYG-QLLLFEDEEEEQKYEELRPELRFVRWHPLSTDVIPKGGSKAK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 169 AMQFLRQKWSFAAEQTVVCGDSGNDIALF-AVGeeRGIIVGNARPELLKwhseypanyryLAQAVCA----GGILEGLKY 243
Cdd:cd07517   145 GIQKVIEHLGIKKEETMAFGDGLNDIEMLeAVG--IGIAMGNAHEELKE-----------IADYVTKdvdeDGILKALKH 211


                  ..
gi 2198613519 244 FG 245
Cdd:cd07517   212 FG 213
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 119-216 5.99e-11

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: 59.52  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 119 FKVSFFLKQEVANILpqleAELLKSKLNVKL-IYSSG-IDLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIAL 196
Cdd:cd07518    71 FKFTLNVPDEAAPDI----IDELNQKFGGILrAVTSGfGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEM 146

                          90       100
                  ....*....|....*....|.
gi 2198613519 197 F-AVGeeRGIIVGNARPELLK 216
Cdd:cd07518   147 LkYAG--YSYAMENAPEEVKA 165
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 70-246 5.07e-07

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 49.20  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  70 GTEIYLDGQDTPDAAWSEILssgwdnelvlkiaQSFPELEMQ---PDSEQRAFKVSF---FLKQEVANILPQLEaellks 143
Cdd:PRK01158   77 GKRIFLGDIEECEKAYSELK-------------KRFPEASTSltkLDPDYRKTEVALrrtVPVEEVRELLEELG------ 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 144 kLNVKLIYSsGIDLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGeERGIIVGNArPELLKWHSEYPA 223
Cdd:PRK01158  138 -LDLEIVDS-GFAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVA-GFGVAVANA-DEELKEAADYVT 213

                         170       180
                  ....*....|....*....|...
gi 2198613519 224 NYRYlaqavcAGGILEGLKYFGF 246
Cdd:PRK01158  214 EKSY------GEGVAEAIEHLLL 230
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 144-227 4.15e-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: 46.27  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 144 KLNVKLIYSsGIDLDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGEERgIIVGNArPELLKWHSEYPA 223
Cdd:TIGR01487 127 ERGLNLVAS-GFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFK-VAVANA-DDQLKEIADYVT 203


                  ....
gi 2198613519 224 NYRY 227
Cdd:TIGR01487 204 SNPY 207
PRK15126 PRK15126
HMP-PP phosphatase;
9-214 2.90e-05

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 44.30  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519   9 DLDNTFVGDDDALTALTQS-LSQHRQvYGSKIVYATGRSPILYRELQTEKNLmepDA-LVLSVGTEIY------LDGQDT 80
Cdd:PRK15126    8 DMDGTLLMPDHHLGEKTLStLARLRE-RDITLTFATGRHVLEMQHILGALSL---DAyLITGNGTRVHslegelLHRQDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519  81 PDAAWSEILSSGWDNELVLKI--------AQSFPELemqpdseQRAFKVSFFLKQ-------------EVANILPQLEAE 139
Cdd:PRK15126   84 PADVAELVLHQQWDTRASMHVfnddgwftGKEIPAL-------LQAHVYSGFRYQlidlkrlpahgvtKICFCGDHDDLT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198613519 140 LLKSKLNVKL-----IYSSGID-LDIVPLTSDKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFA-VGeeRGIIVGNARP 212
Cdd:PRK15126  157 RLQIQLNEALgerahLCFSATDcLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGsVG--RGFIMGNAMP 234


                  ..
gi 2198613519 213 EL 214
Cdd:PRK15126  235 QL 236
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 165-216 4.94e-04

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: 39.11  E-value: 4.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2198613519 165 DKGQAMQFLRQKWSFAAEQTVVCGDSGNDIALFAVGEErGIIVGNARPELLK 216
Cdd:cd07514    67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGF-KVAVANADEELKE 117
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 164-231 1.82e-03

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 38.77  E-value: 1.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2198613519 164 SDKGQAMQFLRQKWSFAAE-QTVVCGDSGNDIALFAVGeERGIIVGNARPELLKWHSEYPANYRYLAQA 231
Cdd:PRK00192  189 GDKGKAVRWLKELYRRQDGvETIALGDSPNDLPMLEAA-DIAVVVPGPDGPNPPLLPGIADGEFILASA 256
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 159-232 6.92e-03

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: 36.96  E-value: 6.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2198613519 159 IVPLTSDKGQAMQFLRQKWS--FAAEQTVVCGDSGNDIALFAVGeERGIIVGNARPellKWHSEYPANYrYLAQAV 232
Cdd:cd07507   179 VLGAGADKGKAVAILAALYRqlYEAIVTVGLGDSPNDLPMLEAV-DIAFVVKSLNG---KYESVILPGV-LKAPAP 249
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 164-216 9.91e-03

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 36.34  E-value: 9.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2198613519 164 SDKGQAMQFLRQKWSFAAEQTVVC---GDSGNDIALFAVGeERGIIVGNARPELLK 216
Cdd:COG3769   187 ADKGKAVRWLVEQYRQRFGKNVVTialGDSPNDIPMLEAA-DIAVVIRSPHGAPPE 241
 
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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