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Conserved domains on  [gi|3024403|sp|P77366|]
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RecName: Full=Beta-phosphoglucomutase; Short=Beta-PGM

Protein Classification

beta-phosphoglucomutase( domain architecture ID 11493425)

beta-phosphoglucomutase (beta-PGM) catalyzes the conversion of beta D-glucose 1-phosphate (G1P) to D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 5-191 1.81e-111

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: 316.94  E-value: 1.81e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      5 GVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKegDFNSQERAQLAYRKNLLYVH 84
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     85 SLRELTVNAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPP 164
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 3024403    165 QACIGIEDAQAGIDAINASGMRSVGIG 191
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 5-191 1.81e-111

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: 316.94  E-value: 1.81e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      5 GVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKegDFNSQERAQLAYRKNLLYVH 84
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     85 SLRELTVNAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPP 164
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 3024403    165 QACIGIEDAQAGIDAINASGMRSVGIG 191
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 5-215 2.09e-78

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: 232.57  E-value: 2.09e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    5 GVIFDLDGVITDTAHLHFQAWQQIAaeigisidaqfneslkgisrdeslrrilqhggkegdfnsqERAQLAYRKNLLYVH 84
Cdd:cd02598   1 GVIFDLDGVITDTAEYHYRAWKKLA----------------------------------------DKEELAARKNRIYVE 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   85 SLRELTVNAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPP 164
Cdd:cd02598  41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3024403  165 QACIGIEDAQAGIDAINASGMRSVGIGAG---LTGAQLLLPSTESLTWPRLSAF 215
Cdd:cd02598 121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREedlLGADIVVPDTTADLTIEELLEV 174
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
2-207 1.38e-65

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 201.21  E-value: 1.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    2 KLQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKEGDfnsqeRAQLAYRKNLL 81
Cdd:COG0637   1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLP-----EEELAARKEEL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   82 YVHSLRELTVnAVLPGIRSLLADLRAQQISVGLASVSL--NAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAG 159
Cdd:COG0637  76 YRELLAEEGL-PLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAER 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3024403  160 LGVPPQACIGIEDAQAGIDAINASGMRSVGIGAG------LTGAQLLLPSTESL 207
Cdd:COG0637 155 LGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGgtaeeeLAGADLVVDDLAEL 208
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-190 5.75e-27

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 101.51  E-value: 5.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      6 VIFDLDGVITDTAHLHFQAWQQIAAEIGISI--DAQFNEsLKGISRDESLRRILQHGGKEGDFNsqeraqlAYRKnlLYV 83
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGElsEEEILK-FIGLPLREIFRYLGVSEDEEEKIE-------FYLR--KYN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     84 HSLRELTVNaVLPGIRSLLADLRAQQISVGLASVSLNAPTI--LAALELREFFTFCADASQLKNSKPDPEIFLAACAGLG 161
Cdd:pfam13419  71 EELHDKLVK-PYPGIKELLEELKEQGYKLGIVTSKSRENVEefLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLG 149

                         170       180
                  ....*....|....*....|....*....
gi 3024403    162 VPPQACIGIEDAQAGIDAINASGMRSVGI 190
Cdd:pfam13419 150 LKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
4-188 2.44e-23

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 92.45  E-value: 2.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     4 QGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKEGDFNsqeraQLAYRKNLLyV 83
Cdd:PRK10725   6 AGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPH-----ALAREKTEA-V 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    84 HSLRELTVNAvLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVP 163
Cdd:PRK10725  80 KSMLLDSVEP-LPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQ 158

                        170       180
                 ....*....|....*....|....*
gi 3024403   164 PQACIGIEDAQAGIDAINASGMRSV 188
Cdd:PRK10725 159 PTQCVVFEDADFGIQAARAAGMDAV 183
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 5-191 1.81e-111

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: 316.94  E-value: 1.81e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      5 GVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKegDFNSQERAQLAYRKNLLYVH 84
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     85 SLRELTVNAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPP 164
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 3024403    165 QACIGIEDAQAGIDAINASGMRSVGIG 191
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 3-190 6.53e-93

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: 269.98  E-value: 6.53e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      3 LQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKEgdFNSQERAQLAYRKNLLY 82
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDG--LSLEEIHQLAERKNELY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     83 VHSLReLTVNAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGV 162
Cdd:TIGR02009  79 RELLR-LTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGV 157

                         170       180
                  ....*....|....*....|....*...
gi 3024403    163 PPQACIGIEDAQAGIDAINASGMRSVGI 190
Cdd:TIGR02009 158 PPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 5-215 2.09e-78

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: 232.57  E-value: 2.09e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    5 GVIFDLDGVITDTAHLHFQAWQQIAaeigisidaqfneslkgisrdeslrrilqhggkegdfnsqERAQLAYRKNLLYVH 84
Cdd:cd02598   1 GVIFDLDGVITDTAEYHYRAWKKLA----------------------------------------DKEELAARKNRIYVE 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   85 SLRELTVNAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPP 164
Cdd:cd02598  41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3024403  165 QACIGIEDAQAGIDAINASGMRSVGIGAG---LTGAQLLLPSTESLTWPRLSAF 215
Cdd:cd02598 121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREedlLGADIVVPDTTADLTIEELLEV 174
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
2-207 1.38e-65

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 201.21  E-value: 1.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    2 KLQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKEGDfnsqeRAQLAYRKNLL 81
Cdd:COG0637   1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLP-----EEELAARKEEL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   82 YVHSLRELTVnAVLPGIRSLLADLRAQQISVGLASVSL--NAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAG 159
Cdd:COG0637  76 YRELLAEEGL-PLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAER 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3024403  160 LGVPPQACIGIEDAQAGIDAINASGMRSVGIGAG------LTGAQLLLPSTESL 207
Cdd:COG0637 155 LGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGgtaeeeLAGADLVVDDLAEL 208
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 6-190 2.14e-47

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: 154.11  E-value: 2.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      6 VIFDLDGVITDTAHLHfqAWQQIAAEIGISIDAQFNESLkgISRDESLRRILQhggKEGDFNSQERAQLAYrKNLLYVHS 85
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAI--AKLINREELGLVPDELGVSAV--GRLELALRRFKA---QYGRTISPEDAQLLY-KQLFYEQI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     86 LRELTVnAVLPGIRSLLADLRAQQISVGLASvslNAPTI----LAALELREFFTFCADASQLKNSKPDPEIFLAACAGLG 161
Cdd:TIGR01509  74 EEEAKL-KPLPGVRALLEALRARGKKLALLT---NSPRAhklvLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALG 149

                         170       180
                  ....*....|....*....|....*....
gi 3024403    162 VPPQACIGIEDAQAGIDAINASGMRSVGI 190
Cdd:TIGR01509 150 LEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 5-190 2.74e-33

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: 116.56  E-value: 2.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    5 GVIFDLDGVITDTAHLHFQAWQQIAaeigisidaqfneslkgisrdeslrrilqhggkegdfnsqeraqlayRKNLLYVH 84
Cdd:cd07505   1 AVIFDMDGVLIDTEPLHRQAWQLLE-----------------------------------------------RKNALLLE 33

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   85 SLRELTVnAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALEL---REFFTFCADASQLKNSKPDPEIFLAACAGLG 161
Cdd:cd07505  34 LIASEGL-KLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELgllRGYFDVIVSGDDVERGKPAPDIYLLAAERLG 112

                       170       180
                ....*....|....*....|....*....
gi 3024403  162 VPPQACIGIEDAQAGIDAINASGMRSVGI 190
Cdd:cd07505 113 VDPERCLVFEDSLAGIEAAKAAGMTVVAV 141
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-200 1.87e-31

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 114.26  E-value: 1.87e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    3 LQGVIFDLDGVITDTAHLHFQAWQQIAAEIGI-SIDAQFNESLKGISRDESLRRILQHGGKEGdfnsQERAQLAYRKnlL 81
Cdd:COG0546   1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLpPLDLEELRALIGLGLRELLRRLLGEDPDEE----LEELLARFRE--L 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   82 YVHSLRELTVnaVLPGIRSLLADLRAQQISVGLASvslNAPT-----ILAALELREFFTFCADASQLKNSKPDPEIFLAA 156
Cdd:COG0546  75 YEEELLDETR--LFPGVRELLEALKARGIKLAVVT---NKPRefaerLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEA 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 3024403  157 CAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLL 200
Cdd:COG0546 150 LERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEEL 193
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 6-200 1.78e-27

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: 102.72  E-value: 1.78e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAHLHFQAWQQIAAEigisidaqfneslkgisrdeslrrilqhggkegdfnsqeraqlayRKNLLYVHS 85
Cdd:cd16423   2 VIFDFDGVIVDTEPLWYEAWQELLNE---------------------------------------------RRNELIKRQ 36

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   86 LRELTVNAVLPGIRSLLADLRAQQISVGLASVSlNAPTI---LAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGV 162
Cdd:cd16423  37 FSEKTDLPPIEGVKELLEFLKEKGIKLAVASSS-PRRWIephLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGV 115

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 3024403  163 PPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLL 200
Cdd:cd16423 116 NPEECVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDF 153
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-190 5.75e-27

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 101.51  E-value: 5.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      6 VIFDLDGVITDTAHLHFQAWQQIAAEIGISI--DAQFNEsLKGISRDESLRRILQHGGKEGDFNsqeraqlAYRKnlLYV 83
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGElsEEEILK-FIGLPLREIFRYLGVSEDEEEKIE-------FYLR--KYN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     84 HSLRELTVNaVLPGIRSLLADLRAQQISVGLASVSLNAPTI--LAALELREFFTFCADASQLKNSKPDPEIFLAACAGLG 161
Cdd:pfam13419  71 EELHDKLVK-PYPGIKELLEELKEQGYKLGIVTSKSRENVEefLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLG 149

                         170       180
                  ....*....|....*....|....*....
gi 3024403    162 VPPQACIGIEDAQAGIDAINASGMRSVGI 190
Cdd:pfam13419 150 LKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-184 3.55e-25

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: 97.27  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      3 LQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISidAQFNESLKGISRD-ESLRRILQHG-----GKEGDFNSQERAQLAY 76
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLA--KAIVAAAEDLPIPvEDFTARLLLGkrdwlEELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     77 RKNLLYVHSLRELTVN---AVLPGIRSLLADLRAQQISVGLAS--VSLNAPTILAALELREFFTFCADASQLKNSKPDPE 151
Cdd:pfam00702  79 GLTVVLVELLGVIALAdelKLYPGAAEALKALKERGIKVAILTgdNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 3024403    152 IFLAACAGLGVPPQACIGIEDAQAGIDAINASG 184
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
4-188 2.44e-23

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 92.45  E-value: 2.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     4 QGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKEGDFNsqeraQLAYRKNLLyV 83
Cdd:PRK10725   6 AGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPH-----ALAREKTEA-V 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    84 HSLRELTVNAvLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVP 163
Cdd:PRK10725  80 KSMLLDSVEP-LPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQ 158

                        170       180
                 ....*....|....*....|....*
gi 3024403   164 PQACIGIEDAQAGIDAINASGMRSV 188
Cdd:PRK10725 159 PTQCVVFEDADFGIQAARAAGMDAV 183
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 5-201 1.57e-21

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: 88.17  E-value: 1.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    5 GVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESlKGISRDESLRRIlqhggkegdFNSQERAQLAYRKNLLYVH 84
Cdd:cd07527   1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEEVLKVS-HGRRAIDVIRKL---------APDDADIELVLALETEEPE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   85 SLRELTVnaVLPGIRSLLADLRAQQIS---VGLASVSLnAPTILAALELREFFTF-CADasQLKNSKPDPEIFLAACAGL 160
Cdd:cd07527  71 SYPEGVI--AIPGAVDLLASLPAAGDRwaiVTSGTRAL-AEARLEAAGLPHPEVLvTAD--DVKNGKPDPEPYLLGAKLL 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3024403  161 GVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLLL 201
Cdd:cd07527 146 GLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEA 186
PRK10826 PRK10826
hexitol phosphatase HxpB;
3-192 1.90e-19

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 82.69  E-value: 1.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     3 LQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIdaqfneslkgiSRDESLR-----RILQ------HGGKEGDFNSQER 71
Cdd:PRK10826   7 ILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDI-----------SRREELPdtlglRIDQvvdlwyARQPWNGPSRQEV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    72 AQLAYRKNLLYVHSLRELtvnavLPGIRSLLADLRAQQISVGLASVS----LNAptILAALELREFFTFCADASQLKNSK 147
Cdd:PRK10826  76 VQRIIARVISLIEETRPL-----LPGVREALALCKAQGLKIGLASASplhmLEA--VLTMFDLRDYFDALASAEKLPYSK 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 3024403   148 PDPEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGA 192
Cdd:PRK10826 149 PHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPA 193
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 6-188 2.97e-19

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: 82.38  E-value: 2.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQ-------------FNESLKG-ISRDESLRRILQHGGKEgDFNSQER 71
Cdd:COG1011   4 VLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEelaeayraieyalWRRYERGeITFAELLRRLLEELGLD-LAEELAE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   72 AQLAYRKNLLYVHslreltvnavlPGIRSLLADLRAQQISVGLASvslNAPT-----ILAALELREFFTFCADASQLKNS 146
Cdd:COG1011  83 AFLAALPELVEPY-----------PDALELLEALKARGYRLALLT---NGSAelqeaKLRRLGLDDLFDAVVSSEEVGVR 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 3024403  147 KPDPEIFLAACAGLGVPPQACIGIEDAQAG-IDAINASGMRSV 188
Cdd:COG1011 149 KPDPEIFELALERLGVPPEEALFVGDSPETdVAGARAAGMRTV 191
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 6-188 4.13e-18

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: 78.96  E-value: 4.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAHLHFQAW-QQIAAEIGISID---AQFNESLKGISRDESLRRILQHGGKE--GDFNSQER-AQLAYRK 78
Cdd:cd07528   2 LIFDVDGTLAETEELHRRAFnNAFFAERGLDWYwdrELYGELLRVGGGKERIAAYFEKVGWPesAPKDLKELiADLHKAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   79 NLLYVHSLRELTVnAVLPGIRSLLADLRAQQISVGLASVS--LNAPTILAAL---ELREFFTFCADASQLKNSKPDPEIF 153
Cdd:cd07528  82 TERYAELIAAGLL-PLRPGVARLIDEAKAAGVRLAIATTTspANVDALLSALlgpERRAIFDAIAAGDDVAEKKPDPDIY 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 3024403  154 LAACAGLGVPPQACIGIEDAQAGIDAINASGMRSV 188
Cdd:cd07528 161 LLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 6-201 2.63e-17

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: 76.67  E-value: 2.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAHLHFQAWQQIAAEIGISI-DAQFNESLKGISRDESLRRILQHGGKegdfnSQERAQLAYRKnllYVH 84
Cdd:cd07533   2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVpSAAEVRSIIGLSLDEAIARLLPMATP-----ALVAVAERYKE---AFD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   85 SLRELTVNA--VLPGIRSLLADLRAQQISVGLAS----VSLNAptILAALELREFF--TFCADASQlknSKPDPEIFLAA 156
Cdd:cd07533  74 ILRLLPEHAepLFPGVREALDALAAQGVLLAVATgksrRGLDR--VLEQHGLGGYFdaTRTADDTP---SKPHPEMLREI 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 3024403  157 CAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLLL 201
Cdd:cd07533 149 LAELGVDPSRAVMVGDTAYDMQMAANAGAHAVGVAWGYHSLEDLR 193
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 6-188 2.52e-16

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: 73.92  E-value: 2.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGG----KEGDFNSQERAQLAYRKNLL 81
Cdd:cd07529   4 CIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKlpmsLEEEFDEQQEALAELFMGTA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   82 yvhslreltvnAVLPGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTF-----CADASQLK-NSKPDPEIFLA 155
Cdd:cd07529  84 -----------KLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLfhhvvTGDDPEVKgRGKPAPDIFLV 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 3024403  156 ACAGLGVP---PQACIGIEDAQAGIDAINASGMRSV 188
Cdd:cd07529 153 AAKRFNEPpkdPSKCLVFEDSPNGVKAAKAAGMQVV 188
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 2-199 7.14e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 75.66  E-value: 7.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      2 KLQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLrrilqhGGKEGDFNSQERAQLAYRKNLL 81
Cdd:PLN02919   74 KVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEANFL------GGVASVKGVKGFDPDAAKKRFF 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     82 YVHSLRELTVNAVL--PGIRSLLADLRAQQISVGLAS----VSLNAPTILAALELREFFTFC-ADAsqLKNSKPDPEIFL 154
Cdd:PLN02919  148 EIYLEKYAKPNSGIgfPGALELITQCKNKGLKVAVASsadrIKVDANLAAAGLPLSMFDAIVsADA--FENLKPAPDIFL 225

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 3024403    155 AACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQL 199
Cdd:PLN02919  226 AAAKILGVPTSECVVIEDALAGVQAARAAGMRCIAVTTTLSEEIL 270
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 5-201 1.87e-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: 69.23  E-value: 1.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    5 GVIFDLDGVITDTAHLHFQAWQQIAAEIGisidaqfnesLKGISRDESLRRI---LQHGGKEGDFNSQERAQLAYRKNll 81
Cdd:cd02616   3 TILFDLDGTLIDTNELIIKSFNHTLKEYG----------LEGYTREEVLPFIgppLRETFEKIDPDKLEDMVEEFRKY-- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   82 YVHSLRELTvnAVLPGIRSLLADLRAQQISVGLASVSLNAPTI--LAALELREFFTFCADASQLKNSKPDPEIFLAACAG 159
Cdd:cd02616  71 YREHNDDLT--KEYPGVYETLARLKSQGIKLGVVTTKLRETALkgLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALEL 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 3024403  160 LGVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLLL 201
Cdd:cd02616 149 LGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLK 190
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 6-188 2.48e-14

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: 68.53  E-value: 2.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAHlhFQAWQQIAAEIGISIDAqfneslkgisrdeslrrILQHGGKEGDFNSQERAQL----------A 75
Cdd:cd02603   4 VLFDFGGVLIDPDP--AAAVARFEALTGEPSEF-----------------VLDTEGLAGAFLELERGRIteeefweelrE 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   76 YRKNLLYVHSLREL--TVNAVLPGIRSLLADLRAQQISVGLASvslNAPTILAALELRE---FFTFCADA---SQLKNSK 147
Cdd:cd02603  65 ELGRPLSAELFEELvlAAVDPNPEMLDLLEALRAKGYKVYLLS---NTWPDHFKFQLELlprRGDLFDGVvesCRLGVRK 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3024403  148 PDPEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSV 188
Cdd:cd02603 142 PDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAI 182
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 5-190 5.61e-14

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 68.91  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     5 GVIFDLDGVIT-DTAHLHFQAWQQIAAEIGISIDAQFN-ESLKGISRDESLRRILQHggkEGDFNSQERaqLAYRKNLLY 82
Cdd:PLN03243  26 GVVLEWEGVIVeDDSELERKAWRALAEEEGKRPPPAFLlKRAEGMKNEQAISEVLCW---SRDFLQMKR--LAIRKEDLY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    83 VHSLRELTvnAVLPGIRSLLADLRAQQISVGLASVSLNAPT--ILAALELREFFTFCADASQLKNSKPDPEIFLAACAGL 160
Cdd:PLN03243 101 EYMQGGLY--RLRPGSREFVQALKKHEIPIAVASTRPRRYLerAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERL 178

                        170       180       190
                 ....*....|....*....|....*....|
gi 3024403   161 GVPPQACIGIEDAQAGIDAINASGMRSVGI 190
Cdd:PLN03243 179 GFIPERCIVFGNSNSSVEAAHDGCMKCVAV 208
PLN02811 PLN02811
hydrolase
 10-188 9.35e-13

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 64.78  E-value: 9.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    10 LDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGGKEGDFNSQERaqLAYRKNLLyvhslREL 89
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPEDF--LVEREAML-----QDL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    90 TVNAVL-PGIRSLLADLRAQQISVGLASVSLNAPTILAALELREFFTF-----CADASQLKNSKPDPEIFLAACAGLGVP 163
Cdd:PLN02811  74 FPTSDLmPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLmhhvvTGDDPEVKQGKPAPDIFLAAARRFEDG 153

                        170       180
                 ....*....|....*....|....*...
gi 3024403   164 ---PQACIGIEDAQAGIDAINASGMRSV 188
Cdd:PLN02811 154 pvdPGKVLVFEDAPSGVEAAKNAGMSVV 181
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 3-188 9.49e-13

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 65.50  E-value: 9.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     3 LQGVIFDLDGVITDT-AHLHFQAWQQIAAEIGisidaqfnesLKGISRDESLRRILQH--GGKEGDF------------- 66
Cdd:PLN02779  40 PEALLFDCDGVLVETeRDGHRVAFNDAFKEFG----------LRPVEWDVELYDELLNigGGKERMTwyfnengwptsti 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    67 -----NSQER----AQLAYRKNLLYVHSLRELTVNAvLPGIRSLLADLRAQQISVGLAS------VSLNAPTILAALELR 131
Cdd:PLN02779 110 ekapkDEEERkelvDSLHDRKTELFKELIESGALPL-RPGVLRLMDEALAAGIKVAVCStsnekaVSKIVNTLLGPERAQ 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 3024403   132 EFFTFCADasQLKNSKPDPEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSV 188
Cdd:PLN02779 189 GLDVFAGD--DVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCI 243
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-189 9.94e-13

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 64.83  E-value: 9.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     1 MKLQGVIFDLDGVITDTA------------HLHFQAW--QQIAAEIGISIDAQFneslkgisrdeslRRILQHGGKEGDF 66
Cdd:PRK13222   4 MDIRAVAFDLDGTLVDSApdlaaavnaalaALGLPPAgeERVRTWVGNGADVLV-------------ERALTWAGREPDE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    67 NSQERAQLAYRKnlLYVHSLRELTVnaVLPGIRSLLADLRAQQISVGLASvslNAPT-----ILAALELREFFT--FCAD 139
Cdd:PRK13222  71 ELLEKLRELFDR--HYAENVAGGSR--LYPGVKETLAALKAAGYPLAVVT---NKPTpfvapLLEALGIADYFSvvIGGD 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 3024403   140 AsqLKNSKPDPEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVG 189
Cdd:PRK13222 144 S--LPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVG 191
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 5-179 2.21e-12

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 62.80  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403      5 GVIFDLDGVITDTAHLHFQAWQQIAAEIGISIdaqfnESLKGISRDESLRRILQHGGKEGDFNS-QERAQLAYRKNLLYV 83
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDP-----ASFKALKQAGGLAEEEWYRIATSALEElQGRFWSEYDAEEAYI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     84 HSLRELtvnavlpgirslLADLRAQQISVGLASvslNAPTILAALELR-----EFFTFcADASQLKNSKPDPEIFLAACA 158
Cdd:TIGR01549  76 RGAADL------------LARLKSAGIKLGIIS---NGSLRAQKLLLRlfglgDYFEL-ILVSDEPGSKPEPEIFLAALE 139

                         170       180
                  ....*....|....*....|....
gi 3024403    159 GLGVPPQAC-IG--IEDAQAGIDA 179
Cdd:TIGR01549 140 SLGVPPEVLhVGdnLNDIEGARNA 163
PRK11587 PRK11587
putative phosphatase; Provisional
 1-208 1.65e-11

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 61.16  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     1 MKLQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDaQFNESLKGISRDESLRRILQhgGKegdfnSQERAQLAYRKnl 80
Cdd:PRK11587   1 MRCKGFLFDLDGTLVDSLPAVERAWSNWADRHGIAPD-EVLNFIHGKQAITSLRHFMA--GA-----SEAEIQAEFTR-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    81 lyvhsLRELTVN-----AVLPGIRSLLADLRAQQI--------SVGLASVSLNAptilAAL-ELREFFTfcadASQLKNS 146
Cdd:PRK11587  71 -----LEQIEATdtegiTALPGAIALLNHLNKLGIpwaivtsgSVPVASARHKA----AGLpAPEVFVT----AERVKRG 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3024403   147 KPDPEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGA-----GLTGAQLLLPSTESLT 208
Cdd:PRK11587 138 KPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNApadtpRLDEVDLVLHSLEQLT 204
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 5-197 1.98e-11

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: 61.18  E-value: 1.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    5 GVIFDLDGVITDTAhlhfqawQQIAAEIGISIDAqfnESLKGISRDEsLRRILQHGGK---EGDFNSQERAQLAYRKNLL 81
Cdd:cd07512   1 AVIFDLDGTLIDSA-------PDLHAALNAVLAA---EGLAPLSLAE-VRSFVGHGAPaliRRAFAAAGEDLDGPLHDAL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   82 YV----HSLRELTV-NAVLPGIRSLLADLRAQQISVGLASVSLNAPT--ILAALELREFFTFCADASQLKNSKPDPEIFL 154
Cdd:cd07512  70 LArfldHYEADPPGlTRPYPGVIEALERLRAAGWRLAICTNKPEAPAraLLSALGLADLFAAVVGGDTLPQRKPDPAPLR 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 3024403  155 AACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGA 197
Cdd:cd07512 150 AAIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYRHA 192
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 6-189 2.59e-11

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: 59.25  E-value: 2.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAHLHFQAWQQIAAEIGisidaqfneslkgisrdeslrrilqhggkegdfnsqerAQLAYRKnllyvhs 85
Cdd:cd07526   3 VIFDCDGVLVDSEVIAARVLVEVLAELG--------------------------------------ARVLAAF------- 37

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   86 LRELTVnavLPGIRSLLADLraqQISVGLASvslNAPT--ILAALE---LREFFT-FCADASQLKNSKPDPEIFLAACAG 159
Cdd:cd07526  38 EAELQP---IPGAAAALSAL---TLPFCVAS---NSSRerLTHSLGlagLLAYFEgRIFSASDVGRGKPAPDLFLHAAAQ 108

                       170       180       190
                ....*....|....*....|....*....|
gi 3024403  160 LGVPPQACIGIEDAQAGIDAINASGMRSVG 189
Cdd:cd07526 109 MGVAPERCLVIEDSPTGVRAALAAGMTVFG 138
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 5-193 6.18e-11

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: 59.56  E-value: 6.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    5 GVIFDLDGVITDTA------------HLHFQAW--QQIAAEIGisidaqfneslKGISRdeSLRRILQH-GGKEGDfnsQ 69
Cdd:cd16417   1 LVAFDLDGTLVDSApdlaeaanamlaALGLPPLpeETVRTWIG-----------NGADV--LVERALTGaREAEPD---E 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   70 ERAQLAYRknlLYVHSLRE-LTVNAVL-PGIRSLLADLRAQQISVGLASvslNAPT-----ILAALELREFFTFCADASQ 142
Cdd:cd16417  65 ELFKEARA---LFDRHYAEtLSVHSHLyPGVKEGLAALKAQGYPLACVT---NKPErfvapLLEALGISDYFSLVLGGDS 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 3024403  143 LKNSKPDPEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAG 193
Cdd:cd16417 139 LPEKKPDPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLTYG 189
PLN02940 PLN02940
riboflavin kinase
 6-190 1.56e-10

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 59.85  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     6 VIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQFNESLKGISRDESLRRILQHGG---KEGDFNSQeraqlayrknllY 82
Cdd:PLN02940  14 VILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGlpcSTDEFNSE------------I 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    83 VHSLRELTVNA-VLPGIRSLLADLRAQQISVGLASVSLNApTILAALEL----REFFTFCADASQLKNSKPDPEIFLAAC 157
Cdd:PLN02940  82 TPLLSEQWCNIkALPGANRLIKHLKSHGVPMALASNSPRA-NIEAKISChqgwKESFSVIVGGDEVEKGKPSPDIFLEAA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 3024403   158 AGLGVPPQACIGIEDAQAGIDAINASGMRSVGI 190
Cdd:PLN02940 161 KRLNVEPSNCLVIEDSLPGVMAGKAAGMEVIAV 193
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 1-179 2.10e-10

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 58.17  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     1 MKLQGVIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQ-FNESLKGISRDESLRRI-LQHGGKEgdfnSQERAQLAYRK 78
Cdd:PRK10563   2 SQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEeVFKRFKGVKLYEIIDIIsKEHGVTL----AKAELEPVYRA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    79 NllyVHSLRELTVNAVlPGIRSLLAdlraqQISVGLASVSlNAPTI-----LAALELREFFTfcaD----ASQLKNSKPD 149
Cdd:PRK10563  78 E---VARLFDSELEPI-AGANALLE-----SITVPMCVVS-NGPVSkmqhsLGKTGMLHYFP---DklfsGYDIQRWKPD 144

                        170       180       190
                 ....*....|....*....|....*....|....
gi 3024403   150 PEIFLAACAGLGVPPQACIGIED----AQAGIDA 179
Cdd:PRK10563 145 PALMFHAAEAMNVNVENCILVDDssagAQSGIAA 178
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 6-193 2.17e-10

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: 57.99  E-value: 2.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAhlhfqawqqiaaeIGI--SIDAQFNE------SLKGISR------DESLRRILQHGGKEgdfnsQER 71
Cdd:cd04302   2 ILFDLDGTLTDSA-------------EGItaSVQYALEElgipvpDESELRRfigpplEDSFRELLPFDEEE-----AQR 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   72 AQLAYRKNllYVHslRELTVNAVLPGIRSLLADLRAQQISVGLASvSLNAPT---ILAALELREFFTFCADASqLKNSKP 148
Cdd:cd04302  64 AVDAYREY--YKE--KGLFENEVYPGIPELLEKLKAAGYRLYVAT-SKPEVFarrILEHFGLDEYFDGIAGAS-LDGSRV 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 3024403  149 D-PEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAG 193
Cdd:cd04302 138 HkADVIRYALDTLGIAPEQAVMIGDRKHDIIGARANGIDSIGVLYG 183
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 3-193 1.97e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 56.00  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     3 LQGVIFDLDGVITDTAHLHFQAWQQIAAEI----GISIDAQF-NESLKGISRDESLRRI----LQHGGKegdFNSQERAq 73
Cdd:PLN02770  22 LEAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEEFfVENIAGKHNEDIALGLfpddLERGLK---FTDDKEA- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    74 lAYRKnllyVHSLRELTVNAvLPGIRSLLADLRAQQISVGLASVSlNAPTILAALELREFFTFCADASQLKNSKPDPEIF 153
Cdd:PLN02770  98 -LFRK----LASEQLKPLNG-LYKLKKWIEDRGLKRAAVTNAPRE-NAELMISLLGLSDFFQAVIIGSECEHAKPHPDPY 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 3024403   154 LAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAG 193
Cdd:PLN02770 171 LKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTR 210
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 5-192 1.97e-08

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 53.72  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     5 GVIFDLDGVIT-DTAHLHFQAWQQIAAEIGISIDAQFneslkgisrdeSLRRIlqhggkEGDFNSQ-------------E 70
Cdd:PLN02575 133 GAIFEWEGVIIeDNPDLENQAWLTLAQEEGKSPPPAF-----------ILRRV------EGMKNEQaisevlcwsrdpaE 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    71 RAQLAYRKNLLY------VHSLREltvnavlpGIRSLLADLRAQQISVGLASVSLNA--PTILAALELREFFTFCADASQ 142
Cdd:PLN02575 196 LRRMATRKEEIYqalqggIYRLRT--------GSQEFVNVLMNYKIPMALVSTRPRKtlENAIGSIGIRGFFSVIVAAED 267

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 3024403   143 LKNSKPDPEIFLAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGA 192
Cdd:PLN02575 268 VYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDARMKCVAVAS 317
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 99-188 1.89e-07

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: 48.44  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   99 RSLLADLRAQQISVGLASvslNA----PTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPPQACIGIEDA- 173
Cdd:cd16415  13 VETLKDLKEKGLKLAVVS---NFdrrlRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDDl 89

                        90
                ....*....|....*
gi 3024403  174 QAGIDAINASGMRSV 188
Cdd:cd16415  90 KNDYLGARAVGWHAL 104
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 6-200 5.61e-07

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: 48.12  E-value: 5.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    6 VIFDLDGVITDTAHLHFQAWQQIAAEIGI-SIDAQFNESLKGISRDESLRRIlqhggkegDFNSQERAQLAYRKNLLYVH 84
Cdd:cd04303   2 IIFDFDGTLADSFPWFLSILNQLAARHGFkTVDEEEIEQLRQLSSREILKQL--------GVPLWKLPLIAKDFRRLMAE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   85 SLRELtvnAVLPGIRSLLADLRAQqiSVGLASVSLNAPT----ILAALELREFFTfCADASQLKNSKPDPEIFLAACagl 160
Cdd:cd04303  74 AAPEL---ALFPGVEDMLRALHAR--GVRLAVVSSNSEEnirrVLGPEELISLFA-VIEGSSLFGKAKKIRRVLRRT--- 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 3024403  161 GVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLL 200
Cdd:cd04303 145 KITAAQVIYVGDETRDIEAARKVGLAFAAVSWGYAKPEVL 184
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 98-190 2.13e-06

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: 45.08  E-value: 2.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   98 IRSLLADLRAQQISVGLASvslNAPT-----ILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPPQACIGIED 172
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVT---NRSRealraLLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGD 88

                        90
                ....*....|....*...
gi 3024403  173 AQAGIDAINASGMRSVGI 190
Cdd:cd01427  89 SENDIEAARAAGGRTVAV 106
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 1-200 4.37e-06

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 45.79  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     1 MKLQGVIFDLDGVITDTAHLHFQAWQQiaaeigisidaQFNESLKG-ISRDESLRRI---LQHGGKEGDFNSQERAQLAY 76
Cdd:PRK13288   1 MKINTVLFDLDGTLINTNELIISSFLH-----------TLKTYYPNqYKREDVLPFIgpsLHDTFSKIDESKVEEMITTY 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    77 RKnllYVHSLRELTVNAvLPGIRSLLADLRAQQISVGLASVSLNApTILAALEL---REFFTFCADASQLKNSKPDPEIF 153
Cdd:PRK13288  70 RE---FNHEHHDELVTE-YETVYETLKTLKKQGYKLGIVTTKMRD-TVEMGLKLtglDEFFDVVITLDDVEHAKPDPEPV 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 3024403   154 LAACAGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLL 200
Cdd:PRK13288 145 LKALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVAWTIKGREYL 191
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 6-193 5.27e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 46.01  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     6 VIFDLDGVITDTAHLHFQAWQQIAAEIGISIDAQfnESLK---GISRDESLRRILQhGGKEGDFNSQERAQLAYRKNLLY 82
Cdd:PRK13223  16 VMFDLDGTLVDSVPDLAAAVDRMLLELGRPPAGL--EAVRhwvGNGAPVLVRRALA-GSIDHDGVDDELAEQALALFMEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    83 VHSLRELTVnaVLPGIRSLLADLRAQQISVGLASvslNAPT-----ILAALELREFFTFCADASQLKNSKPDPEIFLAAC 157
Cdd:PRK13223  93 YADSHELTV--VYPGVRDTLKWLKKQGVEMALIT---NKPErfvapLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVM 167

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 3024403   158 AGLGVPPQACIGIEDAQAGIDAINASGMRSVGIGAG 193
Cdd:PRK13223 168 KMAGVPPSQSLFVGDSRSDVLAAKAAGVQCVALSYG 203
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 3-211 1.05e-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: 44.98  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    3 LQGVIFDLDGVITDTAHLH-FQAWQQIAAEIGISIDAQFNESLKGISRDESLRRIL-------------QHGGKEGD--- 65
Cdd:cd02586   1 IEAVIFDWAGTTVDYGSFApVNAFVEAFAQRGVQITLEEARKPMGLLKIDHIRALLemprvaeawravfGRLPTEADvda 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   66 -FNSQERAQLAyrknllyvhSLRELTvnAVLPGIRSLLADLRAQQISVG---------LASVSLNAptilAALELREFFT 135
Cdd:cd02586  81 lYEEFEPILIA---------SLAEYS--SPIPGVLEVIAKLRARGIKIGsttgytremMDIVLPEA----AAQGYRPDSL 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403  136 FCADasQLKNSKPDPEIFLAACAGLGV-PPQACIGIEDAQAGI-DAINAsGMRSVGI-----GAGLTGAQLLLPSTESLT 208
Cdd:cd02586 146 VTPD--DVPAGRPYPWMCYKNAIELGVyDVAAVVKVGDTVPDIkEGLNA-GMWTVGVilsgnELGLSEEEVEALDSEELA 222


                ...
gi 3024403  209 WPR 211
Cdd:cd02586 223 ARR 225
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 7-188 9.48e-05

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: 41.59  E-value: 9.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    7 IFDLDGVITDTAHLHFQAWQQIAAEIGISIDAqfnESLKGISRDESLRRILQHGGKEGDFNsQERAQLAyrknllyvhsL 86
Cdd:cd07523   3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDL---ETVYKIIKESSVQFAIQYYAEVPDLE-EEYKELE----------A 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   87 RELTVNAVLPGIRSLLADLRAQQI-SVGLASVSLNAPTILAALELREFFTFCADASQLKNSKPDPEIFLAACAGLGVPPQ 165
Cdd:cd07523  69 EYLAKPILFPGAKAVLRWIKEQGGkNFLMTHRDHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPE 148

                       170       180
                ....*....|....*....|...
gi 3024403  166 ACIGIEDAQAGIDAINASGMRSV 188
Cdd:cd07523 149 ETVMIGDRELDIEAGHNAGISTI 171
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 1-195 1.48e-04

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 41.77  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     1 MKLQGVIFDLDGVITDtahlhF------QAWQQIAAEIGISIDAQFNESLKGISRDESLRRIL-----------QHGGKE 63
Cdd:PRK13478   2 MKIQAVIFDWAGTTVD-----FgsfaptQAFVEAFAQFGVEITLEEARGPMGLGKWDHIRALLkmprvaarwqaVFGRLP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    64 GD------FNSQERAQLAyrknllyvhSLRELTvnAVLPGIRSLLADLRAQQISVG---------LASVSLNAptilAAL 128
Cdd:PRK13478  77 TEadvdalYAAFEPLQIA---------KLADYA--TPIPGVLEVIAALRARGIKIGsttgytremMDVVVPLA----AAQ 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3024403   129 ELREFFTFCADasQLKNSKPDPEIFLAACAGLGV-PPQACIGIEDAQAGID-AINAsGMRSVGI-----GAGLT 195
Cdd:PRK13478 142 GYRPDHVVTTD--DVPAGRPYPWMALKNAIELGVyDVAACVKVDDTVPGIEeGLNA-GMWTVGVilsgnELGLS 212
Hydrolase_like pfam13242
HAD-hyrolase-like;
147-201 1.95e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 38.75  E-value: 1.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 3024403    147 KPDPEIFLAACAGLGVPPQACIGIEDAQA-GIDAINASGMRSVGIGAGLTGAQLLL 201
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTGVTRPADLE 59
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 92-188 3.16e-04

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: 39.06  E-value: 3.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   92 NAVLPGIRSLLADLRaQQISVGLASvslNAPTI-----LAALELREFFtfcaDA----SQLKNSKPDPEIFLAACAGLGV 162
Cdd:cd04305   8 DTLLPGAKELLEELK-KGYKLGIIT---NGPTEvqwekLEQLGIHKYF----DHivisEEVGVQKPNPEIFDYALNQLGV 79

                        90       100
                ....*....|....*....|....*...
gi 3024403  163 PPQACIGIED-AQAGID-AINAsGMRSV 188
Cdd:cd04305  80 KPEETLMVGDsLESDILgAKNA-GIKTV 106
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 98-190 6.85e-04

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: 37.82  E-value: 6.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   98 IRSLLADLRAQQISVGLASVSLNAPTILAALELREF-FTFCADASQLKNSKPDPEIFLAACAGLGVPPQACIGIEDAQAG 176
Cdd:cd16421  12 ILELLKALRQKGIKLAVLSNKPNEAVQVLVEELFPGsFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGVD 91

                        90
                ....*....|....
gi 3024403  177 IDAINASGMRSVGI 190
Cdd:cd16421  92 MQTARNAGMDEIGV 105
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 7-188 7.49e-04

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: 39.15  E-value: 7.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    7 IFDLDgvitDTAH-LHFQAWQQIAAeigiSIDAQFNESLkGISRDE--SLRRILQH------GGK--EGDFNSQERaqla 75
Cdd:cd02604   3 FFDLD----NTLYpLSTGLFDQIQA----RITEFVATKL-GLSPEEarRLRKSYYKeygttlRGLmaEHGIDPDEF---- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   76 yrknLLYVHSLRELTVNAVLPGIRSLLADLRAQQISVGLASVSlNAPTILAALELREFF--TFCADASQlKNSKPDPEIF 153
Cdd:cd02604  70 ----LDRVVHLILYDHLKPDPKLRNLLLALPGRKIIFTNASKN-HAIRVLKRLGLADLFdgIFDIEYAG-PDPKPHPAAF 143

                       170       180       190
                ....*....|....*....|....*....|....*
gi 3024403  154 LAACAGLGVPPQACIGIEDAQAGIDAINASGMRSV 188
Cdd:cd02604 144 EKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTV 178
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 51-190 2.13e-03

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: 38.02  E-value: 2.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403   51 ESLRRILQHGGKEGDfnSQERAQLAyrknllyvHSLRELTVnavLPGIRSLLADLRAQQISVGLASVSLN--APTILAAL 128
Cdd:cd02588  62 DALRATAAELGLELD--ESDLDELG--------DAYLRLPP---FPDVVAGLRRLREAGYRLAILSNGSPdlIEDVVANA 128

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3024403  129 ELREFF--TFCADASQLknSKPDPEIFLAACAGLGVPPQACIGIedAQAGIDAINAS--GMRSVGI 190
Cdd:cd02588 129 GLRDLFdaVLSAEDVRA--YKPAPAVYELAAERLGVPPDEILHV--ASHAWDLAGARalGLRTAWI 190
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 3-203 7.67e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 36.61  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403     3 LQGVIFDLDGVITDTAHLHFQAWQQIAAEIGIS-IDAQFNESLkgisRDESLRRILQHGGkegdFNSQERAQLAYRKNLL 81
Cdd:PRK13225  62 LQAIIFDFDGTLVDSLPTVVAIANAHAPDFGYDpIDERDYAQL----RQWSSRTIVRRAG----LSPWQQARLLQRVQRQ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3024403    82 YVHSLRELTVnavLPGIRSLLADLRAQQISVGLASVS--LNAPTILAALELREFFTFCADASQLKNSKpdpEIFLAACAG 159
Cdd:PRK13225 134 LGDCLPALQL---FPGVADLLAQLRSRSLCLGILSSNsrQNIEAFLQRQGLRSLFSVVQAGTPILSKR---RALSQLVAR 207

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 3024403   160 LGVPPQACIGIEDAQAGIDAINASGMRSVGIGAGLTGAQLLLPS 203
Cdd:PRK13225 208 EGWQPAAVMYVGDETRDVEAARQVGLIAVAVTWGFNDRQSLVAA 251
 
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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