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Conserved domains on  [gi|1668100059|ref|WP_138128258|]
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HAD hydrolase-like protein [Streptococcus dysgalactiae]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 3-208 2.52e-88

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd04302:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 209  Bit Score: 259.06  E-value: 2.52e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFF-ENKDQVEQAILHFRAFYKESGIHQV 81
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLpFDEEEAQRAVDAYREYYKEKGLFEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  82 SVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGST--SVRYHKADVIQACLQTMSTSAQNPIII 159
Cdd:cd04302    81 EVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASldGSRVHKADVIRYALDTLGIAPEQAVMI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1668100059 160 GDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLL 208
Cdd:cd04302   161 GDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLELL 209
 
Name Accession Description Interval E-value
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 3-208 2.52e-88

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 259.06  E-value: 2.52e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFF-ENKDQVEQAILHFRAFYKESGIHQV 81
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLpFDEEEAQRAVDAYREYYKEKGLFEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  82 SVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGST--SVRYHKADVIQACLQTMSTSAQNPIII 159
Cdd:cd04302    81 EVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASldGSRVHKADVIRYALDTLGIAPEQAVMI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1668100059 160 GDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLL 208
Cdd:cd04302   161 GDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLELL 209
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1-209 3.62e-65

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 200.16  E-value: 3.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   1 MTAILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFF--ENKDQVEQAILHFRAFYKESGI 78
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLgeDPDEELEELLARFRELYEEELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  79 HQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQACLQTMSTSAQNP 156
Cdd:COG0546    81 DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKpkPEPLLEALERLGLDPEEV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1668100059 157 IIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLLQ 209
Cdd:COG0546   161 LMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLALLA 213
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
4-179 2.08e-38

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 130.78  E-value: 2.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   4 ILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFFENKDqVEQAILHFRAFYKESGIHQ-VS 82
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSED-EEEKIEFYLRKYNEELHDKlVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  83 VYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQACLQTMSTSAQNPIIIG 160
Cdd:pfam13419  80 PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKpdPDPILKALEQLGLKPEEVIYVG 159

                         170
                  ....*....|....*....
gi 1668100059 161 DTKFDIIGGKQANLTTIGV 179
Cdd:pfam13419 160 DSPRDIEAAKNAGIKVIAV 178
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 2-208 1.70e-34

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 122.06  E-value: 1.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   2 TAILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFfeNKDQVEQAILHFRAFYKESGIHQV 81
Cdd:PRK13288    4 NTVLFDLDGTLINTNELIISSFLHTLKTYYPNQYKREDVLPFIGPSLHDTFSKI--DESKVEEMITTYREFNHEHHDELV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  82 SVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD--VIQACLQTMSTSAQNPIII 159
Cdd:PRK13288   82 TEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDpePVLKALELLGAKPEEALMV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1668100059 160 GDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLL 208
Cdd:PRK13288  162 GDNHHDILAGKNAGTKTAGVAWTIKGREYLEQYKPDFMLDKMSDLLAIV 210
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 4-208 6.42e-21

2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702). [Energy metabolism, Sugars]


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 86.41  E-value: 6.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   4 ILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIG---PPL-ETTFRAFFENKDQVEQAIL--HFRAFYKESG 77
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGLPPATLARVIGFIGngvPVLmERVLAWAGQEPDAQRVAELrkLFDRHYEEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  78 IHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD---VIQAClQTMSTSAQ 154
Cdd:TIGR01449  81 GELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHpdpLLLAA-ERLGVAPQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1668100059 155 NPIIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLL 208
Cdd:TIGR01449 160 QMVYVGDSRVDIQAARAAGCPSVLLTYGYRYGEAIDLLPPDVLYDSLNELPPLL 213
 
Name Accession Description Interval E-value
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 3-208 2.52e-88

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 259.06  E-value: 2.52e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFF-ENKDQVEQAILHFRAFYKESGIHQV 81
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLpFDEEEAQRAVDAYREYYKEKGLFEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  82 SVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGST--SVRYHKADVIQACLQTMSTSAQNPIII 159
Cdd:cd04302    81 EVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASldGSRVHKADVIRYALDTLGIAPEQAVMI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1668100059 160 GDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLL 208
Cdd:cd04302   161 GDRKHDIIGARANGIDSIGVLYGYGSEDELEEAGATYIVETPAELLELL 209
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1-209 3.62e-65

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 200.16  E-value: 3.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   1 MTAILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFF--ENKDQVEQAILHFRAFYKESGI 78
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLgeDPDEELEELLARFRELYEEELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  79 HQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQACLQTMSTSAQNP 156
Cdd:COG0546    81 DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKpkPEPLLEALERLGLDPEEV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1668100059 157 IIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLLQ 209
Cdd:COG0546   161 LMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYVIDSLAELLALLA 213
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 2-207 1.89e-48

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 157.44  E-value: 1.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   2 TAILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFfeNKDQVEQAILHFRAFYKESGIHQV 81
Cdd:cd02616     2 TTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGPPLRETFEKI--DPDKLEDMVEEFRKYYREHNDDLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  82 SVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD---VIQAcLQTMSTSAQNPII 158
Cdd:cd02616    80 KEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDpepVLKA-LELLGAEPEEALM 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1668100059 159 IGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTL 207
Cdd:cd02616   159 VGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFNPDFIIDKMSDLLTI 207
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
4-179 2.08e-38

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 130.78  E-value: 2.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   4 ILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFFENKDqVEQAILHFRAFYKESGIHQ-VS 82
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSED-EEEKIEFYLRKYNEELHDKlVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  83 VYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQACLQTMSTSAQNPIIIG 160
Cdd:pfam13419  80 PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKpdPDPILKALEQLGLKPEEVIYVG 159

                         170
                  ....*....|....*....
gi 1668100059 161 DTKFDIIGGKQANLTTIGV 179
Cdd:pfam13419 160 DSPRDIEAAKNAGIKVIAV 178
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 2-208 1.70e-34

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 122.06  E-value: 1.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   2 TAILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFfeNKDQVEQAILHFRAFYKESGIHQV 81
Cdd:PRK13288    4 NTVLFDLDGTLINTNELIISSFLHTLKTYYPNQYKREDVLPFIGPSLHDTFSKI--DESKVEEMITTYREFNHEHHDELV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  82 SVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD--VIQACLQTMSTSAQNPIII 159
Cdd:PRK13288   82 TEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDpePVLKALELLGAKPEEALMV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1668100059 160 GDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLL 208
Cdd:PRK13288  162 GDNHHDILAGKNAGTKTAGVAWTIKGREYLEQYKPDFMLDKMSDLLAIV 210
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-212 1.15e-32

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 117.60  E-value: 1.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   1 MTAILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIG---PPL-ETTFRAFFE--NKDQVEQAILHFRAFYK 74
Cdd:PRK13222    6 IRAVAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVRTWVGngaDVLvERALTWAGRepDEELLEKLRELFDRHYA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  75 ESgIHQVS-VYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQACLQTMST 151
Cdd:PRK13222   86 EN-VAGGSrLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKpdPAPLLLACEKLGL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1668100059 152 SAQNPIIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLLQNLS 212
Cdd:PRK13222  165 DPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYNYGEPIALSEPDVVIDHFAELLPLLGLAL 225
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 3-198 7.85e-28

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 104.62  E-value: 7.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLE-------TTFRAFFENKDQVEQAILHFRAFYKE 75
Cdd:cd16417     1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEETVRTWIGNGADvlveralTGAREAEPDEELFKEARALFDRHYAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  76 SGIHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD--VIQACLQTMSTSA 153
Cdd:cd16417    81 TLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDpaPLLHACEKLGIAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1668100059 154 QNPIIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIV 198
Cdd:cd16417   161 AQMLMVGDSRNDILAARAAGCPSVGLTYGYNYGEDIAASGPDAVI 205
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-198 7.91e-28

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 104.52  E-value: 7.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   1 MTAILFDLDGTLVDSSPGILNAFQYTFKQMNhIVPDASLLSTYIGPPLETTFRAFFE--NKDQVEQAIL-----HFRAFY 73
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAELG-IDLTEEEYRRLMGRSREDILRYLLEeyGLDLPEEELAarkeeLYRELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  74 KESGIHqvsVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQACLQTMST 151
Cdd:COG0637    81 AEEGLP---LIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKpdPDIYLLAAERLGV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1668100059 152 SAQNPIIIGDTKFDIIGGKQANLTTIGVTwgFGSQEELQLSKADYIV 198
Cdd:COG0637   158 DPEECVVFEDSPAGIRAAKAAGMRVVGVP--DGGTAEEELAGADLVV 202
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 1-208 2.47e-22

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 90.47  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   1 MTAILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIG---------PPLETTFRAFFE------NKDQVEQA 65
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAieyalwrryERGEITFAELLRrlleelGLDLAEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  66 ILHFRAFYKESgihqVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQ 143
Cdd:COG1011    81 AEAFLAALPEL----VEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKpdPEIFE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1668100059 144 ACLQTMSTSAQNPIIIGDT-KFDIIGGKQANLTTIGVTwGFGSQEELQLsKADYIVKQPLDIYTLL 208
Cdd:COG1011   157 LALERLGVPPEEALFVGDSpETDVAGARAAGMRTVWVN-RSGEPAPAEP-RPDYVISDLAELLELL 220
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 3-184 2.11e-21

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 87.76  E-value: 2.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAfqytfkqMNHIVPDASLlstyiGPPLETTFRAFF----------------ENKDQVEQAI 66
Cdd:cd07512     1 AVIFDLDGTLIDSAPDLHAA-------LNAVLAAEGL-----APLSLAEVRSFVghgapalirrafaaagEDLDGPLHDA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  67 LH--FRAFYKESGIHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD--VI 142
Cdd:cd07512    69 LLarFLDHYEADPPGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDpaPL 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1668100059 143 QACLQTMSTSAQNPIIIGDTKFDIIGGKQANLTTIGVTWGFG 184
Cdd:cd07512   149 RAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYR 190
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 4-208 6.42e-21

2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702). [Energy metabolism, Sugars]


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 86.41  E-value: 6.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   4 ILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIG---PPL-ETTFRAFFENKDQVEQAIL--HFRAFYKESG 77
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGLPPATLARVIGFIGngvPVLmERVLAWAGQEPDAQRVAELrkLFDRHYEEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  78 IHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD---VIQAClQTMSTSAQ 154
Cdd:TIGR01449  81 GELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHpdpLLLAA-ERLGVAPQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1668100059 155 NPIIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDIYTLL 208
Cdd:TIGR01449 160 QMVYVGDSRVDIQAARAAGCPSVLLTYGYRYGEAIDLLPPDVLYDSLNELPPLL 213
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 4-198 4.08e-18

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 78.98  E-value: 4.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   4 ILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFFEnkdQVEQAILHFRAFYKESGI----- 78
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRSIIGLSLDEAIARLLP---MATPALVAVAERYKEAFDilrll 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  79 --HQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYF--TGVFGSTSVRYHKADVIQACLQTmSTSAQ 154
Cdd:cd07533    79 peHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFdaTRTADDTPSKPHPEMLREILAEL-GVDPS 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1668100059 155 NPIIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIV 198
Cdd:cd07533   158 RAVMVGDTAYDMQMAANAGAHAVGVAWGYHSLEDLRSAGADAVV 201
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 1-173 4.78e-18

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 78.40  E-value: 4.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   1 MTAILFDLDGTLVDSSPGILNAFQYT------FKQMNHIVPDASLLSTYIGPPLETTFRAFFENKDQVEQAILHFRAFYK 74
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELasehplAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  75 ES----------GIHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVI 142
Cdd:pfam00702  81 TVvlvellgviaLADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKpkPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1668100059 143 QACLQTMSTSAQNPIIIGDTKFDIIGGKQAN 173
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 3-204 1.48e-14

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 69.31  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSP---GILN--AFQYTFKQMN-HIVPDASLLST-----YIGPPLEttfraffenkdQVEQAILHFRA 71
Cdd:cd04303     1 LIIFDFDGTLADSFPwflSILNqlAARHGFKTVDeEEIEQLRQLSSreilkQLGVPLW-----------KLPLIAKDFRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  72 FYKESgIHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTgVFGSTSVrYHKADVIQACLQTMST 151
Cdd:cd04303    70 LMAEA-APELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFA-VIEGSSL-FGKAKKIRRVLRRTKI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1668100059 152 SAQNPIIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDI 204
Cdd:cd04303   147 TAAQVIYVGDETRDIEAARKVGLAFAAVSWGYAKPEVLKALAPDHMLEDPEDL 199
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 3-179 1.47e-13

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 65.90  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKqmnHIVPDASLLSTYIGPPLetTFRAFFENKDQVEQAILhFRAFYKESGIHQ-- 80
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREEL---GLVPDELGVSAVGRLEL--ALRRFKAQYGRTISPED-AQLLYKQLFYEQie 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  81 ----VSVYDDIETLLRTLVQEGFDLYVTTSKHePMAIQMLTNLGIADYFTGVFGSTSVRYHKADV--IQACLQTMSTSAQ 154
Cdd:TIGR01509  75 eeakLKPLPGVRALLEALRARGKKLALLTNSP-RAHKLVLALLGLRDLFDVVIDSSDVGLGKPDPdiYLQALKALGLEPS 153

                         170       180
                  ....*....|....*....|....*
gi 1668100059 155 NPIIIGDTKFDIIGGKQANLTTIGV 179
Cdd:TIGR01509 154 ECVFVDDSPAGIEAAKAAGMHTVGV 178
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 2-179 2.80e-13

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 65.44  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   2 TAILFDLDGTLVDSSP-------GILNAFQYTF-KQMNHIVPdasllstyiGPPLETTFRAFFE------NKDQVEQAIL 67
Cdd:TIGR02009   2 KAVIFDMDGVITDTAPlhaqawkHIAAKYGISFdKQYNESLK---------GLSREDILRAILKlrgdglSLEEIHQLAE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  68 HFRAFYKESGIHQVS-VYDDIETLLRTLVQEGFDLYVTTSKHEpmAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQA 144
Cdd:TIGR02009  73 RKNELYRELLRLTGVaVLPGIRNLLKRLKAKGIAVGLGSSSKN--APRILAKLGLRDYFDAIVDASEVKNGKphPETFLL 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1668100059 145 CLQTMSTSAQNPIIIGDTKFDIIGGKQANLTTIGV 179
Cdd:TIGR02009 151 AAELLGVPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 3-177 1.09e-12

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 63.55  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQMNhivpdasllstyIGPPLETTFRAFFENKDQ-VEQ--AILH-FRAFYKESG- 77
Cdd:cd07523     1 NFIWDLDGTLLDSYPAMTKALSETLADFG------------IPQDLETVYKIIKESSVQfAIQyyAEVPdLEEEYKELEa 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  78 --IHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPmAIQMLTNLGIADYFTGVFGSTS--VRYHKADVIQACLQTMSTSA 153
Cdd:cd07523    69 eyLAKPILFPGAKAVLRWIKEQGGKNFLMTHRDHS-ALTILKKDGIASYFTEIVTSDNgfPRKPNPEAINYLLNKYQLNP 147

                         170       180
                  ....*....|....*....|....
gi 1668100059 154 QNPIIIGDTKFDIIGGKQANLTTI 177
Cdd:cd07523   148 EETVMIGDRELDIEAGHNAGISTI 171
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 87-179 3.50e-12

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 60.49  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  87 IETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQACLQTMSTSAQNPIIIGDTKF 164
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKpkPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                          90
                  ....*....|....*
gi 1668100059 165 DIIGGKQANLTTIGV 179
Cdd:cd01427    92 DIEAARAAGGRTVAV 106
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 3-173 4.68e-12

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 61.64  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDAS-LLSTYIGPPLETTFRAFFENKDQVEQAILHFRAFYKEsgihqv 81
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKaLKQAGGLAEEEWYRIATSALEELQGRFWSEYDAEEAY------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  82 svYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGStSVRYHKAD--VIQACLQTMSTSAQnPIII 159
Cdd:TIGR01549  75 --IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVS-DEPGSKPEpeIFLAALESLGVPPE-VLHV 150

                         170
                  ....*....|....
gi 1668100059 160 GDTKFDIIGGKQAN 173
Cdd:TIGR01549 151 GDNLNDIEGARNAG 164
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 3-206 8.73e-11

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 59.48  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFFENKDQVEQAIL--HFRAFYkESGIHQ 80
Cdd:PRK13226   14 AVLFDLDGTLLDSAPDMLATVNAMLAARGRAPITLAQLRPVVSKGARAMLAVAFPELDAAARDALipEFLQRY-EALIGT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  81 VSV-YDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKADVI--QACLQTMSTSAQNPI 157
Cdd:PRK13226   93 QSQlFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLplLVAAERIGVAPTDCV 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1668100059 158 IIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLS-KADYIVKQPLDIYT 206
Cdd:PRK13226  173 YVGDDERDILAARAAGMPSVAALWGYRLHDDDPLAwQADVLVEQPQLLWN 222
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 4-183 2.31e-10

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 58.72  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   4 ILFDLDGTLVDSSPGILNAFQYTFKQMNHivPDASLLST--YIGPPLETTFRAFFEN--------KDQVEQAILHFRAFY 73
Cdd:PRK13223   16 VMFDLDGTLVDSVPDLAAAVDRMLLELGR--PPAGLEAVrhWVGNGAPVLVRRALAGsidhdgvdDELAEQALALFMEAY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  74 KESgiHQVS-VYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD--VIQACLQTMS 150
Cdd:PRK13223   94 ADS--HELTvVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDpaALLFVMKMAG 171

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1668100059 151 TSAQNPIIIGDTKFDIIGGKQANLTTIGVTWGF 183
Cdd:PRK13223  172 VPPSQSLFVGDSRSDVLAAKAAGVQCVALSYGY 204
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 3-180 3.15e-10

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 56.09  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQytfkqmnhivpdasllstyigpplettfraFFENKDQVEQAILHFrafykesgiHQVS 82
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAWQ------------------------------LLERKNALLLELIAS---------EGLK 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  83 VYDDIETLLRTLVQEGFDL-YVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKA--DVIQACLQTMSTSAQNPIII 159
Cdd:cd07505    42 LKPGVVELLDALKAAGIPVaVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPapDIYLLAAERLGVDPERCLVF 121

                         170       180
                  ....*....|....*....|.
gi 1668100059 160 GDTKFDIIGGKQANLTTIGVT 180
Cdd:cd07505   122 EDSLAGIEAAKAAGMTVVAVP 142
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 3-204 6.04e-07

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 48.11  E-value: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQmnHIVPDASLLSTYIGPPLETTFRAFFENKDQVEqAILHFRAFYKESGIHQVS 82
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKE--HGVDPEEVLKVSHGRRAIDVIRKLAPDDADIE-LVLALETEEPESYPEGVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  83 VYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIA--DYFTGVFgstSVRYHKAD---VIQAcLQTMSTSAQNPI 157
Cdd:cd07527    78 AIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGLPhpEVLVTAD---DVKNGKPDpepYLLG-AKLLGLDPSDCV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1668100059 158 IIGDTKFDIIGGKQANLTTIGVTWGFgSQEELQLSKADYIVKQPLDI 204
Cdd:cd07527   154 VFEDAPAGIKAGKAAGARVVAVNTSH-DLEQLEAAGADLVVEDLSDI 199
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 84-177 2.78e-06

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 44.46  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  84 YDDIETLLRTLvQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD--VIQACLQTMSTSAQNPIIIGD 161
Cdd:cd04305    11 LPGAKELLEEL-KKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNpeIFDYALNQLGVKPEETLMVGD 89

                          90
                  ....*....|....*..
gi 1668100059 162 T-KFDIIGGKQANLTTI 177
Cdd:cd04305    90 SlESDILGAKNAGIKTV 106
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 1-182 8.45e-06

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 45.22  E-value: 8.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   1 MTAILFDLDGTLVDSSPGILNAFQYTFKQMNHivpdasllstYIGPPLETTFraFFEN---KDQVEQAILHFRAFYkESG 77
Cdd:PLN02770   22 LEAVLFDVDGTLCDSDPLHYYAFREMLQEINF----------NGGVPITEEF--FVENiagKHNEDIALGLFPDDL-ERG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  78 IhqvSVYDDIETLLRTLVQE------------------GFDLYVTTSKHEPMAIQMLTNLGIADYFTGV-FGSTSVRY-- 136
Cdd:PLN02770   89 L---KFTDDKEALFRKLASEqlkplnglyklkkwiedrGLKRAAVTNAPRENAELMISLLGLSDFFQAViIGSECEHAkp 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1668100059 137 HKADVIQAcLQTMSTSAQNPIIIGDTKFDIIGGKQANLTTIGVTWG 182
Cdd:PLN02770  166 HPDPYLKA-LEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTR 210
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 1-214 3.86e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 43.55  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   1 MTAILFDLDGTLVDSSP---GILNAFQYTFKQMNHIVPDASLLSTYIGpplETTFRAffENKDQVEQAILHFRAfYKESG 77
Cdd:PRK13225   62 LQAIIFDFDGTLVDSLPtvvAIANAHAPDFGYDPIDERDYAQLRQWSS---RTIVRR--AGLSPWQQARLLQRV-QRQLG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  78 --IHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKadviQACLQTMSTSAQN 155
Cdd:PRK13225  136 dcLPALQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQRQGLRSLFSVVQAGTPILSKR----RALSQLVAREGWQ 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1668100059 156 P---IIIGDTKFDIIGGKQANLTTIGVTWGFGSQEELQLSKADYIVKQPLDiytLLQNLSTL 214
Cdd:PRK13225  212 PaavMYVGDETRDVEAARQVGLIAVAVTWGFNDRQSLVAACPDWLLETPSD---LLQAVTQL 270
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-166 4.46e-05

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 42.52  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   4 ILFDLDGTLVDSSPGILnaFQYTFKQMNHIVPDASLLSTYIGPPLETTFRAFFENKDQVEQAIL---------HFRAFYK 74
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFL--LIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLaglpeedaaELERFVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  75 EsgIHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGI-----------ADYFTG---VFGSTSVRYHKAD 140
Cdd:pfam12710  79 E--VALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFdevlatelevdDGRFTGelrLIGPPCAGEGKVR 156

                         170       180
                  ....*....|....*....|....*...
gi 1668100059 141 VIQACLQT--MSTSAQNPIIIGDTKFDI 166
Cdd:pfam12710 157 RLRAWLAArgLGLDLADSVAYGDSPSDL 184
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 3-140 4.99e-05

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 42.64  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQMNHIVPD-------ASLLSTYIGPplettFRAFFENKDQVEQAIL-HFRAFYK 74
Cdd:cd02588     2 ALVFDVYGTLIDWHSGLAAAERAFPGRGEELSRLwrqkqleYTWLVTLMGP-----YVDFDELTRDALRATAaELGLELD 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1668100059  75 ES-------GIHQVSVYDDIETLLRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD 140
Cdd:cd02588    77 ESdldelgdAYLRLPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPA 149
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
3-179 5.72e-05

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 42.37  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   3 AILFDLDGTLVDSSPGILNAFQYTFKQ--MNHivpDASLLSTYIGPPletTFRaffenkdqVEQAIL---------HFRA 71
Cdd:PRK10725    7 GLIFDMDGTILDTEPTHRKAWREVLGRygLQF---DEQAMVALNGSP---TWR--------IAQAIIelnqadldpHALA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  72 FYKESGIHQVsVYDDIETL-LRTLVQEGFD---LYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHK--ADVIQAC 145
Cdd:PRK10725   73 REKTEAVKSM-LLDSVEPLpLIEVVKAWHGrrpMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKpaPDTFLRC 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1668100059 146 LQTMSTSAQNPIIIGDTKFDIIGGKQANLTTIGV 179
Cdd:PRK10725  152 AQLMGVQPTQCVVFEDADFGIQAARAAGMDAVDV 185
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 4-177 3.10e-04

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 40.55  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059   4 ILFDLDGTLVDSSPGILNAFQYTFKQMNhIVPDASLLSTY--IGPPLETTFRAFFENKDQVEQAilHFRAFYKESGIHQ- 80
Cdd:TIGR02254   4 LLFDLDDTILDFQAAEALALRLLFEDQG-IPLTEDMFAQYkeINQGLWRAYEEGKITKDEVVNT--RFSALLKEYNTEAd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668100059  81 --------VSVYDDIETL------LRTLVQEGFDLYVTTSKHEPMAIQMLTNLGIADYFTGVFGSTSVRYHKAD--VIQA 144
Cdd:TIGR02254  81 eallnqkyLRFLEEGHQLlpgafeLMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDkeIFNY 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1668100059 145 CLQTMST-SAQNPIIIGDT-KFDIIGGKQANLTTI 177
Cdd:TIGR02254 161 ALERMPKfSKEEVLMIGDSlTADIKGGQNAGLDTC 195
Hydrolase_like pfam13242
HAD-hyrolase-like;
146-199 3.92e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 37.98  E-value: 3.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1668100059 146 LQTMSTSAQNPIIIGDTK-FDIIGGKQANLTTIGVTWGFGSQEELQLS--KADYIVK 199
Cdd:pfam13242  14 LARLGLDPERTVMIGDRLdTDILGAREAGARTILVLTGVTRPADLEKApiRPDYVVD 70
 
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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