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Conserved domains on  [gi|2787376968|ref|WP_370463859|]
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beta-phosphoglucomutase [Leclercia sp. J807]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bPGM super family cl33302
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 4-190 1.92e-92

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


The actual alignment was detected with superfamily member TIGR01990:

Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 268.79  E-value: 1.92e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLLRILRHGGKEqtFDHQQRLALASKKNDLYVQ 83
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKK--YSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHESLLPGIREVLEDIRAADVRIGLASVSLNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKVHP 163
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 2787376968 164 KEAIGIEDAAAGVEAINAAGMLSVGIG 190
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 4-190 1.92e-92

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 268.79  E-value: 1.92e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLLRILRHGGKEqtFDHQQRLALASKKNDLYVQ 83
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKK--YSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHESLLPGIREVLEDIRAADVRIGLASVSLNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKVHP 163
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 2787376968 164 KEAIGIEDAAAGVEAINAAGMLSVGIG 190
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-206 2.52e-62

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 193.12  E-value: 2.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   1 MLKAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLLRILRHGGKEQTFDhqqrlALASKKNDL 80
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEE-----ELAARKEEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  81 YVQSLAsLTHESLLPGIREVLEDIRAADVRIGLASVSL--NAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAG 158
Cdd:COG0637    76 YRELLA-EEGLPLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAER 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2787376968 159 LKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPG------LDRAGLQLHSTREL 206
Cdd:COG0637   155 LGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGgtaeeeLAGADLVVDDLAEL 208
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 4-208 7.86e-61

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include 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. 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 188.27  E-value: 7.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQevgitidesfneelkgisrmdsllrilrhggkeqtfdhqqRLALASKKNDLYVQ 83
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAWKKLAD----------------------------------------KEELAARKNRIYVE 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHESLLPGIREVLEDIRAADVRIGLASVSLNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKVHP 163
Cdd:cd02598    41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2787376968 164 KEAIGIEDAAAGVEAINAAGMLSVGIGPGLDRAG---LQLHSTRELTW 208
Cdd:cd02598   121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGadiVVPDTTADLTI 168
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-183 1.05e-24

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: 96.12  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   2 LKAIIFDLDGVITDTAHLHFLAWRAVAQEvgITIDESFNEELKGISR-MDSLLRILRHGG----KEQTFDHQQRLALASK 76
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASE--HPLAKAIVAAAEDLPIpVEDFTARLLLGKrdwlEELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  77 KNDLYVQSLASL----THESLLPGIREVLEDIRAADVRIGLAS--VSLNAPGILHALGIEQAFDFCADASRITCSKPHPE 150
Cdd:pfam00702  79 GLTVVLVELLGVialaDELKLYPGAAEALKALKERGIKVAILTgdNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2787376968 151 IFLAACAGLKVHPKEAIGIEDAAAGVEAINAAG 183
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-207 4.88e-20

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 84.61  E-value: 4.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   1 MLKAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIdeSFNEELKgisrmDSL-LRIlrhggkEQTFDH-QQRLALASKKN 78
Cdd:PRK10826    6 QILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDI--SRREELP-----DTLgLRI------DQVVDLwYARQPWNGPSR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  79 DLYVQSL----ASLTHES--LLPGIREVLEDIRAADVRIGLASVS----LNApgILHALGIEQAFDFCADASRITCSKPH 148
Cdd:PRK10826   73 QEVVQRIiarvISLIEETrpLLPGVREALALCKAQGLKIGLASASplhmLEA--VLTMFDLRDYFDALASAEKLPYSKPH 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787376968 149 PEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPGLDR-------AGLQLHSTRELT 207
Cdd:PRK10826  151 PEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQQndprwalADVKLESLTELT 216
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 4-190 1.92e-92

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 268.79  E-value: 1.92e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLLRILRHGGKEqtFDHQQRLALASKKNDLYVQ 83
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKK--YSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHESLLPGIREVLEDIRAADVRIGLASVSLNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKVHP 163
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 2787376968 164 KEAIGIEDAAAGVEAINAAGMLSVGIG 190
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 2-189 6.24e-70

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: 211.82  E-value: 6.24e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   2 LKAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLLRILRHGGKEqtFDHQQRLALASKKNDLY 81
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDG--LSLEEIHQLAERKNELY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  82 VQSLaSLTHESLLPGIREVLEDIRAADVRIGLASVSLNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKV 161
Cdd:TIGR02009  79 RELL-RLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGV 157

                         170       180
                  ....*....|....*....|....*...
gi 2787376968 162 HPKEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:TIGR02009 158 PPNECIVFEDALAGVQAARAAGMFAVAV 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-206 2.52e-62

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 193.12  E-value: 2.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   1 MLKAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLLRILRHGGKEQTFDhqqrlALASKKNDL 80
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEE-----ELAARKEEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  81 YVQSLAsLTHESLLPGIREVLEDIRAADVRIGLASVSL--NAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAG 158
Cdd:COG0637    76 YRELLA-EEGLPLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAER 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2787376968 159 LKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPG------LDRAGLQLHSTREL 206
Cdd:COG0637   155 LGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGgtaeeeLAGADLVVDDLAEL 208
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 4-208 7.86e-61

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include 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. 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 188.27  E-value: 7.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQevgitidesfneelkgisrmdsllrilrhggkeqtfdhqqRLALASKKNDLYVQ 83
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAWKKLAD----------------------------------------KEELAARKNRIYVE 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHESLLPGIREVLEDIRAADVRIGLASVSLNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKVHP 163
Cdd:cd02598    41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2787376968 164 KEAIGIEDAAAGVEAINAAGMLSVGIGPGLDRAG---LQLHSTRELTW 208
Cdd:cd02598   121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGadiVVPDTTADLTI 168
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 4-189 1.21e-34

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: 121.37  E-value: 1.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHflAWRAVAQEVGITIDESFNEELkgiSRMDslLRILRHGGKEQTFDHQQRLALAsKKNDLYVQ 83
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAI--AKLINREELGLVPDELGVSAV---GRLE--LALRRFKAQYGRTISPEDAQLL-YKQLFYEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLThESLLPGIREVLEDIRAADVRIGLASvslNAPGILHA----LGIEQAFDFCADASRITCSKPHPEIFLAACAGL 159
Cdd:TIGR01509  73 IEEEAK-LKPLPGVRALLEALRARGKKLALLT---NSPRAHKLvlalLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKAL 148

                         170       180       190
                  ....*....|....*....|....*....|
gi 2787376968 160 KVHPKEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:TIGR01509 149 GLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 4-189 7.23e-30

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: 108.09  E-value: 7.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAqevgitidesfneelkgisrmdsllrilrhggkeqtfdhqqrlalasKKNDLYVQ 83
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAWQLLE-----------------------------------------------RKNALLLE 33

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHEsLLPGIREVLEDIRAADVRIGLASVSLNAPGILHAL---GIEQAFDFCADASRITCSKPHPEIFLAACAGLK 160
Cdd:cd07505    34 LIASEGLK-LKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLelgLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLG 112

                         170       180
                  ....*....|....*....|....*....
gi 2787376968 161 VHPKEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:cd07505   113 VDPERCLVFEDSLAGIEAAKAAGMTVVAV 141
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
2-192 4.69e-29

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 108.09  E-value: 4.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   2 LKAIIFDLDGVITDTAHLHFLAWRAVAQEVGI-TIDESFNEELKGISRMDSLLRILrhgGKEQTFDHQQRLALAskkNDL 80
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLpPLDLEELRALIGLGLRELLRRLL---GEDPDEELEELLARF---REL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  81 YVQSLASLTHesLLPGIREVLEDIRAADVRIGLASvslNAPG-----ILHALGIEQAFDFCADASRITCSKPHPEIFLAA 155
Cdd:COG0546    75 YEEELLDETR--LFPGVRELLEALKARGIKLAVVT---NKPRefaerLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEA 149

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2787376968 156 CAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPG 192
Cdd:COG0546   150 LERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWG 186
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 4-189 2.80e-25

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs 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), 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. 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 96.94  E-value: 2.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEvgitidesfneelkgisrmdsllrilrhggkeqtfdhqqrlalasKKNDLYVQ 83
Cdd:cd16423     1 AVIFDFDGVIVDTEPLWYEAWQELLNE---------------------------------------------RRNELIKR 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHESLLPGIREVLEDIRAADVRIGLASVS--LNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKV 161
Cdd:cd16423    36 QFSEKTDLPPIEGVKELLEFLKEKGIKLAVASSSprRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGV 115

                         170       180
                  ....*....|....*....|....*...
gi 2787376968 162 HPKEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:cd16423   116 NPEECVVIEDSRNGVLAAKAAGMKCVGV 143
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-183 1.05e-24

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: 96.12  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   2 LKAIIFDLDGVITDTAHLHFLAWRAVAQEvgITIDESFNEELKGISR-MDSLLRILRHGG----KEQTFDHQQRLALASK 76
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASE--HPLAKAIVAAAEDLPIpVEDFTARLLLGKrdwlEELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  77 KNDLYVQSLASL----THESLLPGIREVLEDIRAADVRIGLAS--VSLNAPGILHALGIEQAFDFCADASRITCSKPHPE 150
Cdd:pfam00702  79 GLTVVLVELLGVialaDELKLYPGAAEALKALKERGIKVAILTgdNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2787376968 151 IFLAACAGLKVHPKEAIGIEDAAAGVEAINAAG 183
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 3-206 3.32e-20

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: 85.08  E-value: 3.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   3 KAIIFDLDGVITDTAHLHFLAWRAVAQEVGITID-ESFNEELKGISRMDSLLRILRHGGKEQTFDH---QQRLALASKKN 78
Cdd:COG1011     2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEaEELAEAYRAIEYALWRRYERGEITFAELLRRlleELGLDLAEELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  79 DLYVQSLASLTHesLLPGIREVLEDIRAADVRIGLASvslNAPG-----ILHALGIEQAFDFCADASRITCSKPHPEIFL 153
Cdd:COG1011    82 EAFLAALPELVE--PYPDALELLEALKARGYRLALLT---NGSAelqeaKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968 154 AACAGLKVHPKEAIGIEDAAAG-VEAINAAGMLSV------GIGPGLDRAGLQLHSTREL 206
Cdd:COG1011   157 LALERLGVPPEEALFVGDSPETdVAGARAAGMRTVwvnrsgEPAPAEPRPDYVISDLAEL 216
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-207 4.88e-20

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 84.61  E-value: 4.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   1 MLKAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIdeSFNEELKgisrmDSL-LRIlrhggkEQTFDH-QQRLALASKKN 78
Cdd:PRK10826    6 QILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDI--SRREELP-----DTLgLRI------DQVVDLwYARQPWNGPSR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  79 DLYVQSL----ASLTHES--LLPGIREVLEDIRAADVRIGLASVS----LNApgILHALGIEQAFDFCADASRITCSKPH 148
Cdd:PRK10826   73 QEVVQRIiarvISLIEETrpLLPGVREALALCKAQGLKIGLASASplhmLEA--VLTMFDLRDYFDALASAEKLPYSKPH 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787376968 149 PEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPGLDR-------AGLQLHSTRELT 207
Cdd:PRK10826  151 PEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQQndprwalADVKLESLTELT 216
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
5-189 1.96e-19

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 81.86  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   5 IIFDLDGVITDTAHLHFLAWRAVAQE--------------VGITIDESFnEELKGISRMDSLLRILRHggkeqtfdhqqr 70
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEfgygelseeeilkfIGLPLREIF-RYLGVSEDEEEKIEFYLR------------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  71 lALASKKNDLYVqslasltheSLLPGIREVLEDIRAADVRIGLASVSL--NAPGILHALGIEQAFDFCADASRITCSKPH 148
Cdd:pfam13419  68 -KYNEELHDKLV---------KPYPGIKELLEELKEQGYKLGIVTSKSreNVEEFLKQLGLEDYFDVIVGGDDVEGKKPD 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2787376968 149 PEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:pfam13419 138 PDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 4-201 6.45e-17

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: 75.84  E-value: 6.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEVGItideSFNEELKGIsrmdsllrilrHGgkEQTFDHQQRLALASKKNDLYVQ 83
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGV----DPEEVLKVS-----------HG--RRAIDVIRKLAPDDADIELVLA 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHE-----SLLPGIREVLEDIRAADVRIGL---ASVSLnAPGILHALGIEQAFDF-CADasRITCSKPHPEIFLA 154
Cdd:cd07527    64 LETEEPESypegvIAIPGAVDLLASLPAAGDRWAIvtsGTRAL-AEARLEAAGLPHPEVLvTAD--DVKNGKPDPEPYLL 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2787376968 155 ACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPGLDRAGLQLH 201
Cdd:cd07527   141 GAKLLGLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEAA 187
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 4-184 8.41e-17

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs 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), 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. 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: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 75.49  E-value: 8.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAW-RAVAQEVGITIDESfneelkgISRMDSLLRILrhGGKEQTFDHQQRL----------- 71
Cdd:cd07528     1 ALIFDVDGTLAETEELHRRAFnNAFFAERGLDWYWD-------RELYGELLRVG--GGKERIAAYFEKVgwpesapkdlk 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  72 ----ALASKKNDLYVQSLASLTHEsLLPGIREVLEDIRAADVRIGLASVS--LNAPGILHA-LGIE--QAFDFCADASRI 142
Cdd:cd07528    72 eliaDLHKAKTERYAELIAAGLLP-LRPGVARLIDEAKAAGVRLAIATTTspANVDALLSAlLGPErrAIFDAIAAGDDV 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2787376968 143 TCSKPHPEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGM 184
Cdd:cd07528   151 AEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGL 192
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 2-184 3.12e-15

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 72.82  E-value: 3.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   2 LKAIIFDLDGVITDT-AHLHFLAWRAVAQEVGITiDESFNEELkgisrMDSLLRIlrHGGKEQTFDH------------- 67
Cdd:PLN02779   40 PEALLFDCDGVLVETeRDGHRVAFNDAFKEFGLR-PVEWDVEL-----YDELLNI--GGGKERMTWYfnengwptstiek 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  68 -------QQRL--ALASKKNDLYVQSLASLTHEsLLPGIREVLEDIRAADVRIGLASVSLNAP--GILHA-LGIEQA--F 133
Cdd:PLN02779  112 apkdeeeRKELvdSLHDRKTELFKELIESGALP-LRPGVLRLMDEALAAGIKVAVCSTSNEKAvsKIVNTlLGPERAqgL 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2787376968 134 DFCA--DASRitcSKPHPEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGM 184
Cdd:PLN02779  191 DVFAgdDVPK---KKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGM 240
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 5-213 4.83e-15

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: 70.89  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   5 IIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESfnEELKGISRMdSLLRILRHGGKEQTFDhqQRLALASKKNDLYVQS 84
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSA--AEVRSIIGL-SLDEAIARLLPMATPA--LVAVAERYKEAFDILR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  85 LASLTHESLLPGIREVLEDIRAADVRIGLAS----VSLNApgILHALGIEQAFDF--CADASRitcSKPHPEIFLAACAG 158
Cdd:cd07533    77 LLPEHAEPLFPGVREALDALAAQGVLLAVATgksrRGLDR--VLEQHGLGGYFDAtrTADDTP---SKPHPEMLREILAE 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2787376968 159 LKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPGldraglqLHStRELTWKCLTD 213
Cdd:cd07533   152 LGVDPSRAVMVGDTAYDMQMAANAGAHAVGVAWG-------YHS-LEDLRSAGAD 198
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 3-201 2.80e-14

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: 68.85  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   3 KAIIFDLDGVITDTAHLHFLAWRAVAQEVGITidESFNEELK---GISRMDSLLRILRHGGKEqtfdhqqRLALASKKND 79
Cdd:cd02616     2 TTILFDLDGTLIDTNELIIKSFNHTLKEYGLE--GYTREEVLpfiGPPLRETFEKIDPDKLED-------MVEEFRKYYR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  80 LYVqslASLTHEslLPGIREVLEDIRAADVRIGLASVSLNAPGI--LHALGIEQAFDFCADASRITCSKPHPEIFLAACA 157
Cdd:cd02616    73 EHN---DDLTKE--YPGVYETLARLKSQGIKLGVVTTKLRETALkgLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALE 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2787376968 158 GLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPGL-DRAGLQLH 201
Cdd:cd02616   148 LLGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYkGREYLKAF 192
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
4-187 1.53e-13

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 66.25  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLLRILRHggkeqtfdHQQRL---ALASKKndl 80
Cdd:PRK10725    7 GLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIEL--------NQADLdphALAREK--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  81 yvqslASLTHESLLPGIREV--LEDIRAADVR----IGLASVSLNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLA 154
Cdd:PRK10725   76 -----TEAVKSMLLDSVEPLplIEVVKAWHGRrpmaVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLR 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2787376968 155 ACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSV 187
Cdd:PRK10725  151 CAQLMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 2-184 1.53e-13

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 66.60  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   2 LKAIIFDLDGVITDTAHLHflAWRAVAQEVGITIDESFNEEL---------KGISRMDSLLRILRhggkeqtfdhqQRLA 72
Cdd:cd02603     1 IRAVLFDFGGVLIDPDPAA--AVARFEALTGEPSEFVLDTEGlagafleleRGRITEEEFWEELR-----------EELG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  73 LASKKNDLYVQSLASLThesLLPGIREVLEDIRAADVRIGLASVSLNAPGILHALGIEQAFDFCADA---SRITCSKPHP 149
Cdd:cd02603    68 RPLSAELFEELVLAAVD---PNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVvesCRLGVRKPDP 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2787376968 150 EIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGM 184
Cdd:cd02603   145 EIYQLALERLGVKPEEVLFIDDREENVEAARALGI 179
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-192 1.80e-13

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 66.76  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   1 MLKAIIFDLDGVITDTA-HLHFLAWRAVAqEVGItidESFNEEL------KGISRMdsLLRILRHGGKEQT---FDHQQR 70
Cdd:PRK13222    5 DIRAVAFDLDGTLVDSApDLAAAVNAALA-ALGL---PPAGEERvrtwvgNGADVL--VERALTWAGREPDeelLEKLRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  71 LALaskknDLYVQSLASLTHesLLPGIREVLEDIRAADVRIGLASvslN-----APGILHALGIEQAFD--FCADAsrIT 143
Cdd:PRK13222   79 LFD-----RHYAENVAGGSR--LYPGVKETLAALKAAGYPLAVVT---NkptpfVAPLLEALGIADYFSvvIGGDS--LP 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2787376968 144 CSKPHPEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPG 192
Cdd:PRK13222  147 NKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYG 195
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 2-198 6.04e-13

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 67.57  E-value: 6.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968    2 LKAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLlrilrhGGKEQTFDHQQRLALASKKN--D 79
Cdd:PLN02919    75 VSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEANFL------GGVASVKGVKGFDPDAAKKRffE 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   80 LYVQSLASLTHESLLPGIREVLEDIRAADVRIGLAS----VSLNAPgiLHALGIEQA-FDFCADASRITCSKPHPEIFLA 154
Cdd:PLN02919   149 IYLEKYAKPNSGIGFPGALELITQCKNKGLKVAVASsadrIKVDAN--LAAAGLPLSmFDAIVSADAFENLKPAPDIFLA 226

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2787376968  155 ACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPGLDRAGL 198
Cdd:PLN02919   227 AAKILGVPTSECVVIEDALAGVQAARAAGMRCIAVTTTLSEEIL 270
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 5-189 3.46e-12

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 63.90  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   5 IIFDLDGVIT-DTAHLHFLAWRAVAQEVGITIDESFneELKGISRMDSLLRILRHGGKEQTFDHQQRLALasKKNDLYvQ 83
Cdd:PLN03243   27 VVLEWEGVIVeDDSELERKAWRALAEEEGKRPPPAF--LLKRAEGMKNEQAISEVLCWSRDFLQMKRLAI--RKEDLY-E 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHEsLLPGIREVLEDIRAADVRIGLASVSLN--APGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKV 161
Cdd:PLN03243  102 YMQGGLYR-LRPGSREFVQALKKHEIPIAVASTRPRryLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLGF 180

                         170       180
                  ....*....|....*....|....*...
gi 2787376968 162 HPKEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:PLN03243  181 IPERCIVFGNSNSSVEAAHDGCMKCVAV 208
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 2-189 3.50e-12

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 63.71  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   2 LKAIIFDLDGVITDTAHLHFLAWRAVAQEV----GITIDESF-NEELKGISRMDSLLRILRHggkeqtfDHQQRLALASK 76
Cdd:PLN02770   22 LEAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEEFfVENIAGKHNEDIALGLFPD-------DLERGLKFTDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  77 KNDLYvQSLASlthESLLP-----GIREVLED---IRAADVRIGLAsvslNAPGILHALGIEQAFDFCADASRITCSKPH 148
Cdd:PLN02770   95 KEALF-RKLAS---EQLKPlnglyKLKKWIEDrglKRAAVTNAPRE----NAELMISLLGLSDFFQAVIIGSECEHAKPH 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2787376968 149 PEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:PLN02770  167 PDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGL 207
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 5-192 1.50e-11

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: 61.38  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   5 IIFDLDGVITDTA-HLHFLAWRAVAQEVGITIDEsfnEELKG-ISRMDSLL--RILRHGGKEQTfdhQQRLALASKKNDL 80
Cdd:TIGR01449   1 VLFDLDGTLVDSApDIAAAVNMALAALGLPPATL---ARVIGfIGNGVPVLmeRVLAWAGQEPD---AQRVAELRKLFDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  81 YVQSLASlTHESLLPGIREVLEDIRAADVRIGLAS---VSLNAPgILHALGIEQAFDFCADASRITCSKPHPEIFLAACA 157
Cdd:TIGR01449  75 HYEEVAG-ELTSVFPGVEATLGALRAKGLRLGLVTnkpTPLARP-LLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAE 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2787376968 158 GLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPG 192
Cdd:TIGR01449 153 RLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYG 187
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 3-188 1.68e-10

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs 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), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 56.94  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   3 KAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGIsrmdsllrilrhggkeqtfdhqqrlalaskkndlyv 82
Cdd:cd07526     1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGARVLAAFEAELQPI------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  83 qslaslthesllPGIREVLEDIR-----AADVRIGLASVSLNAPGILHALGieqafDFCADASRITCSKPHPEIFLAACA 157
Cdd:cd07526    45 ------------PGAAAALSALTlpfcvASNSSRERLTHSLGLAGLLAYFE-----GRIFSASDVGRGKPAPDLFLHAAA 107

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2787376968 158 GLKVHPKEAIGIEDAAAGVEAINAAGMLSVG 188
Cdd:cd07526   108 QMGVAPERCLVIEDSPTGVRAALAAGMTVFG 138
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 4-192 5.01e-10

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: 57.24  E-value: 5.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEVGITideSFNEEL------KGISRMdsLLRILRHGG----KEQTFDHQQRLAL 73
Cdd:cd16417     1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLP---PLPEETvrtwigNGADVL--VERALTGAReaepDEELFKEARALFD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  74 askknDLYVQSLASLTHesLLPGIREVLEDIRAADVRIGLASvslN-----APGILHALGIEQAFDFCADASRITCSKPH 148
Cdd:cd16417    76 -----RHYAETLSVHSH--LYPGVKEGLAALKAQGYPLACVT---NkperfVAPLLEALGISDYFSLVLGGDSLPEKKPD 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2787376968 149 PEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPG 192
Cdd:cd16417   146 PAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLTYG 189
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 1-190 9.52e-10

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 56.58  E-value: 9.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   1 MLKAIIFDLDGVITDTAHL----------HFLAWRAVAQEVGITIDESFNEELKGI--SRMDSLLRILRhggkeqTFDHQ 68
Cdd:PRK13288    2 KINTVLFDLDGTLINTNELiissflhtlkTYYPNQYKREDVLPFIGPSLHDTFSKIdeSKVEEMITTYR------EFNHE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  69 QrlalaskkndlyvqslasltHESLL---PGIREVLEDIRAADVRIGLASVSLNAPGI--LHALGIEQAFDFCADASRIT 143
Cdd:PRK13288   76 H--------------------HDELVteyETVYETLKTLKKQGYKLGIVTTKMRDTVEmgLKLTGLDEFFDVVITLDDVE 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2787376968 144 CSKPHPEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIG 190
Cdd:PRK13288  136 HAKPDPEPVLKALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVA 182
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 1-184 5.89e-09

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 54.32  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   1 MLKAIIFDLDGVITDTAHLHFLAWRAVAQEVGITID-ESFNEELKGISRMDSLLRI-LRHGgkeqtfdhqqrlaLASKKN 78
Cdd:PRK10563    3 QIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSlEEVFKRFKGVKLYEIIDIIsKEHG-------------VTLAKA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  79 DL---YVQSLASLTHESL--LPGIREVLEDIRAAdvrigLASVSlNAP--GILHALGIEQAFDFCAD----ASRITCSKP 147
Cdd:PRK10563   70 ELepvYRAEVARLFDSELepIAGANALLESITVP-----MCVVS-NGPvsKMQHSLGKTGMLHYFPDklfsGYDIQRWKP 143

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2787376968 148 HPEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGM 184
Cdd:PRK10563  144 DPALMFHAAEAMNVNVENCILVDDSSAGAQSGIAAGM 180
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 3-184 1.51e-08

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs 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), 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. 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: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 52.73  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   3 KAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEELKGISRMDSLLRILRHGG----KEQTFDHQQRLALASKKN 78
Cdd:cd07529     2 THCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKlpmsLEEEFDEQQEALAELFMG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  79 DLyvqslasltheSLLPGIREVLEDIRAADVRIGLASVSLNAPGIL---HALGIEQAFDF--CADASRITC-SKPHPEIF 152
Cdd:cd07529    82 TA-----------KLMPGAERLLRHLHAHNIPIALATSSCTRHFKLktsRHKELFSLFHHvvTGDDPEVKGrGKPAPDIF 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2787376968 153 LAACAGLK---VHPKEAIGIEDAAAGVEAINAAGM 184
Cdd:cd07529   151 LVAAKRFNeppKDPSKCLVFEDSPNGVKAAKAAGM 185
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 98-184 2.29e-08

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 51.14  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  98 REVLEDIRAADVRIGLASvslNA----PGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKVHPKEAIGIEDA- 172
Cdd:cd16415    13 VETLKDLKEKGLKLAVVS---NFdrrlRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDDl 89

                          90
                  ....*....|..
gi 2787376968 173 AAGVEAINAAGM 184
Cdd:cd16415    90 KNDYLGARAVGW 101
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 4-164 3.73e-08

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: 51.24  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAhlhFLAWRAVAQEVgitidESFNEELKGISRMDSLLRILRhggkeqtfDHQQRLALASKKNDLYVQ 83
Cdd:TIGR01549   1 AILFDIDGTLVDIK---FAIRRAFPQTF-----EEFGLDPASFKALKQAGGLAE--------EEWYRIATSALEELQGRF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLASLTHESLLPGIREVLEDIRAADVRIGLASvSLNAPGILHAL---GIEQAFDFCADASRItCSKPHPEIFLAACAGLK 160
Cdd:TIGR01549  65 WSEYDAEEAYIRGAADLLARLKSAGIKLGIIS-NGSLRAQKLLLrlfGLGDYFELILVSDEP-GSKPEPEIFLAALESLG 142


                  ....
gi 2787376968 161 VHPK 164
Cdd:TIGR01549 143 VPPE 146
PLN02940 PLN02940
riboflavin kinase
 94-189 4.69e-08

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 52.53  E-value: 4.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  94 LPGIREVLEDIRAADVRIGLASvslNAPG------ILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKVHPKEAI 167
Cdd:PLN02940   95 LPGANRLIKHLKSHGVPMALAS---NSPRanieakISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSNCL 171

                          90       100
                  ....*....|....*....|..
gi 2787376968 168 GIEDAAAGVEAINAAGMLSVGI 189
Cdd:PLN02940  172 VIEDSLPGVMAGKAAGMEVIAV 193
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 97-189 5.90e-08

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: 49.32  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  97 IREVLEDIRAADVRIGLASvslNAPG-----ILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKVHPKEAIGIED 171
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVT---NRSRealraLLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGD 88

                          90
                  ....*....|....*...
gi 2787376968 172 AAAGVEAINAAGMLSVGI 189
Cdd:cd01427    89 SENDIEAARAAGGRTVAV 106
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 4-196 9.74e-08

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: 50.43  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEVGI-TIDESFNEELKGISRMDsllrILRHGGKEqtfdhQQRLALASKknDLYV 82
Cdd:cd04303     1 LIIFDFDGTLADSFPWFLSILNQLAARHGFkTVDEEEIEQLRQLSSRE----ILKQLGVP-----LWKLPLIAK--DFRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  83 QSLASLTHESLLPGIREVLEDIRAADVRIGLASVS--LNAPGILHALGIEQAFDfCADASRITCSKPHPEIFLAACaglK 160
Cdd:cd04303    70 LMAEAAPELALFPGVEDMLRALHARGVRLAVVSSNseENIRRVLGPEELISLFA-VIEGSSLFGKAKKIRRVLRRT---K 145

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2787376968 161 VHPKEAIGIEDAAAGVEAINAAGMLSVGIGPGLDRA 196
Cdd:cd04303   146 ITAAQVIYVGDETRDIEAARKVGLAFAAVSWGYAKP 181
PLN02811 PLN02811
hydrolase
 146-196 1.60e-06

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 47.06  E-value: 1.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2787376968 146 KPHPEIFLAACAGL---KVHPKEAIGIEDAAAGVEAINAAGMLSVGI-GPGLDRA 196
Cdd:PLN02811  137 KPAPDIFLAAARRFedgPVDPGKVLVFEDAPSGVEAAKNAGMSVVMVpDPRLDKS 191
PRK11587 PRK11587
putative phosphatase; Provisional
 3-207 1.68e-06

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 47.30  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   3 KAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEeLKGISRMDSLlrilRH---GGKEQTFDHQQRLALASKKND 79
Cdd:PRK11587    4 KGFLFDLDGTLVDSLPAVERAWSNWADRHGIAPDEVLNF-IHGKQAITSL----RHfmaGASEAEIQAEFTRLEQIEATD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  80 lyVQSLASLthesllPGIREVLEDIRAADV--------RIGLASVSLNAPGilhaLGIEQAFdfcADASRITCSKPHPEI 151
Cdd:PRK11587   79 --TEGITAL------PGAIALLNHLNKLGIpwaivtsgSVPVASARHKAAG----LPAPEVF---VTAERVKRGKPEPDA 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2787376968 152 FLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIG-----PGLDRAGLQLHSTRELT 207
Cdd:PRK11587  144 YLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNapadtPRLDEVDLVLHSLEQLT 204
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 6-189 2.87e-06

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 47.17  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   6 IFDLDGVIT-DTAHLHFLAWRAVAQEVGITIDESFneELKGISRMDSllrilrhggkEQTF--------DHQQRLALASK 76
Cdd:PLN02575  135 IFEWEGVIIeDNPDLENQAWLTLAQEEGKSPPPAF--ILRRVEGMKN----------EQAIsevlcwsrDPAELRRMATR 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  77 KNDLYvQSLASLTHEsLLPGIREVLEDIraADVRIGLASVSLNAPGILH----ALGIEQAFDFCADASRITCSKPHPEIF 152
Cdd:PLN02575  203 KEEIY-QALQGGIYR-LRTGSQEFVNVL--MNYKIPMALVSTRPRKTLEnaigSIGIRGFFSVIVAAEDVYRGKPDPEMF 278

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2787376968 153 LAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:PLN02575  279 IYAAQLLNFIPERCIVFGNSNQTVEAAHDARMKCVAV 315
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 4-184 9.61e-06

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: 44.29  E-value: 9.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDesfneelkgisrMDSLLRILRhggKEQTFDHQQRLALASKKNDLYVQ 83
Cdd:cd07523     1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQD------------LETVYKIIK---ESSVQFAIQYYAEVPDLEEEYKE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  84 SLAS-LTHESLLPGIREVLEDIRAADVRIGLAS-VSLNAPGILHALGIEQAFDFCADASRITCSKPHPEIFLAACAGLKV 161
Cdd:cd07523    66 LEAEyLAKPILFPGAKAVLRWIKEQGGKNFLMThRDHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQL 145

                         170       180
                  ....*....|....*....|...
gi 2787376968 162 HPKEAIGIEDAAAGVEAINAAGM 184
Cdd:cd07523   146 NPEETVMIGDRELDIEAGHNAGI 168
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 2-209 1.74e-05

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 44.21  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   2 LKAIIFDLDGVITDtahlhF--LAWRAVAQEV----GITIDESFNEELKGISRMDSLLRILRHGG-KEQTFDHQQRLALA 74
Cdd:cd02586     1 IEAVIFDWAGTTVD-----YgsFAPVNAFVEAfaqrGVQITLEEARKPMGLLKIDHIRALLEMPRvAEAWRAVFGRLPTE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  75 SKKNDLY-------VQSLAslTHESLLPGIREVLEDIRAADVRIGlaSVSLNAPGILHALGIEQAF-----DFCADASRI 142
Cdd:cd02586    76 ADVDALYeefepilIASLA--EYSSPIPGVLEVIAKLRARGIKIG--STTGYTREMMDIVLPEAAAqgyrpDSLVTPDDV 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2787376968 143 TCSKPHPEIFLAACAGLKVHPKEA-IGIEDAAAGVEAINAAGMLSVGIGP-----GLDRAGLQLHSTRELTWK 209
Cdd:cd02586   152 PAGRPYPWMCYKNAIELGVYDVAAvVKVGDTVPDIKEGLNAGMWTVGVILsgnelGLSEEEVEALDSEELAAR 224
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 123-191 3.95e-05

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 42.62  E-value: 3.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2787376968 123 ILHALGIEQAFD--FCADASRiTCSKPHPEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGP 191
Cdd:cd02604   113 VLKRLGLADLFDgiFDIEYAG-PDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLVGP 182
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 4-187 1.59e-04

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: 41.15  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTA-HLHFLAWRAVAQEVGITIDESFNEEL--KGISRMDSLLRILRHGGKEQTfDHQQRLALASkknDL 80
Cdd:cd07512     1 AVIFDLDGTLIDSApDLHAALNAVLAAEGLAPLSLAEVRSFvgHGAPALIRRAFAAAGEDLDGP-LHDALLARFL---DH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  81 YVQSLASLTheSLLPGIREVLEDIRAADVRIGLASVSLNAPG--ILHALGIEQAFDFCADASRITCSKPHPEIFLAACAG 158
Cdd:cd07512    77 YEADPPGLT--RPYPGVIEALERLRAAGWRLAICTNKPEAPAraLLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRR 154

                         170       180
                  ....*....|....*....|....*....
gi 2787376968 159 LKVHPKEAIGIEDAAAGVEAINAAGMLSV 187
Cdd:cd07512   155 LGGDVSRALMVGDSETDAATARAAGVPFV 183
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 3-166 4.00e-04

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: 40.33  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   3 KAIIFDLDGVITDTAHLHFLAWRAVAQEVGITIDESFNEEL---------------KGISRmDSLLRILRHGGKEQTFDH 67
Cdd:cd02588     1 KALVFDVYGTLIDWHSGLAAAERAFPGRGEELSRLWRQKQLeytwlvtlmgpyvdfDELTR-DALRATAAELGLELDESD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  68 QQRLAlaskkndlyvQSLASLThesLLPGIREVLEDIRAADVRIGLASVSLN--APGILHALGIEQAFD--FCADASRIt 143
Cdd:cd02588    80 LDELG----------DAYLRLP---PFPDVVAGLRRLREAGYRLAILSNGSPdlIEDVVANAGLRDLFDavLSAEDVRA- 145

                         170       180
                  ....*....|....*....|...
gi 2787376968 144 cSKPHPEIFLAACAGLKVHPKEA 166
Cdd:cd02588   146 -YKPAPAVYELAAERLGVPPDEI 167
Hydrolase_like pfam13242
HAD-hyrolase-like;
144-208 5.22e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 37.60  E-value: 5.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787376968 144 CSKPHPEIFLAACAGLKVHPKEAIGIED-AAAGVEAINAAGMLSVGIGPGLDRAGLQLHSTRELTW 208
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDrLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDY 67
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 4-192 9.77e-04

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: 39.11  E-value: 9.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   4 AIIFDLDGVITDTAhlhflawravaqeVGITidESFNEELK--GISR--MDSLLRILrhgGK--EQTFdhqQRLALASKK 77
Cdd:cd04302     1 TILFDLDGTLTDSA-------------EGIT--ASVQYALEelGIPVpdESELRRFI---GPplEDSF---RELLPFDEE 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  78 N-----DLYVQSLAS--LTHESLLPGIREVLEDIRAADVRIGLAS--VSLNAPGILHALGIEQAFDFCA----DASRITc 144
Cdd:cd04302    60 EaqravDAYREYYKEkgLFENEVYPGIPELLEKLKAAGYRLYVATskPEVFARRILEHFGLDEYFDGIAgaslDGSRVH- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2787376968 145 skpHPEIFLAACAGLKVHPKEAIGIEDAAAGVEAINAAGMLSVGIGPG 192
Cdd:cd04302   139 ---KADVIRYALDTLGIAPEQAVMIGDRKHDIIGARANGIDSIGVLYG 183
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 93-187 1.75e-03

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: 36.75  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  93 LLPGIREVLEDIRAaDVRIGLASvslNAPGI-----LHALGIEQAFD--FCADASRItcSKPHPEIFLAACAGLKVHPKE 165
Cdd:cd04305    10 LLPGAKELLEELKK-GYKLGIIT---NGPTEvqwekLEQLGIHKYFDhiVISEEVGV--QKPNPEIFDYALNQLGVKPEE 83

                          90       100
                  ....*....|....*....|...
gi 2787376968 166 AIGIED-AAAGVEAINAAGMLSV 187
Cdd:cd04305    84 TLMVGDsLESDILGAKNAGIKTV 106
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 85-189 5.15e-03

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 37.15  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  85 LASL-THESLLPGIREVLEDIRAADVRIG---------LASVSLNAPgilhALGIEQAFDFCAD---ASRitcskPHPEI 151
Cdd:PRK13478   93 IAKLaDYATPIPGVLEVIAALRARGIKIGsttgytremMDVVVPLAA----AQGYRPDHVVTTDdvpAGR-----PYPWM 163

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2787376968 152 FLAACAGLKVHP-KEAIGIEDAAAGVEAINAAGMLSVGI 189
Cdd:PRK13478  164 ALKNAIELGVYDvAACVKVDDTVPGIEEGLNAGMWTVGV 202
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 97-189 5.22e-03

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; 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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 35.51  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968  97 IREVLEDIRAADVRIGLASvslNAPG-----ILHALGiEQAFDFCADASRITCSKPHPEIFLAACAGLKVHPKEAIGIED 171
Cdd:cd16421    12 ILELLKALRQKGIKLAVLS---NKPNeavqvLVEELF-PGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGD 87

                          90
                  ....*....|....*...
gi 2787376968 172 AAAGVEAINAAGMLSVGI 189
Cdd:cd16421    88 SGVDMQTARNAGMDEIGV 105
HAD pfam12710
haloacid dehalogenase-like hydrolase;
5-131 5.78e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 36.36  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787376968   5 IIFDLDGVITDTAHLHFLaWRAVAQEVGITIDESFNEELkgISRMDSLLRILRHGGKEQTFDHQQRlALASKKNDLYVQS 84
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLL-IRALLRRGGPDLWRALLVLL--LLALLRLLGRLSRAGARELLRALLA-GLPEEDAAELERF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2787376968  85 LASLTHESLLPGIREVLEDIRAADVRIGL--ASVSLNAPGILHALGIEQ 131
Cdd:pfam12710  77 VAEVALPRLHPGALELLAAHRAAGDRVVVvtGGLRPLVEPVLAELGFDE 125
 
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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