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Conserved domains on  [gi|2787884964|gb|XDQ86226|]
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beta-phosphoglucomutase [Lactiplantibacillus plantarum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bPGM super family cl33302
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 9-195 1.16e-92

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


The actual alignment was detected with superfamily member TIGR01990:

Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 269.18  E-value: 1.16e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILAQGHRenDFTPAQKQALATEKNTNYLQ 88
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 LVNQMTPANILPGITAFLTELTTAGYALSLASASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNP 168
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 2787884964 169 ADCIGVEDAAAGVQSIKGAGETAIGIG 195
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 9-195 1.16e-92

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


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 269.18  E-value: 1.16e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILAQGHRenDFTPAQKQALATEKNTNYLQ 88
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 LVNQMTPANILPGITAFLTELTTAGYALSLASASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNP 168
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 2787884964 169 ADCIGVEDAAAGVQSIKGAGETAIGIG 195
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 9-221 2.42e-76

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: 227.56  E-value: 2.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADkvgvswndqladalkgisrmdslnlilaqghrendftpaqKQALATEKNTNYLQ 88
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAWKKLAD----------------------------------------KEELAARKNRIYVE 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 LVNQMTPANILPGITAFLTELTTAGYALSLASASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNP 168
Cdd:cd02598    41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2787884964 169 ADCIGVEDAAAGVQSIKGAGETAIGIGDPTVLAAADINFTDTT-QLTLANIKAQ 221
Cdd:cd02598   121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGADIVVPDTTaDLTIEELLEV 174
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-213 5.66e-61

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 189.65  E-value: 5.66e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILAQGHRenDFTPAqkqALATEKNTNY 86
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL--DLPEE---ELAARKEELY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  87 LQLVnQMTPANILPGITAFLTELTTAGYALSLASASK--NAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEIL 164
Cdd:COG0637    77 RELL-AEEGLPLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2787884964 165 GLNPADCIGVEDAAAGVQSIKGAGETAIGIGDPT----VLAAADINFTDTTQL 213
Cdd:COG0637   156 GVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGtaeeELAGADLVVDDLAEL 208
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-188 7.85e-24

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 93.80  E-value: 7.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIAD-----KVGVSWNDQLADALKGI---SRMDSLNLILAQGHRENDFTPAQKQAL 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASehplaKAIVAAAEDLPIPVEDFtarLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  79 aTEKNTNYLQLVNQMTPANILPGITAFLTELTTAGYALSLASAS--KNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEI 156
Cdd:pfam00702  81 -TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDnpEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2787884964 157 FRRGAEILGLNPADCIGVEDAAAGVQSIKGAG 188
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
9-192 1.98e-23

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 92.83  E-value: 1.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGisrmdSLNLILAQG---HRENDFTPaqkQALATEKNtn 85
Cdd:PRK10725    7 GLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNG-----SPTWRIAQAiieLNQADLDP---HALAREKT-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  86 ylQLVNQMTPANI--LPgitafLTELTTAGY-----ALSLASASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFR 158
Cdd:PRK10725   77 --EAVKSMLLDSVepLP-----LIEVVKAWHgrrpmAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFL 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2787884964 159 RGAEILGLNPADCIGVEDAAAGVQSIKGAGETAI 192
Cdd:PRK10725  150 RCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 9-195 1.16e-92

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


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 269.18  E-value: 1.16e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILAQGHRenDFTPAQKQALATEKNTNYLQ 88
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGK--KYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 LVNQMTPANILPGITAFLTELTTAGYALSLASASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNP 168
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 2787884964 169 ADCIGVEDAAAGVQSIKGAGETAIGIG 195
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 9-221 2.42e-76

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: 227.56  E-value: 2.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADkvgvswndqladalkgisrmdslnlilaqghrendftpaqKQALATEKNTNYLQ 88
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAWKKLAD----------------------------------------KEELAARKNRIYVE 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 LVNQMTPANILPGITAFLTELTTAGYALSLASASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNP 168
Cdd:cd02598    41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2787884964 169 ADCIGVEDAAAGVQSIKGAGETAIGIGDPTVLAAADINFTDTT-QLTLANIKAQ 221
Cdd:cd02598   121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGADIVVPDTTaDLTIEELLEV 174
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-213 5.66e-61

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 189.65  E-value: 5.66e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILAQGHRenDFTPAqkqALATEKNTNY 86
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL--DLPEE---ELAARKEELY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  87 LQLVnQMTPANILPGITAFLTELTTAGYALSLASASK--NAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEIL 164
Cdd:COG0637    77 RELL-AEEGLPLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2787884964 165 GLNPADCIGVEDAAAGVQSIKGAGETAIGIGDPT----VLAAADINFTDTTQL 213
Cdd:COG0637   156 GVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGtaeeELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-194 3.99e-58

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: 181.77  E-value: 3.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILAqgHRENDFTPAQKQALATEKNTNY 86
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILK--LRGDGLSLEEIHQLAERKNELY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  87 LQLVNqMTPANILPGITAFLTELTTAGYALSLASASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGL 166
Cdd:TIGR02009  79 RELLR-LTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGV 157

                         170       180
                  ....*....|....*....|....*...
gi 2787884964 167 NPADCIGVEDAAAGVQSIKGAGETAIGI 194
Cdd:TIGR02009 158 PPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-194 9.10e-29

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: 106.35  E-value: 9.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  10 FVFDLDGVITDTSTFH-SQAWHQIADKVGVSWNDQLADALKGisrmdSLNLILAQGHRENDftPAQKQALatEKNTNYLQ 88
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIaKLINREELGLVPDELGVSAVGRLEL-----ALRRFKAQYGRTIS--PEDAQLL--YKQLFYEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 LVNQMTPAnILPGITAFLTELTTAGYALSLASAS-KNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLN 167
Cdd:TIGR01509  73 IEEEAKLK-PLPGVRALLEALRARGKKLALLTNSpRAHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLE 151

                         170       180
                  ....*....|....*....|....*..
gi 2787884964 168 PADCIGVEDAAAGVQSIKGAGETAIGI 194
Cdd:TIGR01509 152 PSECVFVDDSPAGIEAAKAAGMHTVGV 178
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 9-196 1.08e-26

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: 100.00  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADKvgvswNDQLADalkgisrmdslnLILAQGHRendftpaqkqalatekntnylq 88
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAWQLLERK-----NALLLE------------LIASEGLK---------------------- 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 lvnqmtpanILPGITAFLTELTTAGYALSLASAS--KNAPLVLRKLGLS-DYFTKAVDPASLKHGKPDPEIFRRGAEILG 165
Cdd:cd07505    42 ---------LKPGVVELLDALKAAGIPVAVATSSsrRNVELLLLELGLLrGYFDVIVSGDDVERGKPAPDIYLLAAERLG 112

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2787884964 166 LNPADCIGVEDAAAGVQSIKGAGETAIGIGD 196
Cdd:cd07505   113 VDPERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-188 7.85e-24

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 93.80  E-value: 7.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIAD-----KVGVSWNDQLADALKGI---SRMDSLNLILAQGHRENDFTPAQKQAL 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASehplaKAIVAAAEDLPIPVEDFtarLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  79 aTEKNTNYLQLVNQMTPANILPGITAFLTELTTAGYALSLASAS--KNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEI 156
Cdd:pfam00702  81 -TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDnpEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2787884964 157 FRRGAEILGLNPADCIGVEDAAAGVQSIKGAG 188
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
9-192 1.98e-23

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 92.83  E-value: 1.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGisrmdSLNLILAQG---HRENDFTPaqkQALATEKNtn 85
Cdd:PRK10725    7 GLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNG-----SPTWRIAQAiieLNQADLDP---HALAREKT-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  86 ylQLVNQMTPANI--LPgitafLTELTTAGY-----ALSLASASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFR 158
Cdd:PRK10725   77 --EAVKSMLLDSVepLP-----LIEVVKAWHgrrpmAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFL 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2787884964 159 RGAEILGLNPADCIGVEDAAAGVQSIKGAGETAI 192
Cdd:PRK10725  150 RCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-213 1.44e-21

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 88.45  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIADKVGV-SWNDQLADALKGISRMDSLNLILAqghrenDFTPAQKQALATEKNTN 85
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLpPLDLEELRALIGLGLRELLRRLLG------EDPDEELEELLARFREL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  86 YLQLVNQMTPanILPGITAFLTELTTAGYALSLASaSKNAPLV---LRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAE 162
Cdd:COG0546    75 YEEELLDETR--LFPGVRELLEALKARGIKLAVVT-NKPREFAerlLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALE 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2787884964 163 ILGLNPADCIGVEDAAAGVQSIKGAGETAI----GIGDPTVLAA--ADINFTDTTQL 213
Cdd:COG0546   152 RLGLDPEEVLMVGDSPHDIEAARAAGVPFIgvtwGYGSAEELEAagADYVIDSLAEL 208
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 9-214 3.93e-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: 87.01  E-value: 3.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADKVGVSwNDQLADALKGISRMDSLNLILAqghrenDFTPAQkQALATEKntnylQ 88
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVD-PEEVLKVSHGRRAIDVIRKLAP------DDADIE-LVLALET-----E 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 LVNQMTPANI-LPGITAFLTEL----------TTAGYALSlASASKNAPLvlrklGLSDYFTKAVDpasLKHGKPDPEIF 157
Cdd:cd07527    68 EPESYPEGVIaIPGAVDLLASLpaagdrwaivTSGTRALA-EARLEAAGL-----PHPEVLVTADD---VKNGKPDPEPY 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2787884964 158 RRGAEILGLNPADCIGVEDAAAGVQSIKGAGETAIGIGDPTVLAA-----ADINFTDTTQLT 214
Cdd:cd07527   139 LLGAKLLGLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQleaagADLVVEDLSDIS 200
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 10-205 1.23e-20

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: 85.00  E-value: 1.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  10 FVFDLDGVITDTSTFHSQAWhqiadkvgvswndqladalkgisrmdslnlilaqghrendftpaqKQALATEKNTNYLQL 89
Cdd:cd16423     2 VIFDFDGVIVDTEPLWYEAW---------------------------------------------QELLNERRNELIKRQ 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  90 VNQMTPANILPGITAFLTELTTAGYALSLASAS--KNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLN 167
Cdd:cd16423    37 FSEKTDLPPIEGVKELLEFLKEKGIKLAVASSSprRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVN 116

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2787884964 168 PADCIGVEDAAAGVQSIKGAGETAIGI----GDPTVLAAADI 205
Cdd:cd16423   117 PEECVVIEDSRNGVLAAKAAGMKCVGVpnpvTGSQDFSKADL 158
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-184 3.97e-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: 82.00  E-value: 3.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIADKVGvswndQLADALKGISRMDSLNLILAQGHRENDFTPAQ---------KQA 77
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLG-----LLDEAEELAEAYRAIEYALWRRYERGEITFAEllrrlleelGLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  78 LATEKNTNYLQLVNQMTPANilPGITAFLTELTTAGYALSLAS--ASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPE 155
Cdd:COG1011    76 LAEELAEAFLAALPELVEPY--PDALELLEALKARGYRLALLTngSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPE 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2787884964 156 IFRRGAEILGLNPADCIGVED---------AAAGVQSI 184
Cdd:COG1011   154 IFELALERLGVPPEEALFVGDspetdvagaRAAGMRTV 191
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-194 4.61e-19

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 81.09  E-value: 4.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  11 VFDLDGVITDTSTFHSQAWHQIADKVGVS-WNDQLADALKGISRMDSLNLILAQGHRENDFtPAQKQALATEKNTNYLQL 89
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEFGYGeLSEEEILKFIGLPLREIFRYLGVSEDEEEKI-EFYLRKYNEELHDKLVKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  90 vnqmtpaniLPGITAFLTELTTAGYALSLASaSKNAPLV---LRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGL 166
Cdd:pfam13419  81 ---------YPGIKELLEELKEQGYKLGIVT-SKSRENVeefLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGL 150

                         170       180
                  ....*....|....*....|....*...
gi 2787884964 167 NPADCIGVEDAAAGVQSIKGAGETAIGI 194
Cdd:pfam13419 151 KPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
PRK11587 PRK11587
putative phosphatase; Provisional
 8-198 1.90e-17

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 77.73  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   8 KGFVFDLDGVITDTSTFHSQAWHQIADKVGVSwNDQLADALKGISRMDSLNLILAqGHRENDFtpaQKQALATEKntnyl 87
Cdd:PRK11587    4 KGFLFDLDGTLVDSLPAVERAWSNWADRHGIA-PDEVLNFIHGKQAITSLRHFMA-GASEAEI---QAEFTRLEQ----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  88 qlVNQMTPANI--LPGITAFLTELTTAGY--------ALSLASASKNAPlvlrKLGLSDYFTKAvdpASLKHGKPDPEIF 157
Cdd:PRK11587   74 --IEATDTEGItaLPGAIALLNHLNKLGIpwaivtsgSVPVASARHKAA----GLPAPEVFVTA---ERVKRGKPEPDAY 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2787884964 158 RRGAEILGLNPADCIGVEDAAAGVQSIKGAGETAIGIGDPT 198
Cdd:PRK11587  145 LLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAPA 185
PRK10826 PRK10826
hexitol phosphatase HxpB;
7-220 4.71e-17

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 76.52  E-value: 4.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIADKVGV--SWNDQLADALkGIsRMDslnLILAQGHRENDFTPAQKQALATEKNT 84
Cdd:PRK10826    7 ILAAIFDMDGLLIDSEPLWDRAELDVMASLGVdiSRREELPDTL-GL-RID---QVVDLWYARQPWNGPSRQEVVQRIIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  85 NYLQLVNQMTPAniLPGITAFLTELTTAGYALSLASASKNAPL--VLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAE 162
Cdd:PRK10826   82 RVISLIEETRPL--LPGVREALALCKAQGLKIGLASASPLHMLeaVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2787884964 163 ILGLNPADCIGVEDAAAGVQSIKGAGETAIGIGDP-----TVLAAADINFTDTTQLTLANIKA 220
Cdd:PRK10826  160 KLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPeqqndPRWALADVKLESLTELTAADLLG 222
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 11-192 1.22e-14

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: 69.72  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  11 VFDLDGVITDTSTFHSQAW-HQIADKVGVSWN------DQLADALKGISRMDSLNLILAQGHRENDFTPAQKQALATEKN 83
Cdd:cd07528     3 IFDVDGTLAETEELHRRAFnNAFFAERGLDWYwdrelyGELLRVGGGKERIAAYFEKVGWPESAPKDLKELIADLHKAKT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  84 TNYLQLVNQMTPAnILPGITAFLTELTTAGYALSLASAS--KNAPLVLRKLGLSDY---FTKAVDPASLKHGKPDPEIFR 158
Cdd:cd07528    83 ERYAELIAAGLLP-LRPGVARLIDEAKAAGVRLAIATTTspANVDALLSALLGPERraiFDAIAAGDDVAEKKPDPDIYL 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2787884964 159 RGAEILGLNPADCIGVEDAAAGVQSIKGAGETAI 192
Cdd:cd07528   162 LALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
PLN02940 PLN02940
riboflavin kinase
 11-199 1.08e-12

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 66.01  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  11 VFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILaqghrENDFTPAQKQALATEKntnYLQLV 90
Cdd:PLN02940   15 ILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVV-----EDYGLPCSTDEFNSEI---TPLLS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  91 NQMTPANILPGITAFLTELTTAGYALSLASASKNAPLVLR---KLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLN 167
Cdd:PLN02940   87 EQWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKiscHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVE 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2787884964 168 PADCIGVEDAAAGVQSIKGAGETAIGIgdPTV 199
Cdd:PLN02940  167 PSNCLVIEDSLPGVMAGKAAGMEVIAV--PSI 196
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 7-192 2.05e-12

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: 63.52  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHS-QAWHQIadkvgvswNDQLADALKGISRMDSLNLILAQGH-RENDFTPAQKQALATEKNt 84
Cdd:cd02603     1 IRAVLFDFGGVLIDPDPAAAvARFEAL--------TGEPSEFVLDTEGLAGAFLELERGRiTEEEFWEELREELGRPLS- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  85 nYLQLVNQMTPAN-ILPGITAFLTELTTAGYALSLASaskNAPLVLRKLGLS------DYFTKAVDPASLKHGKPDPEIF 157
Cdd:cd02603    72 -AELFEELVLAAVdPNPEMLDLLEALRAKGYKVYLLS---NTWPDHFKFQLEllprrgDLFDGVVESCRLGVRKPDPEIY 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2787884964 158 RRGAEILGLNPADCIGVEDAAAGVQSIKGAGETAI 192
Cdd:cd02603   148 QLALERLGVKPEEVLFIDDREENVEAARALGIHAI 182
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 2-192 2.52e-12

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 64.34  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   2 VKFAAIKGFVFDLDGVITDTST-FHSQAWHQI---ADKVGVSWNDQLADALKGIS----RMD---SLNLILAQGHRENDF 70
Cdd:PLN02779   35 SASALPEALLFDCDGVLVETERdGHRVAFNDAfkeFGLRPVEWDVELYDELLNIGggkeRMTwyfNENGWPTSTIEKAPK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  71 TPAQKQALATE----KNTNYLQLVNQMT-PANilPGITAFLTELTTAGYALSLASAS--KNAPLVLRKLGLSDYFTK--- 140
Cdd:PLN02779  115 DEEERKELVDSlhdrKTELFKELIESGAlPLR--PGVLRLMDEALAAGIKVAVCSTSneKAVSKIVNTLLGPERAQGldv 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2787884964 141 -AVDPASLKhgKPDPEIFRRGAEILGLNPADCIGVEDAAAGVQSIKGAGETAI 192
Cdd:PLN02779  193 fAGDDVPKK--KPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCI 243
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 99-193 6.43e-12

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: 60.80  E-value: 6.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  99 LPGITAFLTELTTAgYALSLASASKNAPLVLRKLGLSDYFT-KAVDPASLKHGKPDPEIFRRGAEILGLNPADCIGVEDA 177
Cdd:cd07526    44 IPGAAAALSALTLP-FCVASNSSRERLTHSLGLAGLLAYFEgRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIEDS 122

                          90
                  ....*....|....*.
gi 2787884964 178 AAGVQSIKGAGETAIG 193
Cdd:cd07526   123 PTGVRAALAAGMTVFG 138
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 100-194 2.47e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 56.78  E-value: 2.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  100 PGITAFLTELTTAGYALSLASASK----NAPLVLRKLGLSDyFTKAVDPASLKHGKPDPEIFRRGAEILGLNPADCIGVE 175
Cdd:PLN02919   164 PGALELITQCKNKGLKVAVASSADrikvDANLAAAGLPLSM-FDAIVSADAFENLKPAPDIFLAAAKILGVPTSECVVIE 242

                           90
                   ....*....|....*....
gi 2787884964  176 DAAAGVQSIKGAGETAIGI 194
Cdd:PLN02919   243 DALAGVQAARAAGMRCIAV 261
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 9-219 2.62e-09

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 55.81  E-value: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVIT-DTSTFHSQAWHQIADKVGVSWNDQ-LADALKGISRMDSLNLILAQGHrenDFTPAQKQALATEKNTNY 86
Cdd:PLN03243   26 GVVLEWEGVIVeDDSELERKAWRALAEEEGKRPPPAfLLKRAEGMKNEQAISEVLCWSR---DFLQMKRLAIRKEDLYEY 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  87 LQlvnqMTPANILPGITAFLTELTTAGYALSLASASKNAPL--VLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEIL 164
Cdd:PLN03243  103 MQ----GGLYRLRPGSREFVQALKKHEIPIAVASTRPRRYLerAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2787884964 165 GLNPADCIGVEDAAAGVQSIKGAGETAIGI-GDPTV--LAAADINFTDTTQLTLANIK 219
Cdd:PLN03243  179 GFIPERCIVFGNSNSSVEAAHDGCMKCVAVaGKHPVyeLSAGDLVVRRLDDLSVVDLK 236
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 11-188 2.95e-09

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: 54.66  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  11 VFDLDGVITDTSTFHSQAWHQIADKVG--VSWNDQladalkgiSRMDSLNLILAQGHRENDFT-PAQKQALATEKNTNYL 87
Cdd:cd07529     5 IFDMDGLLLDTERIYTETTQEILARYGktYTWDVK--------AKMMGRPASEAARIIVDELKlPMSLEEEFDEQQEALA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  88 QLvnQMTPANILPGITAFLTELTTAGYALSLASASKNAPLVLRK------LGLSDYFTKAVDPASLKHGKPDPEIFRRGA 161
Cdd:cd07529    77 EL--FMGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTsrhkelFSLFHHVVTGDDPEVKGRGKPAPDIFLVAA 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 2787884964 162 EILG---LNPADCIGVEDAAAGVQSIKGAG 188
Cdd:cd07529   155 KRFNeppKDPSKCLVFEDSPNGVKAAKAAG 184
PLN02811 PLN02811
hydrolase
 14-197 3.73e-09

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 54.76  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  14 LDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILAQGHRENDFTPAQkqaLATEKNTnylqLVNQM 93
Cdd:PLN02811    1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPED---FLVEREA----MLQDL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  94 TP-ANILPGITAFLTELTTAGYALSLASASKNAPLVLRK------LGLSDYFTKAVDPAsLKHGKPDPEIF---RRGAEI 163
Cdd:PLN02811   74 FPtSDLMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTqrhgelFSLMHHVVTGDDPE-VKQGKPAPDIFlaaARRFED 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2787884964 164 LGLNPADCIGVEDAAAGVQSIKGAGETAIGIGDP 197
Cdd:PLN02811  153 GPVDPGKVLVFEDAPSGVEAAKNAGMSVVMVPDP 186
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 100-194 1.96e-08

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: 52.62  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964 100 PGITAFLTELTTAGYALSLASaSKNAPLV---LRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNPADCIGVED 176
Cdd:cd16417    90 PGVKEGLAALKAQGYPLACVT-NKPERFVaplLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLGIAPAQMLMVGD 168

                          90
                  ....*....|....*...
gi 2787884964 177 AAAGVQSIKGAGETAIGI 194
Cdd:cd16417   169 SRNDILAARAAGCPSVGL 186
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 9-188 3.68e-08

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 51.24  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVITDTSTFHSQAWHQIADKVGvswndqlaDALKGISRMDSLnLILAQGHRENDFTPAQKQALATEKntnYLQ 88
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFG--------LDPASFKALKQA-GGLAEEEWYRIATSALEELQGRFW---SEY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  89 LVNQMTpaniLPGITAFLTELTTAGYALSLASA--SKNAPLVLRKLGLSDYFtKAVDPASLKHGKPDPEIFRRGAEILGL 166
Cdd:TIGR01549  69 DAEEAY----IRGAADLLARLKSAGIKLGIISNgsLRAQKLLLRLFGLGDYF-ELILVSDEPGSKPEPEIFLAALESLGV 143

                         170       180
                  ....*....|....*....|..
gi 2787884964 167 NPaDCIGVEDAAAGVQSIKGAG 188
Cdd:TIGR01549 144 PP-EVLHVGDNLNDIEGARNAG 164
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 105-192 1.07e-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: 49.21  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964 105 FLTELTTAGYALSLASaskNA----PLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNPADCIGVEDA-AA 179
Cdd:cd16415    15 TLKDLKEKGLKLAVVS---NFdrrlRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDDlKN 91

                          90
                  ....*....|...
gi 2787884964 180 GVQSIKGAGETAI 192
Cdd:cd16415    92 DYLGARAVGWHAL 104
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 7-218 1.40e-07

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: 49.97  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTStfhsqawhqiaDKVGVSWNDQLAD-ALKGISRMDSLNLIlAQGHRE--NDFTPAQKQALATEKN 83
Cdd:cd02616     1 ITTILFDLDGTLIDTN-----------ELIIKSFNHTLKEyGLEGYTREEVLPFI-GPPLREtfEKIDPDKLEDMVEEFR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  84 TNYLQLVNQMTpaNILPGITAFLTELTTAGYALSLASaSKNAPLVLRKL---GLSDYFTKAVDPASLKHGKPDPEIFRRG 160
Cdd:cd02616    69 KYYREHNDDLT--KEYPGVYETLARLKSQGIKLGVVT-TKLRETALKGLkllGLDKYFDVIVGGDDVTHHKPDPEPVLKA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2787884964 161 AEILGLNPADCIGVEDAAAGVQSIKGAG-ETAI---GIGDPTVLAAADINFTDTTQLTLANI 218
Cdd:cd02616   146 LELLGAEPEEALMVGDSPHDILAGKNAGvKTVGvtwGYKGREYLKAFNPDFIIDKMSDLLTI 207
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
3-188 1.91e-07

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 49.81  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   3 KFAAIKGFVFDLDGVITDTST-FHSQAWHQIADK----VGV----SWNDQLADALkgISRMdslnLILAQGhrenDFTPA 73
Cdd:PRK13222    2 KFMDIRAVAFDLDGTLVDSAPdLAAAVNAALAALglppAGEervrTWVGNGADVL--VERA----LTWAGR----EPDEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  74 QKQALATEKNTNYLQLVNQMTpaNILPGITAFLTELTTAGYALSLAS--ASKNAPLVLRKLGLSDYFTKAVDPASLKHGK 151
Cdd:PRK13222   72 LLEKLRELFDRHYAENVAGGS--RLYPGVKETLAALKAAGYPLAVVTnkPTPFVAPLLEALGIADYFSVVIGGDSLPNKK 149

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2787884964 152 PDPEIFRRGAEILGLNPADCIGVEDAAAGVQSIKGAG 188
Cdd:PRK13222  150 PDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAG 186
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 3-194 2.89e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 49.45  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   3 KFAAIKGFVFDLDGVITDTSTFHSQAWHQIADKVGVSWNDQLADALKGISRMDSLNLILAQGHRENDFTPAQKqaLATEK 82
Cdd:PLN02770   18 GLAPLEAVLFDVDGTLCDSDPLHYYAFREMLQEINFNGGVPITEEFFVENIAGKHNEDIALGLFPDDLERGLK--FTDDK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  83 NTNYLQLV-NQMTPANILPGITAFLTELTTAGYALSLASaSKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGA 161
Cdd:PLN02770   96 EALFRKLAsEQLKPLNGLYKLKKWIEDRGLKRAAVTNAP-RENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKAL 174

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2787884964 162 EILGLNPADCIGVEDAAAGVQSIKGAGETAIGI 194
Cdd:PLN02770  175 EVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGL 207
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 11-195 6.04e-07

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: 48.16  E-value: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  11 VFDLDGVITDTStfhsqawHQIADKVGVSWND----QLADAlkGISRMDSLNLILAQGHRENDFTPAQKQALATEKNTNY 86
Cdd:cd07533     3 IFDWDGTLADSQ-------HNIVAAMTAAFADlglpVPSAA--EVRSIIGLSLDEAIARLLPMATPALVAVAERYKEAFD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  87 LQLVNQMTPANILPGITAFLTELTTAGYALSLASASKNAPL--VLRKLGLSDYF--TKAVDPASlkhGKPDPEIFRRGAE 162
Cdd:cd07533    74 ILRLLPEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLdrVLEQHGLGGYFdaTRTADDTP---SKPHPEMLREILA 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2787884964 163 ILGLNPADCIGVEDAAAGVQSIKGAGETAIGIG 195
Cdd:cd07533   151 ELGVDPSRAVMVGDTAYDMQMAANAGAHAVGVA 183
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 7-188 1.24e-06

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 47.38  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   7 IKGFVFDLDGVITDTSTFHSQAWHQIADKVGVSWN-DQLADALKGISrmdsLNLILAQGHRENDFTPAQKQAlatEKNtn 85
Cdd:PRK10563    4 IEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSlEEVFKRFKGVK----LYEIIDIISKEHGVTLAKAEL---EPV-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  86 YLQLVNQMTPANI--LPGITAFLTELTTAGYALSLASASKnAPLVLRKLGLSDYFT-KAVDPASLKHGKPDPEIFRRGAE 162
Cdd:PRK10563   75 YRAEVARLFDSELepIAGANALLESITVPMCVVSNGPVSK-MQHSLGKTGMLHYFPdKLFSGYDIQRWKPDPALMFHAAE 153

                         170       180
                  ....*....|....*....|....*.
gi 2787884964 163 ILGLNPADCIGVEDAAAGVQSIKGAG 188
Cdd:PRK10563  154 AMNVNVENCILVDDSSAGAQSGIAAG 179
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 98-187 2.36e-06

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 44.84  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  98 ILPGITAFLTELTtAGYALSLASaskNAPLV-----LRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNPADCI 172
Cdd:cd04305    10 LLPGAKELLEELK-KGYKLGIIT---NGPTEvqwekLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETL 85

                          90
                  ....*....|....*
gi 2787884964 173 GVEDAAAgvQSIKGA 187
Cdd:cd04305    86 MVGDSLE--SDILGA 98
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 9-172 3.84e-06

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 46.78  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964   9 GFVFDLDGVIT-DTSTFHSQAWHQIADKVGVSwnDQLADALKGISRMDSLNLILAQGHRENDftPAQKQALATEKNTNYL 87
Cdd:PLN02575  133 GAIFEWEGVIIeDNPDLENQAWLTLAQEEGKS--PPPAFILRRVEGMKNEQAISEVLCWSRD--PAELRRMATRKEEIYQ 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  88 QLVNQMTpaNILPGITAFLTELttAGYALSLASASKNAPLVLRK----LGLSDYFTKAVDPASLKHGKPDPEIFRRGAEI 163
Cdd:PLN02575  209 ALQGGIY--RLRTGSQEFVNVL--MNYKIPMALVSTRPRKTLENaigsIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQL 284


                  ....*....
gi 2787884964 164 LGLNPADCI 172
Cdd:PLN02575  285 LNFIPERCI 293
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 102-194 4.39e-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: 43.92  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964 102 ITAFLTELTTAGYALSLASASKNAPL--VLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNPADCIGVEDAAA 179
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALraLLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                          90
                  ....*....|....*
gi 2787884964 180 GVQSIKGAGETAIGI 194
Cdd:cd01427    92 DIEAARAAGGRTVAV 106
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 11-209 7.00e-06

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: 45.04  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  11 VFDLDGVITDTSTFHSQAWHQIADKVG-VSWNDQLADALKGISRMDSLnlilaqghRENDFTPAQKQALATEKntnYLQL 89
Cdd:cd04303     3 IFDFDGTLADSFPWFLSILNQLAARHGfKTVDEEEIEQLRQLSSREIL--------KQLGVPLWKLPLIAKDF---RRLM 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  90 VNQMTPANILPGITAFLTELTTAGYALSLASAS--KNAPLVLRKLGLSDYFTkAVDPASLkHGKpdPEIFRRGAEILGLN 167
Cdd:cd04303    72 AEAAPELALFPGVEDMLRALHARGVRLAVVSSNseENIRRVLGPEELISLFA-VIEGSSL-FGK--AKKIRRVLRRTKIT 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2787884964 168 PADCIGVEDAAAGVQSIKGAGETAIGIG----DPTVLAAA--DINFTD 209
Cdd:cd04303   148 AAQVIYVGDETRDIEAARKVGLAFAAVSwgyaKPEVLKALapDHMLED 195
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 11-188 8.36e-06

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: 45.00  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  11 VFDLDGVITDTStfhsqawhqiADKVGVSwNDQLADALKGISRMDSLNLILAQGHR---ENDFTPAQKQALATEKNTNYL 87
Cdd:cd07512     3 IFDLDGTLIDSA----------PDLHAAL-NAVLAAEGLAPLSLAEVRSFVGHGAPaliRRAFAAAGEDLDGPLHDALLA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964  88 QLVNQMTPA-----NILPGITAFLTELTTAGYALSLAS--ASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRG 160
Cdd:cd07512    72 RFLDHYEADppgltRPYPGVIEALERLRAAGWRLAICTnkPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAA 151

                         170       180
                  ....*....|....*....|....*...
gi 2787884964 161 AEILGLNPADCIGVEDAAAGVQSIKGAG 188
Cdd:cd07512   152 IRRLGGDVSRALMVGDSETDAATARAAG 179
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 106-171 1.21e-05

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 44.57  E-value: 1.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2787884964 106 LTELTTAGYALSLASASKNAPL--VLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNPADC 171
Cdd:cd02588   100 LRRLREAGYRLAILSNGSPDLIedVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEI 167
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 100-184 6.18e-05

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: 42.58  E-value: 6.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964 100 PGITAFLTELTTAGYALSLASaSKNAPL---VLRKLGLSDYFTkAVDPASLKHGKPD-PEIFRRGAEILGLNPADCIGVE 175
Cdd:cd04302    84 PGIPELLEKLKAAGYRLYVAT-SKPEVFarrILEHFGLDEYFD-GIAGASLDGSRVHkADVIRYALDTLGIAPEQAVMIG 161

                          90
                  ....*....|....*..
gi 2787884964 176 D--------AAAGVQSI 184
Cdd:cd04302   162 DrkhdiigaRANGIDSI 178
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 121-192 2.63e-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: 40.31  E-value: 2.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2787884964 121 ASKN-APLVLRKLGLSDYFTKAVD-PASLKHGKPDPEIFRRGAEILGLNPADCIGVEDAAAGVQSIKGAGETAI 192
Cdd:cd02604   105 ASKNhAIRVLKRLGLADLFDGIFDiEYAGPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTV 178
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 106-195 5.80e-04

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 39.63  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787884964 106 LTELTTAGYALSLAS--ASKNAPLVLRKLGLSDYFTKAVDPASLKHGKPDPEIFRRGAEILGLNPADCIGVEDAAAGVQS 183
Cdd:PRK13288   91 LKTLKKQGYKLGIVTtkMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKPEEALMVGDNHHDILA 170

                          90
                  ....*....|..
gi 2787884964 184 IKGAGETAIGIG 195
Cdd:PRK13288  171 GKNAGTKTAGVA 182
 
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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