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Conserved domains on  [gi|42571071|ref|NP_973609|]
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Sucrose-6F-phosphate phosphohydrolase family protein [Arabidopsis thaliana]

Protein Classification

PLN02382 family protein( domain architecture ID 11476726)

PLN02382 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02382 PLN02382
probable sucrose-phosphatase
 1-411 0e+00

probable sucrose-phosphatase


:

Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 870.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    1 MERLTSPPRLMIVSDLDHTMVDHHDPENLSLLRFNSLWEHAYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGT 80
Cdd:PLN02382   1 MDRLSGSPRLMIVSDLDHTMVDHHDPENLSLLRFNALWEAEYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   81 EITYGNSMVPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKII 160
Cdd:PLN02382  81 EIAYGESMVPDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVDKKKAQEVIKELSERLEKRGLDVKII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  161 YSGGMDLDILPQGAGKGQALAYLLKKLKTEGKLPVNTLACGDSGNDAELFSIPDVYGVMVSNAQEELLKWHAENAKDNPK 240
Cdd:PLN02382 161 YSGGIDLDVLPQGAGKGQALAYLLKKLKAEGKAPVNTLVCGDSGNDAELFSVPDVYGVMVSNAQEELLQWYAENAKDNPK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  241 VIHAKERCAGGIIQAIGHFKLGPNLSPRDVSDFLEIKVENVNPGHEVVKFFLFYERWRRGEVENSEAYTASLKASVHPGG 320
Cdd:PLN02382 241 IIHATERCAAGIIQAIGHFNLGPNVSPRDVSDFLYGKLDNVNPAHEVVKFYLFYEKWRRGEVENSDEVFQRLKSSCAPNG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  321 VFVHPSGTEKSLRDTIDELRKYHGDKQGKKFRVWADQVLATDTTPGTWIVKLDKWEQDGDERRCCTTTVKFTSKEG--EG 398
Cdd:PLN02382 321 VFVHPSGVEKSLHDSIDELRSCYGDKKGKKFRVWVDRVLSTQLGPDTWLVKFDKWEQSGDERKCCLTTALLTSKEDtpNG 400

                        410
                 ....*....|...
gi 42571071  399 LVWEHVQQTWSKE 411
Cdd:PLN02382 401 LEWMHVHQTWLEG 413
 
Name Accession Description Interval E-value
PLN02382 PLN02382
probable sucrose-phosphatase
 1-411 0e+00

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 870.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    1 MERLTSPPRLMIVSDLDHTMVDHHDPENLSLLRFNSLWEHAYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGT 80
Cdd:PLN02382   1 MDRLSGSPRLMIVSDLDHTMVDHHDPENLSLLRFNALWEAEYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   81 EITYGNSMVPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKII 160
Cdd:PLN02382  81 EIAYGESMVPDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVDKKKAQEVIKELSERLEKRGLDVKII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  161 YSGGMDLDILPQGAGKGQALAYLLKKLKTEGKLPVNTLACGDSGNDAELFSIPDVYGVMVSNAQEELLKWHAENAKDNPK 240
Cdd:PLN02382 161 YSGGIDLDVLPQGAGKGQALAYLLKKLKAEGKAPVNTLVCGDSGNDAELFSVPDVYGVMVSNAQEELLQWYAENAKDNPK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  241 VIHAKERCAGGIIQAIGHFKLGPNLSPRDVSDFLEIKVENVNPGHEVVKFFLFYERWRRGEVENSEAYTASLKASVHPGG 320
Cdd:PLN02382 241 IIHATERCAAGIIQAIGHFNLGPNVSPRDVSDFLYGKLDNVNPAHEVVKFYLFYEKWRRGEVENSDEVFQRLKSSCAPNG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  321 VFVHPSGTEKSLRDTIDELRKYHGDKQGKKFRVWADQVLATDTTPGTWIVKLDKWEQDGDERRCCTTTVKFTSKEG--EG 398
Cdd:PLN02382 321 VFVHPSGVEKSLHDSIDELRSCYGDKKGKKFRVWVDRVLSTQLGPDTWLVKFDKWEQSGDERKCCLTTALLTSKEDtpNG 400

                        410
                 ....*....|...
gi 42571071  399 LVWEHVQQTWSKE 411
Cdd:PLN02382 401 LEWMHVHQTWLEG 413
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 9-262 7.16e-140

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: 399.57  E-value: 7.16e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071     9 RLMIVSDLDHTMVDHHDPENLSLLRFNSLWEHAYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEITYGNSM 88
Cdd:TIGR01485   1 RLLLVSDLDNTLVDHTDGDNQALLRLNALLEDHRGEDSLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGGAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    89 VPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKIIYSGGMDLD 168
Cdd:TIGR01485  81 VPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTEMLKETGLDVKLIYSSGKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   169 ILPQGAGKGQALAYLLKKLKTEgklPVNTLACGDSGNDAELFSIPDVYGVMVSNAQEELLKWHAENAKDnpKVIHAKERC 248
Cdd:TIGR01485 161 ILPQGSGKGQALQYLLQKLAME---PSQTLVCGDSGNDIELFEIGSVRGVIVSNAQEELLQWYDENAKD--KIYHASERC 235

                         250
                  ....*....|....
gi 42571071   249 AGGIIQAIGHFKLG 262
Cdd:TIGR01485 236 AGGIIEAIAHFDLL 249
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 8-261 4.39e-135

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: 387.39  E-value: 4.39e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071     8 PRLMIVSDLDHTMVDhhdPENLSLLRFNSLWEHaYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEITYGNS 87
Cdd:pfam05116   1 PPLLLVSDLDNTLVD---GDNEALARLNQLLEA-YRPDVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGPS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    88 MVPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKIIYSGGMDL 167
Cdd:pfam05116  77 LVPDQSWQEHLDYHWDRQAVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLAELEQLLRKRGLDVKVIYSSGRDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   168 DILPQGAGKGQALAYLLKKLKTEgklPVNTLACGDSGNDAELFsIPDVYGVMVSNAQEELLKWHAENAKDNPKVIHAKER 247
Cdd:pfam05116 157 DILPLRASKGEALRYLALKLGLP---LENTLVCGDSGNDEELF-IGGTRGVVVGNAQPELLQWYLENARDNPRIYFASGR 232

                         250
                  ....*....|....
gi 42571071   248 CAGGIIQAIGHFKL 261
Cdd:pfam05116 233 CAGGILEGIRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 11-259 2.35e-108

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: 319.29  E-value: 2.35e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  11 MIVSDLDHTMVDHHDPeNLSLLRFNSLWEHAYRH-DSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEITYGNS-- 87
Cdd:cd02605   1 LLVSDLDETLVGHDTN-LQALERLQDLLEQLTADnDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYGESgy 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  88 MVPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKIIYSGG--M 165
Cdd:cd02605  80 LEPDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGlaY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071 166 DLDILPQGAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDAELFSIPdVYGVMVSNAQEELLKWHAENAKDNpkviHAK 245
Cdd:cd02605 160 DLDILPLGAGKGEALRYLQEKW---NFPPERTLVCGDSGNDIALLSTG-TRGVIVGNAQPELLKWADRVTRSR----LAK 231

                       250
                ....*....|....
gi 42571071 246 ERCAGGIIQAIGHF 259
Cdd:cd02605 232 GPYAGGILEGLAHF 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 11-259 2.48e-22

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: 93.66  E-value: 2.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  11 MIVSDLDHTMVDHH---DPENLSLLRfnslweHAYRHDSLLVFSTGRSPTLYKELRKEKPLltPDITIMSVGTEITYGNs 87
Cdd:COG0561   4 LIALDLDGTLLNDDgeiSPRTKEALR------RLREKGIKVVIATGRPLRSALPLLEELGL--DDPLITSNGALIYDPD- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  88 mvpdhgwvealnnkwdlgivkqeasnfpelklqaetEQRPHKVSFyvekskAQEVTKELSQRFLKRGLDV-KIIYSGGMD 166
Cdd:COG0561  75 ------------------------------------GEVLYERPL------DPEDVREILELLREHGLHLqVVVRSGPGF 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071 167 LDILPQGAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDAELFSIPDvYGVMVSNAQEELLKWHAENAKDNpkvihake 246
Cdd:COG0561 113 LEILPKGVSKGSALKKLAERL---GIPPEEVIAFGDSGNDLEMLEAAG-LGVAMGNAPPEVKAAADYVTGSN-------- 180

                       250
                ....*....|...
gi 42571071 247 rCAGGIIQAIGHF 259
Cdd:COG0561 181 -DEDGVAEALEKL 192
 
Name Accession Description Interval E-value
PLN02382 PLN02382
probable sucrose-phosphatase
 1-411 0e+00

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 870.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    1 MERLTSPPRLMIVSDLDHTMVDHHDPENLSLLRFNSLWEHAYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGT 80
Cdd:PLN02382   1 MDRLSGSPRLMIVSDLDHTMVDHHDPENLSLLRFNALWEAEYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   81 EITYGNSMVPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKII 160
Cdd:PLN02382  81 EIAYGESMVPDHGWVEYLNKKWDREIVVEETSKFPELKLQPETEQRPHKVSFYVDKKKAQEVIKELSERLEKRGLDVKII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  161 YSGGMDLDILPQGAGKGQALAYLLKKLKTEGKLPVNTLACGDSGNDAELFSIPDVYGVMVSNAQEELLKWHAENAKDNPK 240
Cdd:PLN02382 161 YSGGIDLDVLPQGAGKGQALAYLLKKLKAEGKAPVNTLVCGDSGNDAELFSVPDVYGVMVSNAQEELLQWYAENAKDNPK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  241 VIHAKERCAGGIIQAIGHFKLGPNLSPRDVSDFLEIKVENVNPGHEVVKFFLFYERWRRGEVENSEAYTASLKASVHPGG 320
Cdd:PLN02382 241 IIHATERCAAGIIQAIGHFNLGPNVSPRDVSDFLYGKLDNVNPAHEVVKFYLFYEKWRRGEVENSDEVFQRLKSSCAPNG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  321 VFVHPSGTEKSLRDTIDELRKYHGDKQGKKFRVWADQVLATDTTPGTWIVKLDKWEQDGDERRCCTTTVKFTSKEG--EG 398
Cdd:PLN02382 321 VFVHPSGVEKSLHDSIDELRSCYGDKKGKKFRVWVDRVLSTQLGPDTWLVKFDKWEQSGDERKCCLTTALLTSKEDtpNG 400

                        410
                 ....*....|...
gi 42571071  399 LVWEHVQQTWSKE 411
Cdd:PLN02382 401 LEWMHVHQTWLEG 413
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 9-262 7.16e-140

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: 399.57  E-value: 7.16e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071     9 RLMIVSDLDHTMVDHHDPENLSLLRFNSLWEHAYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEITYGNSM 88
Cdd:TIGR01485   1 RLLLVSDLDNTLVDHTDGDNQALLRLNALLEDHRGEDSLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGGAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    89 VPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKIIYSGGMDLD 168
Cdd:TIGR01485  81 VPDQHWAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRPHKVSFFLDPEAAPEVIKQLTEMLKETGLDVKLIYSSGKDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   169 ILPQGAGKGQALAYLLKKLKTEgklPVNTLACGDSGNDAELFSIPDVYGVMVSNAQEELLKWHAENAKDnpKVIHAKERC 248
Cdd:TIGR01485 161 ILPQGSGKGQALQYLLQKLAME---PSQTLVCGDSGNDIELFEIGSVRGVIVSNAQEELLQWYDENAKD--KIYHASERC 235

                         250
                  ....*....|....
gi 42571071   249 AGGIIQAIGHFKLG 262
Cdd:TIGR01485 236 AGGIIEAIAHFDLL 249
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 8-261 4.39e-135

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: 387.39  E-value: 4.39e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071     8 PRLMIVSDLDHTMVDhhdPENLSLLRFNSLWEHaYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEITYGNS 87
Cdd:pfam05116   1 PPLLLVSDLDNTLVD---GDNEALARLNQLLEA-YRPDVGLVFATGRSLDSAKELLKEKPLPTPDYLITSVGTEIYYGPS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    88 MVPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKIIYSGGMDL 167
Cdd:pfam05116  77 LVPDQSWQEHLDYHWDRQAVVEALAKFPGLTLQPEEEQRPHKVSYFLDPEAAAAVLAELEQLLRKRGLDVKVIYSSGRDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   168 DILPQGAGKGQALAYLLKKLKTEgklPVNTLACGDSGNDAELFsIPDVYGVMVSNAQEELLKWHAENAKDNPKVIHAKER 247
Cdd:pfam05116 157 DILPLRASKGEALRYLALKLGLP---LENTLVCGDSGNDEELF-IGGTRGVVVGNAQPELLQWYLENARDNPRIYFASGR 232

                         250
                  ....*....|....
gi 42571071   248 CAGGIIQAIGHFKL 261
Cdd:pfam05116 233 CAGGILEGIRHFGL 246
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 11-259 2.35e-108

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: 319.29  E-value: 2.35e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  11 MIVSDLDHTMVDHHDPeNLSLLRFNSLWEHAYRH-DSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEITYGNS-- 87
Cdd:cd02605   1 LLVSDLDETLVGHDTN-LQALERLQDLLEQLTADnDVILVYATGRSPESVLELIKEVMLPKPDFIISDVGTEIYYGESgy 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  88 MVPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKIIYSGG--M 165
Cdd:cd02605  80 LEPDTYWNEVLSEGWERFLFEAIADLFKQLKPQSELEQNPHKISFYLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGlaY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071 166 DLDILPQGAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDAELFSIPdVYGVMVSNAQEELLKWHAENAKDNpkviHAK 245
Cdd:cd02605 160 DLDILPLGAGKGEALRYLQEKW---NFPPERTLVCGDSGNDIALLSTG-TRGVIVGNAQPELLKWADRVTRSR----LAK 231

                       250
                ....*....|....
gi 42571071 246 ERCAGGIIQAIGHF 259
Cdd:cd02605 232 GPYAGGILEGLAHF 245
S6PP_C pfam08472
Sucrose-6-phosphate phosphohydrolase C-terminal; This is the Sucrose-6-phosphate ...
 262-394 1.38e-84

Sucrose-6-phosphate phosphohydrolase C-terminal; This is the Sucrose-6-phosphate phosphohydrolase (S6PP or SPP) C-terminal domain as found in in plant sucrose phosphatases. These enzymes irreversibly catalyze the last step in sucrose synthesis following the formation of Sucrose-6-Phosphate via sucrose-phosphate synthase (SPS).


Pssm-ID: 462487  Cd Length: 133  Bit Score: 254.49  E-value: 1.38e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   262 GPNLSPRDVSDFLEIKVENVNPGHEVVKFFLFYERWRRGEVENSEAYTASLKASVHPGGVFVHPSGTEKSLRDTIDELRK 341
Cdd:pfam08472   1 GPNVSPRDVSDFLYSKADNANPAHEVVKFYLLYEKWRRGEVENSDLYIQRLKAICHPNGVFVHPSGVEKSLHESIDALRS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42571071   342 YHGDKQGKKFRVWADQVLATDTTPGTWIVKLDKWEQDGDERRCCTTTVKFTSK 394
Cdd:pfam08472  81 CYGDKQGKKFRVWVDRVLSSQIGSDTWLVKFDKWELSGEERQCCLTTALLNSK 133
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 12-257 6.92e-73

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: 228.12  E-value: 6.92e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    12 IVSDLDHTMVDHHDPENLSLLRFNSLWEHAYrhdSLLVFSTGRSPTLYKELRKEKPllTPDITIMSVGTEITYGNSMvpD 91
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKG---IPVVLVTGNSVQFARALAKLIG--TPDPVIAENGGEISYNEGL--D 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    92 HGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKrgldvkiiYSGGMDLDILP 171
Cdd:TIGR01482  74 DIFLAYLEEEWFLDIVIAKTFPFSRLKVQYPRRASLVKMRYGIDVDTVREIIKELGLNLVA--------VDSGFDIHILP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   172 QGAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDAELFSIPdVYGVMVSNAQEELLKWHAENAkdNPKVIHAKERCAGG 251
Cdd:TIGR01482 146 QGVNKGVAVKKLKEKL---GIKPGETLVCGDSENDIDLFEVP-GFGVAVANAQPELKEWADYVT--ESPYGEGGAEAIGE 219


                  ....*.
gi 42571071   252 IIQAIG 257
Cdd:TIGR01482 220 ILQAIG 225
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
 11-259 5.64e-39

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: 140.29  E-value: 5.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    11 MIVSDLDHTMVDhhDPENLSLLRfnsLWEHAYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEITYGNSMVP 90
Cdd:TIGR02471   1 LIITDLDNTLLG--DDEGLASFV---ELLRGSGDAVGFGIATGRSVESAKSRYAKLNLPSPDVLIARVGTEIYYGPELQP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    91 DHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVtKELSQRFLKRGLDVKIIYSGGMDLDIL 170
Cdd:TIGR02471  76 DRFWQKHIDHDWRRQAVVEALADIPGLTLQDDQEQGPFKISYLLDPEGEPIL-PQIRQRLRQQSQAAKVILSCGWFLDVL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   171 PQGAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDAELFsIPDVYGVMVSNAQEELlkwhaENAKDNPKVIHAKERCAG 250
Cdd:TIGR02471 155 PLRASKGLALRYLSYRW---GLPLEQILVAGDSGNDEEML-RGLTLGVVVGNHDPEL-----EGLRHQQRIYFANNPHAF 225


                  ....*....
gi 42571071   251 GIIQAIGHF 259
Cdd:TIGR02471 226 GILEGINHY 234
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 11-219 2.00e-32

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: 121.72  E-value: 2.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    11 MIVSDLDHTMVDHHDPEnLSLLRFNSLWEHAYRhDSLLVFSTGRSPTLYKELRKE----KPLLTPDITIMSVGTEITYGN 86
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHE-LSPETIEALERLREA-GVKVVIVTGRSLAEIKELLKQlnlpLPLIAENGALIFYPGEILYIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    87 smvPDHGWVEALNNKWDlgIVKQEASNFPELKLQAETEQRPHKVSF-YVEKSKAQEVTKEL---SQRFLKRGLDVKIIYS 162
Cdd:TIGR01484  79 ---PSDVFEEILGIKFE--EIGAELKSLSEHYVGTFIEDKAIAVAIhYVGAELGQELDSKMrerLEKIGRNDLELEAIYS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571071   163 GGMDLDILPQGAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDAELFSIPDVYGVM 219
Cdd:TIGR01484 154 GKTDLEVLPAGVNKGSALQALLQEL---NGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 11-259 2.48e-22

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: 93.66  E-value: 2.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  11 MIVSDLDHTMVDHH---DPENLSLLRfnslweHAYRHDSLLVFSTGRSPTLYKELRKEKPLltPDITIMSVGTEITYGNs 87
Cdd:COG0561   4 LIALDLDGTLLNDDgeiSPRTKEALR------RLREKGIKVVIATGRPLRSALPLLEELGL--DDPLITSNGALIYDPD- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  88 mvpdhgwvealnnkwdlgivkqeasnfpelklqaetEQRPHKVSFyvekskAQEVTKELSQRFLKRGLDV-KIIYSGGMD 166
Cdd:COG0561  75 ------------------------------------GEVLYERPL------DPEDVREILELLREHGLHLqVVVRSGPGF 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071 167 LDILPQGAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDAELFSIPDvYGVMVSNAQEELLKWHAENAKDNpkvihake 246
Cdd:COG0561 113 LEILPKGVSKGSALKKLAERL---GIPPEEVIAFGDSGNDLEMLEAAG-LGVAMGNAPPEVKAAADYVTGSN-------- 180

                       250
                ....*....|...
gi 42571071 247 rCAGGIIQAIGHF 259
Cdd:COG0561 181 -DEDGVAEALEKL 192
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 128-238 3.77e-16

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


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 76.08  E-value: 3.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071 128 HKVSFYVEKSKAQEVTKELSQRFLKRgldVKIIYSGGMDLDILPQGAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDA 207
Cdd:cd07518  71 FKFTLNVPDEAAPDIIDELNQKFGGI---LRAVTSGFGSIDIIPPGVNKATGLKQLLKHW---GISPDEVMAFGDGGNDI 144

                        90       100       110
                ....*....|....*....|....*....|..
gi 42571071 208 ELFSIPDvYGVMVSNAQEELLKwHAEN-AKDN 238
Cdd:cd07518 145 EMLKYAG-YSYAMENAPEEVKA-AAKYvAPSN 174
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 11-238 1.79e-14

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: 72.69  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    11 MIVSDLDHTMV--DHH-DPENLSLLRfnslwehAYRHDSL-LVFSTGRSPTLYKELRKEKPLLTPDIT-----IMSVGTE 81
Cdd:TIGR00099   1 LIFIDLDGTLLndDHTiSPSTKEALA-------KLREKGIkVVLATGRPYKEVKNILKELGLDTPFITangaaVIDDQGE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    82 ITYGNSMVPDHgwVEALNN--------------------KWDLGIVKQEASNFPELKLQAETEQRPH-----KVSFYVEK 136
Cdd:TIGR00099  74 ILYKKPLDLDL--VEEILNflkkhgldvilygddsiyasKNDPEYFTIFKKFLGEPKLEVVDIQYLPddilkILLLFLDP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   137 SKAQEVTKELSQRFLKrgLDVKIIYSGGMDLDILPQGAGKGQALAYLLKKLKTEgklPVNTLACGDSGNDAELFSIPDvY 216
Cdd:TIGR00099 152 EDLDLLIEALNKLELE--ENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGIS---LEDVIAFGDGMNDIEMLEAAG-Y 225

                         250       260
                  ....*....|....*....|..
gi 42571071   217 GVMVSNAQEELLKWHAENAKDN 238
Cdd:TIGR00099 226 GVAMGNADEELKALADYVTDSN 247
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 12-229 9.60e-14

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 70.73  E-value: 9.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    12 IVSDLDHTMVDHH---DPENLSLLRFnslwehAYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDIT-----IMSVGTEIT 83
Cdd:pfam08282   1 IASDLDGTLLNSDkkiSEKTKEAIKK------LKEKGIKFVIATGRPYRAILPVIKELGLDDPVICyngalIYDENGKIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    84 YGNSMVP----------------------DHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQR--PHKVSFYVEKSKA 139
Cdd:pfam08282  75 YSNPISKeavkeiieylkennleillytdDGVYILNDNELEKILKELNYTKSFVPEIDDFELLEDedINKILILLDEEDL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   140 QEVTKELSQRFlkrGLDVKIIYSGGMDLDILPQGAGKGQALAYLLKKLKTEGKlpvNTLACGDSGNDAELFSIPDvYGVM 219
Cdd:pfam08282 155 DELEKELKELF---GSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLE---EVIAFGDGENDIEMLEAAG-LGVA 227

                         250
                  ....*....|
gi 42571071   220 VSNAQEELLK 229
Cdd:pfam08282 228 MGNASPEVKA 237
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 11-227 7.52e-12

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: 64.92  E-value: 7.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  11 MIVSDLDHTMVDHH---DPENLSLLRFnslwehAYRHDSLLVFSTGRSPT----LYKELRKEKPLLT------------- 70
Cdd:cd07516   1 LIALDLDGTLLNSDkeiSPRTKEAIKK------AKEKGIKVVIATGRPLRgaqpYLEELGLDSPLITfngalvydptgke 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  71 -------PDITIM--SVGTEITYGNSMVPDHGWVEAL--NNKWDLGIVKQEASNFPELKLQAEteqrPHKVSFYVEKSKA 139
Cdd:cd07516  75 ilerlisKEDVKEleEFLRKLGIGINIYTNDDWADTIyeENEDDEIIKPAEILDDLLLPPDED----ITKILFVGEDEEL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071 140 QEVTKELSQRFLKrglDVKIIYSGGMDLDILPQGAGKGQALAYLLKKL--KTEgklpvNTLACGDSGNDAELFSIPDvYG 217
Cdd:cd07516 151 DELIAKLPEEFFD---DLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLgiSLE-----EVIAFGDNENDLSMLEYAG-LG 221

                       250
                ....*....|
gi 42571071 218 VMVSNAQEEL 227
Cdd:cd07516 222 VAMGNAIDEV 231
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 47-227 2.28e-08

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


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 54.15  E-value: 2.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  47 LLVFSTGRSPTLYKELRKEkplLTPDitimsvgTEITYGNSMVPDHGWVEAlNNKWDLGIVKqeasnfpelKLQAETEQR 126
Cdd:cd07517  35 LVVIATGRAPFEIQPIVKA---LGID-------SYVSYNGQYVFFEGEVIY-KNPLPQELVE---------RLTEFAKEQ 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071 127 PHKVSFYVEKSkaQEVTKELSQRFLKRGLDVKIIYSGGMDLDILPQGAGKGQALAYLLKKLkteGKLPVNTLACGDSGND 206
Cdd:cd07517  95 GHPVSFYGQLL--LFEDEEEEQKYEELRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHL---GIKKEETMAFGDGLND 169

                       170       180
                ....*....|....*....|.
gi 42571071 207 AELFSIPDvYGVMVSNAQEEL 227
Cdd:cd07517 170 IEMLEAVG-IGIAMGNAHEEL 189
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 12-260 3.19e-08

mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Several members of this family from thermophiles (and from Dehalococcoides ethenogenes) are now known to act as mannosyl-3-phosphoglycerate (MPG) phosphatase. In these cases, the enzyme acts after MPG synthase to make the compatible solute mannosylglycerate. We propose that other mesophilic members of this family do not act as mannosyl-3-phosphoglycerate phosphatase. A member of this family is found in Escherichia coli, which appears to lack MPG synthase. Mannosylglycerate is imported in E. coli by phosphoenolpyruvate-dependent transporter (), but it appears the phosphorylation is not on the glycerate moiety, that the phosphorylated import is degraded by an alpha-mannosidase from an adjacent gene, and that E. coli would have no pathway to obtain MPG.


Pssm-ID: 130550 [Multi-domain]  Cd Length: 256  Bit Score: 54.33  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    12 IVSDLDHTMVDHH----DPENLSLLRfnsLWEHAYRhdslLVFSTGRSPTLYKELRKEkpLLTPDITIMSVGTEItYG-- 85
Cdd:TIGR01486   2 IFTDLDGTLLDPHgydwGPAKEVLER---LQELGIP----VIPCTSKTAAEVEYLRKE--LGLEDPFIVENGGAI-YGpr 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    86 NSMVPDHGWVEALNNKWdlGIVKqeasnfPELKLQAETEQRPHKVSFYVEKSKAQEVT---KELSQRFLKRGLDVKII-- 160
Cdd:TIGR01486  72 GWRPEPEYPVIALGIPY--EKIR------ARLRELSEELGFKFRGLGDLTDEEIAELTglsRELARLAQRREYSETILws 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071   161 ------------------YSGGMDLDILPQGAGKGQALAYLLKKLKTEGKLPVnTLACGDSGNDAELFSIPDvYGVMVSN 222
Cdd:TIGR01486 144 eerrerftealvavglevTHGGRFYHVLGAGSDKGKAVNALKAFYNQPGGAIK-VVGLGDSPNDLPLLEVVD-LAVVVPG 221

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 42571071   223 AQEELLKWHAENAkdnPKVIHAKERCAGGIIQAIGHFK 260
Cdd:TIGR01486 222 PNGPNVSLKPGDP---GSFLLTPAPGPEGWREALEHLL 256
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 114-261 9.01e-07

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 49.59  E-value: 9.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  114 FPELKLQAET---EQRPHKVSFY--VEKSKAQEVTKELsqrflkrGLDVKIIYSGgMDLDILPQGAGKGQALAYLLKKLK 188
Cdd:PRK01158  99 FPEASTSLTKldpDYRKTEVALRrtVPVEEVRELLEEL-------GLDLEIVDSG-FAIHIKSPGVNKGTGLKKLAELMG 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571071  189 TEgklPVNTLACGDSGNDAELFSIPdVYGVMVSNAQEELlkwhAENAKdnpkviHAKERCAG-GIIQAIGHFKL 261
Cdd:PRK01158 171 ID---PEEVAAIGDSENDLEMFEVA-GFGVAVANADEEL----KEAAD------YVTEKSYGeGVAEAIEHLLL 230
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 173-229 4.83e-06

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: 46.04  E-value: 4.83e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571071 173 GAGKGQALAYLLKKLkteGKLPVNTLACGDSGNDAELFSIPdVYGVMVSNAQEELLK 229
Cdd:cd07514  65 GVDKGTGLEKLAERL---GIDPEEVLAIGDSENDIEMFKVA-GFKVAVANADEELKE 117
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 173-246 2.74e-05

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 45.59  E-value: 2.74e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571071 173 GAGKGQALAYLLKKLKTEGKLPVNTLACGDSGNDAELFSIPDvYGVMVSNAQEELLkwhaeNAKDNPKVIHAKE 246
Cdd:COG3769 186 GADKGKAVRWLVEQYRQRFGKNVVTIALGDSPNDIPMLEAAD-IAVVIRSPHGAPP-----ELEDKPRVIRTPA 253
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 125-215 7.46e-04

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: 40.81  E-value: 7.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071 125 QRPHKVSFYVEKS--KAQEVTKELSQRFLKrgldvkiIYSGGMDLDILPQGAGKGQALAYLLKKLKTEGKLPVnTLACGD 202
Cdd:cd07507 140 EREYSETIILRSDeeEDEKVLEALEERGLK-------ITKGGRFYHVLGAGADKGKAVAILAALYRQLYEAIV-TVGLGD 211

                        90
                ....*....|...
gi 42571071 203 SGNDAELFSIPDV 215
Cdd:cd07507 212 SPNDLPMLEAVDI 224
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 101-256 8.45e-04

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 41.69  E-value: 8.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    101 KWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKIIYS-GGMDLDILPQGAGKGQA 179
Cdd:TIGR02468  881 KWAASINEKKGENEEQIVEEDEESSTDHCYAFKVKDPSKVPPVKELRKLLRIQGLRCHAVYCrNGTRLNVIPLLASRSQA 960

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071    180 LAYLLKKLKTE-GKLPVNTLACGDSGNDaELFSipdvyGV--------MVSNAQEELlkwHAEN--------AKDNPKVI 242
Cdd:TIGR02468  961 LRYLFVRWGIElANMAVFVGESGDTDYE-GLLG-----GLhktvilkgVVSRGSEQL---HANRsyplddvvPLDSPNIV 1031

                          170
                   ....*....|....
gi 42571071    243 HAKERCAGGIIQAI 256
Cdd:TIGR02468 1032 QATGGSSSDDISDA 1045
PRK03669 PRK03669
mannosyl-3-phosphoglycerate phosphatase-related protein;
169-259 5.97e-03

mannosyl-3-phosphoglycerate phosphatase-related protein;


Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 38.46  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571071  169 ILPQGAGKGQALAYLLKKL-KTEGKLPVnTLACGDSGNDAELFSIPDvYGVMVSNAQEELLKWHAEnakDNPKVIHAKER 247
Cdd:PRK03669 181 VLDASAGKDQAANWLIATYqQLSGTRPT-TLGLGDGPNDAPLLDVMD-YAVVVKGLNREGVHLQDD---DPARVYRTQRE 255

                         90
                 ....*....|..
gi 42571071  248 CAGGIIQAIGHF 259
Cdd:PRK03669 256 GPEGWREGLDHF 267
HAD_like cd07520
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 163-218 6.26e-03

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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: 319822  Cd Length: 144  Bit Score: 37.04  E-value: 6.26e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571071 163 GGMDLDILPQGAGKGQALAYLLKKLKTEGKLPvnTLACGDSGNDAELFSIPDVYGV 218
Cdd:cd07520  90 GEPDPEWLPRPVGKAQAVRWLLERHLFPGARP--TLGFGDSLSDLGFMRLCDWAGT 143
 
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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