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Conserved domains on  [gi|1593647813|gb|TDG95254|]
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hypothetical protein C5L28_001428 [Lentilactobacillus parakefiri]

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 6.65e-89

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: 259.93  E-value: 6.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNlqDKYTDDQKVDLATEKNTNYLK 88
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGG--KKYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 LVDQMTPDNILPGIKAFLDEIKNGGYLLSLASASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKP 168
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 1593647813 169 EQCIGVEDAAAGVESINAAGETSIGIG 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 6.65e-89

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: 259.93  E-value: 6.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNlqDKYTDDQKVDLATEKNTNYLK 88
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGG--KKYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 LVDQMTPDNILPGIKAFLDEIKNGGYLLSLASASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKP 168
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 1593647813 169 EQCIGVEDAAAGVESINAAGETSIGIG 195
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 9-221 2.79e-67

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: 204.45  E-value: 2.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVgapwskeledglkgisrmdslemilkagnlqdkytddqkvDLATEKNTNYLK 88
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAWKKLADKE----------------------------------------ELAARKNRIYVE 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 LVDQMTPDNILPGIKAFLDEIKNGGYLLSLASASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKP 168
Cdd:cd02598    41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1593647813 169 EQCIGVEDAAAGVESINAAGETSIGIGDQTILKAADIHFADT-SEMTLANIEKQ 221
Cdd:cd02598   121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGADIVVPDTtADLTIEELLEV 174
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-212 1.77e-61

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 191.19  E-value: 1.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNLQdkYTDDqkvDLATEKNTNY 86
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLD--LPEE---ELAARKEELY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  87 LKLVDqMTPDNILPGIKAFLDEIKNGGYLLSLASASK--NAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELI 164
Cdd:COG0637    77 RELLA-EEGLPLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1593647813 165 DLKPEQCIGVEDAAAGVESINAAGETSIGIGD----QTILKAADIHFADTSE 212
Cdd:COG0637   156 GVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDggtaEEELAGADLVVDDLAE 207
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-188 4.53e-22

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: 89.18  E-value: 4.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSIFHSQAWHQVAD-----KVGAPWSKELEDGLKGI---SRMDSLEMILKAGNLQDKYTDDQKVDL 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASehplaKAIVAAAEDLPIPVEDFtarLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  79 aTEKNTNYLKLVDQMTPDNILPGIKAFLDEIKNGGYLLSLASAS--KNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEI 156
Cdd:pfam00702  81 -TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDnpEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1593647813 157 YLKGAELIDLKPEQCIGVEDAAAGVESINAAG 188
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
9-188 1.05e-18

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 80.12  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNlqdkyTDDQKVDLATEKnTNYLK 88
Cdd:PRK10725    7 GLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQ-----ADLDPHALAREK-TEAVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 --LVDQMTPDNILPGIKAFldeikNGGYLLSLASASKN--APKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELI 164
Cdd:PRK10725   81 smLLDSVEPLPLIEVVKAW-----HGRRPMAVGTGSESaiAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLM 155

                         170       180
                  ....*....|....*....|....
gi 1593647813 165 DLKPEQCIGVEDAAAGVESINAAG 188
Cdd:PRK10725  156 GVQPTQCVVFEDADFGIQAARAAG 179
 
Name Accession Description Interval E-value
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 9-195 6.65e-89

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: 259.93  E-value: 6.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNlqDKYTDDQKVDLATEKNTNYLK 88
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGG--KKYSEEEKEELAERKNDYYVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 LVDQMTPDNILPGIKAFLDEIKNGGYLLSLASASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKP 168
Cdd:TIGR01990  79 LLKELTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSP 158

                         170       180
                  ....*....|....*....|....*..
gi 1593647813 169 EQCIGVEDAAAGVESINAAGETSIGIG 195
Cdd:TIGR01990 159 SECIGIEDAQAGIEAIKAAGMFAVGVG 185
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 9-221 2.79e-67

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: 204.45  E-value: 2.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVgapwskeledglkgisrmdslemilkagnlqdkytddqkvDLATEKNTNYLK 88
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAWKKLADKE----------------------------------------ELAARKNRIYVE 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 LVDQMTPDNILPGIKAFLDEIKNGGYLLSLASASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKP 168
Cdd:cd02598    41 LIEELTPVDVLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1593647813 169 EQCIGVEDAAAGVESINAAGETSIGIGDQTILKAADIHFADT-SEMTLANIEKQ 221
Cdd:cd02598   121 KDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGADIVVPDTtADLTIEELLEV 174
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-194 9.99e-62

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: 191.02  E-value: 9.99e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNlqDKYTDDQKVDLATEKNTNY 86
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRG--DGLSLEEIHQLAERKNELY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  87 LKLVDqMTPDNILPGIKAFLDEIKNGGYLLSLASASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDL 166
Cdd:TIGR02009  79 RELLR-LTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGV 157

                         170       180
                  ....*....|....*....|....*...
gi 1593647813 167 KPEQCIGVEDAAAGVESINAAGETSIGI 194
Cdd:TIGR02009 158 PPNECIVFEDALAGVQAARAAGMFAVAV 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-212 1.77e-61

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 191.19  E-value: 1.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNLQdkYTDDqkvDLATEKNTNY 86
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLD--LPEE---ELAARKEELY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  87 LKLVDqMTPDNILPGIKAFLDEIKNGGYLLSLASASK--NAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELI 164
Cdd:COG0637    77 RELLA-EEGLPLIPGVVELLEALKEAGIKIAVATSSPreNAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1593647813 165 DLKPEQCIGVEDAAAGVESINAAGETSIGIGD----QTILKAADIHFADTSE 212
Cdd:COG0637   156 GVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDggtaEEELAGADLVVDDLAE 207
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 9-196 7.93e-28

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: 102.69  E-value: 7.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWhqvadkvgapwskeledglkgisrmdslemilkagNLQDKYTDDQKVDLATEkntnylk 88
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAW-----------------------------------QLLERKNALLLELIASE------- 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 lvdqmtPDNILPGIKAFLDEIKNGGYLLSLASAS--KNAPKVLQKLNLT-DYFPKIVDPKTLSKGKPDPEIYLKGAELID 165
Cdd:cd07505    39 ------GLKLKPGVVELLDALKAAGIPVAVATSSsrRNVELLLLELGLLrGYFDVIVSGDDVERGKPAPDIYLLAAERLG 112

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1593647813 166 LKPEQCIGVEDAAAGVESINAAGETSIGIGD 196
Cdd:cd07505   113 VDPERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-194 3.02e-25

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: 97.11  E-value: 3.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  10 FVFDLDGVITDTSIFHSQaWHQVADKVGAPwskeLEDGLKGISRMDSLEMILKAGnlqdKYTDDQKVDLAT-EKNTNYLK 88
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAK-LINREELGLVP----DELGVSAVGRLELALRRFKAQ----YGRTISPEDAQLlYKQLFYEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 LVDQMTPDnILPGIKAFLDEIKNGGYLLSLASASKNAPK-VLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLK 167
Cdd:TIGR01509  73 IEEEAKLK-PLPGVRALLEALRARGKKLALLTNSPRAHKlVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLE 151

                         170       180
                  ....*....|....*....|....*..
gi 1593647813 168 PEQCIGVEDAAAGVESINAAGETSIGI 194
Cdd:TIGR01509 152 PSECVFVDDSPAGIEAAKAAGMHTVGV 178
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-212 3.78e-24

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 95.38  E-value: 3.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSIFHSQAWHQVADKVG-APWSKELEDGLKGISRMDSLEMILKAgnlqdkyTDDQKVDLATEK-NT 84
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGlPPLDLEELRALIGLGLRELLRRLLGE-------DPDEELEELLARfRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  85 NYLKLVDQMTPdnILPGIKAFLDEIKNGGYLLSLAS--ASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAE 162
Cdd:COG0546    74 LYEEELLDETR--LFPGVRELLEALKARGIKLAVVTnkPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALE 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1593647813 163 LIDLKPEQCIGVEDAAAGVESINAAGETSI----GIGDQTILKA--ADIHFADTSE 212
Cdd:COG0546   152 RLGLDPEEVLMVGDSPHDIEAARAAGVPFIgvtwGYGSAEELEAagADYVIDSLAE 207
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 10-211 6.92e-24

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: 93.47  E-value: 6.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  10 FVFDLDGVITDTSifhsQAWHQVADKVgapwskeledglkgisrmdslemilkagnlqdkytddqkvdLATEKNTNYLKL 89
Cdd:cd16423     2 VIFDFDGVIVDTE----PLWYEAWQEL-----------------------------------------LNERRNELIKRQ 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  90 VDQMTPDNILPGIKAFLDEIKNGGYLLSLASAS--KNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLK 167
Cdd:cd16423    37 FSEKTDLPPIEGVKELLEFLKEKGIKLAVASSSprRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVN 116

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1593647813 168 PEQCIGVEDAAAGVESINAAGETSIGI-----GDQTILKAADI--HFADTS 211
Cdd:cd16423   117 PEECVVIEDSRNGVLAAKAAGMKCVGVpnpvtGSQDFSKADLVlsSFAEKE 167
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-188 4.53e-22

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: 89.18  E-value: 4.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSIFHSQAWHQVAD-----KVGAPWSKELEDGLKGI---SRMDSLEMILKAGNLQDKYTDDQKVDL 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASehplaKAIVAAAEDLPIPVEDFtarLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  79 aTEKNTNYLKLVDQMTPDNILPGIKAFLDEIKNGGYLLSLASAS--KNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEI 156
Cdd:pfam00702  81 -TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDnpEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1593647813 157 YLKGAELIDLKPEQCIGVEDAAAGVESINAAG 188
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 9-210 1.63e-20

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: 85.47  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVGAPwSKELEDGLKGISRMDSLEMILKAgnlqdkyTDDQKVDLATEKNtnylk 88
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVD-PEEVLKVSHGRRAIDVIRKLAPD-------DADIELVLALETE----- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 LVDQMTPDNI-LPGIKAFLDEIKNGG-----------YLLS--LASASKNAPKVLqklnltdyfpkiVDPKTLSKGKPDP 154
Cdd:cd07527    68 EPESYPEGVIaIPGAVDLLASLPAAGdrwaivtsgtrALAEarLEAAGLPHPEVL------------VTADDVKNGKPDP 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1593647813 155 EIYLKGAELIDLKPEQCIGVEDAAAGVESINAAGETSIGIGDQTILKAADIHFADT 210
Cdd:cd07527   136 EPYLLGAKLLGLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEAAGADL 191
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-194 1.02e-19

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 82.63  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSIFHSQAWHQVADKVGAPwSKELEDGLKGISrmDSLEMILKagNLQDKYTDDQKVDL-----ATEKNTN 85
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEFGYG-ELSEEEILKFIG--LPLREIFR--YLGVSEDEEEKIEFylrkyNEELHDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  86 YLKLvdqmtpdniLPGIKAFLDEIKNGGYLLSLASaSKNAPKV---LQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAE 162
Cdd:pfam13419  77 LVKP---------YPGIKELLEELKEQGYKLGIVT-SKSRENVeefLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALE 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1593647813 163 LIDLKPEQCIGVEDAAAGVESINAAGETSIGI 194
Cdd:pfam13419 147 QLGLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
9-188 1.05e-18

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 80.12  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNlqdkyTDDQKVDLATEKnTNYLK 88
Cdd:PRK10725    7 GLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQ-----ADLDPHALAREK-TEAVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 --LVDQMTPDNILPGIKAFldeikNGGYLLSLASASKN--APKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELI 164
Cdd:PRK10725   81 smLLDSVEPLPLIEVVKAW-----HGRRPMAVGTGSESaiAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLM 155

                         170       180
                  ....*....|....*....|....
gi 1593647813 165 DLKPEQCIGVEDAAAGVESINAAG 188
Cdd:PRK10725  156 GVQPTQCVVFEDADFGIQAARAAG 179
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-218 6.61e-17

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 76.14  E-value: 6.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   1 MAKFSDIKGFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSK--ELED--GLkgisRMDSL-EMILKAGNLQDkyTDDQK 75
Cdd:PRK10826    1 MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRreELPDtlGL----RIDQVvDLWYARQPWNG--PSRQE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  76 VdlATEKNTNYLKLVDQMTPdnILPGIKAFLDEIKNGGYLLSLASASKNA--PKVLQKLNLTDYFPKIVDPKTLSKGKPD 153
Cdd:PRK10826   75 V--VQRIIARVISLIEETRP--LLPGVREALALCKAQGLKIGLASASPLHmlEAVLTMFDLRDYFDALASAEKLPYSKPH 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813 154 PEIYLKGAELIDLKPEQCIGVEDAAAGVESINAAGETSIGI-----GDQTILKAADIHFADTSEMTLANI 218
Cdd:PRK10826  151 PEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVpapeqQNDPRWALADVKLESLTELTAADL 220
PRK11587 PRK11587
putative phosphatase; Provisional
 8-188 1.86e-15

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 72.34  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   8 KGFVFDLDGVITDTSIFHSQAWHQVADKVGAPwSKELEDGLKGISRMDSLEMILkAG----NLQDKYTDDQKVDlATEkn 83
Cdd:PRK11587    4 KGFLFDLDGTLVDSLPAVERAWSNWADRHGIA-PDEVLNFIHGKQAITSLRHFM-AGaseaEIQAEFTRLEQIE-ATD-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  84 tnylklVDQMTPdniLPGIKAFLDE---------IKNGGYLlSLASASKNA-----PKVLqklnltdyfpkiVDPKTLSK 149
Cdd:PRK11587   79 ------TEGITA---LPGAIALLNHlnklgipwaIVTSGSV-PVASARHKAaglpaPEVF------------VTAERVKR 136

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1593647813 150 GKPDPEIYLKGAELIDLKPEQCIGVEDAAAGVESINAAG 188
Cdd:PRK11587  137 GKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAG 175
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-176 6.98e-15

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: 70.83  E-value: 6.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSIFHSQAWHQVADKVGAP-WSKELEDGLKGISRMDSLEMILKAGNLQDKYT---DDQKVDLATEK 82
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLdEAEELAEAYRAIEYALWRRYERGEITFAELLRrllEELGLDLAEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  83 NTNYLKLVDQMTPdnILPGIKAFLDEIKNGGYLLSLAS--ASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKG 160
Cdd:COG1011    81 AEAFLAALPELVE--PYPDALELLEALKARGYRLALLTngSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELA 158

                         170
                  ....*....|....*.
gi 1593647813 161 AELIDLKPEQCIGVED 176
Cdd:COG1011   159 LERLGVPPEEALFVGD 174
PLN02940 PLN02940
riboflavin kinase
 11-194 8.14e-14

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 69.48  E-value: 8.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSIFHSQAWHQVADKVGAPWskeleDGLKGISRMDSLEMILKAGNLQD---KYTDDQKVDLATEKntnyl 87
Cdd:PLN02940   15 ILDLDGTLLNTDGIVSDVLKAFLVKYGKQW-----DGREAQKIVGKTPLEAAATVVEDyglPCSTDEFNSEITPL----- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  88 kLVDQMTPDNILPGIKAFLDEIKNGGYLLSLASASKNA---PKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELI 164
Cdd:PLN02940   85 -LSEQWCNIKALPGANRLIKHLKSHGVPMALASNSPRAnieAKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRL 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1593647813 165 DLKPEQCIGVEDAAAGVESINAAGETSIGI 194
Cdd:PLN02940  164 NVEPSNCLVIEDSLPGVMAGKAAGMEVIAV 193
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 11-192 9.06e-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: 67.40  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSIFHSQAW-HQVADKVGAP--WSKELEDGLK----GISRMDSLEMILKAGNLQDKYTDDQKVDLATEKN 83
Cdd:cd07528     3 IFDVDGTLAETEELHRRAFnNAFFAERGLDwyWDRELYGELLrvggGKERIAAYFEKVGWPESAPKDLKELIADLHKAKT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  84 TNYLKLVDQMTPDnILPGIKAFLDEIKNGGYLLSLASAS--KNAPKVLQKL---NLTDYFPKIVDPKTLSKGKPDPEIYL 158
Cdd:cd07528    83 ERYAELIAAGLLP-LRPGVARLIDEAKAAGVRLAIATTTspANVDALLSALlgpERRAIFDAIAAGDDVAEKKPDPDIYL 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1593647813 159 KGAELIDLKPEQCIGVEDAAAGVESINAAGETSI 192
Cdd:cd07528   162 LALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 11-193 4.22e-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: 61.57  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGIsrmdslemilkagnlqdkytddqkvdlatekntnylklv 90
Cdd:cd07526     4 IFDCDGVLVDSEVIAARVLVEVLAELGARVLAAFEAELQPI--------------------------------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  91 dqmtpdnilPGIKAFLDEIkngGYLLSLASASKNaPKV---LQKLNLTDYF-PKIVDPKTLSKGKPDPEIYLKGAELIDL 166
Cdd:cd07526    45 ---------PGAAAALSAL---TLPFCVASNSSR-ERLthsLGLAGLLAYFeGRIFSASDVGRGKPAPDLFLHAAAQMGV 111

                         170       180
                  ....*....|....*....|....*..
gi 1593647813 167 KPEQCIGVEDAAAGVESINAAGETSIG 193
Cdd:cd07526   112 APERCLVIEDSPTGVRAALAAGMTVFG 138
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 7-195 1.88e-11

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: 61.14  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSifhsqawhqvaDKVGAPWSKELED-GLKGISRMDSLEMIlkAGNLQD---KYTDDQKVDLATEK 82
Cdd:cd02616     1 ITTILFDLDGTLIDTN-----------ELIIKSFNHTLKEyGLEGYTREEVLPFI--GPPLREtfeKIDPDKLEDMVEEF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  83 NTNYLKLVDQMTpdNILPGIKAFLDEIKNGGYLLSLASaSKN---APKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLK 159
Cdd:cd02616    68 RKYYREHNDDLT--KEYPGVYETLARLKSQGIKLGVVT-TKLretALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLK 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1593647813 160 GAELIDLKPEQCIGVEDAAAGVESINAAGETSIGIG 195
Cdd:cd02616   145 ALELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVT 180
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 11-188 2.45e-11

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: 60.44  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNLQDKYTDDqkVDLATEKNTNYLklv 90
Cdd:cd07529     5 IFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEE--FDEQQEALAELF--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  91 dqMTPDNILPGIKAFLDEIKNGGYLLSLASAS---KNAPKVLQKLNLTDYFPKIV---DPKTLSKGKPDPEIYLKGAELI 164
Cdd:cd07529    80 --MGTAKLMPGAERLLRHLHAHNIPIALATSSctrHFKLKTSRHKELFSLFHHVVtgdDPEVKGRGKPAPDIFLVAAKRF 157

                         170       180
                  ....*....|....*....|....*..
gi 1593647813 165 DLK---PEQCIGVEDAAAGVESINAAG 188
Cdd:cd07529   158 NEPpkdPSKCLVFEDSPNGVKAAKAAG 184
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
100-193 3.76e-10

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 57.51  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813 100 PGIKAFLDEIKNGGYLLSLAS--ASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKPEQCIGVEDA 177
Cdd:PRK13222   96 PGVKETLAALKAAGYPLAVVTnkPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDS 175

                          90
                  ....*....|....*.
gi 1593647813 178 AAGVESINAAGETSIG 193
Cdd:PRK13222  176 RNDIQAARAAGCPSVG 191
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 11-194 4.92e-10

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


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 57.14  E-value: 4.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSI-FHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNLQdkyTDDQKV-DLATEKNTNYLK 88
Cdd:TIGR01449   2 LFDLDGTLVDSAPdIAAAVNMALAALGLPPATLARVIGFIGNGVPVLMERVLAWAGQE---PDAQRVaELRKLFDRHYEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 LVDQMTpdNILPGIKAFLDEIKNGGYLLSLASaskNAPK-----VLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAEL 163
Cdd:TIGR01449  79 VAGELT--SVFPGVEATLGALRAKGLRLGLVT---NKPTplarpLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAER 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1593647813 164 IDLKPEQCIGVEDAAAGVESINAAGETSIGI 194
Cdd:TIGR01449 154 LGVAPQQMVYVGDSRVDIQAARAAGCPSVLL 184
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 11-192 2.01e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 56.26  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSI-FHSQAWHQVADKVGAP---WSKELEDGLKGIS----RM-----------DSLEMILKAGNLQDKYT 71
Cdd:PLN02779   44 LFDCDGVLVETERdGHRVAFNDAFKEFGLRpveWDVELYDELLNIGggkeRMtwyfnengwptSTIEKAPKDEEERKELV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  72 D---DQKVDLatekntnYLKLVDQMTPDnILPGIKAFLDEIKNGGYLLSLASAS--KNAPKVLQKLNLTDYFPKI----- 141
Cdd:PLN02779  124 DslhDRKTEL-------FKELIESGALP-LRPGVLRLMDEALAAGIKVAVCSTSneKAVSKIVNTLLGPERAQGLdvfag 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1593647813 142 --VDPKtlskgKPDPEIYLKGAELIDLKPEQCIGVEDAAAGVESINAAGETSI 192
Cdd:PLN02779  196 ddVPKK-----KPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCI 243
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 100-194 8.62e-09

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: 53.78  E-value: 8.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813 100 PGIKAFLDEIKNGGYLLSLAS--ASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKPEQCIGVEDA 177
Cdd:cd16417    90 PGVKEGLAALKAQGYPLACVTnkPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLGIAPAQMLMVGDS 169

                          90
                  ....*....|....*..
gi 1593647813 178 AAGVESINAAGETSIGI 194
Cdd:cd16417   170 RNDILAARAAGCPSVGL 186
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 9-219 2.98e-08

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 52.73  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVIT-DTSIFHSQAWHQVADKVG-APWSKELEDGLKGISRMDSL-EMILKAGNLQdkytddQKVDLATEKNTN 85
Cdd:PLN03243   26 GVVLEWEGVIVeDDSELERKAWRALAEEEGkRPPPAFLLKRAEGMKNEQAIsEVLCWSRDFL------QMKRLAIRKEDL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  86 YLKLvdQMTPDNILPGIKAFLDEIKNggYLLSLASASKNAPKVLQK----LNLTDYFPKIVDPKTLSKGKPDPEIYLKGA 161
Cdd:PLN03243  100 YEYM--QGGLYRLRPGSREFVQALKK--HEIPIAVASTRPRRYLERaieaVGMEGFFSVVLAAEDVYRGKPDPEMFMYAA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1593647813 162 ELIDLKPEQCIGVEDAAAGVESINAAGETSIGI-GDQTI--LKAADIHFADTSEMTLANIE 219
Cdd:PLN03243  176 ERLGFIPERCIVFGNSNSSVEAAHDGCMKCVAVaGKHPVyeLSAGDLVVRRLDDLSVVDLK 236
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 1-194 6.54e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 51.38  E-value: 6.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   1 MAKFSDIKGFVFDLDGVITDTSIFHSQAWHQVADKV----GAPWSKEL-EDGLKGiSRMDSLEMILKAGNLQD--KYTDD 73
Cdd:PLN02770   16 LSGLAPLEAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEEFfVENIAG-KHNEDIALGLFPDDLERglKFTDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  74 qkvdlateKNTNYLKLV-DQMTPDNILPGIKAFLDEikNGGYLLSLASASK-NAPKVLQKLNLTDYFPKIVDPKTLSKGK 151
Cdd:PLN02770   95 --------KEALFRKLAsEQLKPLNGLYKLKKWIED--RGLKRAAVTNAPReNAELMISLLGLSDFFQAVIIGSECEHAK 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1593647813 152 PDPEIYLKGAELIDLKPEQCIGVEDAAAGVESINAAGETSIGI 194
Cdd:PLN02770  165 PHPDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGL 207
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 100-203 8.47e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 52.16  E-value: 8.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  100 PGIKAFLDEIKNGGYLLSLASAsknAPKVLQKLNLT------DYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKPEQCIG 173
Cdd:PLN02919   164 PGALELITQCKNKGLKVAVASS---ADRIKVDANLAaaglplSMFDAIVSADAFENLKPAPDIFLAAAKILGVPTSECVV 240

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1593647813  174 VEDAAAGVESINAAGETSIGIG---DQTILKAA 203
Cdd:PLN02919   241 IEDALAGVQAARAAGMRCIAVTttlSEEILKDA 273
PLN02811 PLN02811
hydrolase
 14-188 1.40e-07

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 50.14  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  14 LDGVITDTSIFHSQAWHQVADKVGAPWSKELEDGLKGISRMDSLEMILKAGNLQDKYTDDqkvDLATEKNTnylkLVDQM 93
Cdd:PLN02811    1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPE---DFLVEREA----MLQDL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  94 TPDN-ILPGIKAFLDEIKNGGYLLSLASASKNAPKVLQKLNLTDYFP---KIV--DPKTLSKGKPDPEIYLKGA---ELI 164
Cdd:PLN02811   74 FPTSdLMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSlmhHVVtgDDPEVKQGKPAPDIFLAAArrfEDG 153

                         170       180
                  ....*....|....*....|....
gi 1593647813 165 DLKPEQCIGVEDAAAGVESINAAG 188
Cdd:PLN02811  154 PVDPGKVLVFEDAPSGVEAAKNAG 177
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 7-192 1.71e-07

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: 49.65  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDTSIFHS-QAWHQ-VADKVGAPWSKELEDGL-----KGisRMDSLEMILKAGnlqdKYTDDQKVDLA 79
Cdd:cd02603     1 IRAVLFDFGGVLIDPDPAAAvARFEAlTGEPSEFVLDTEGLAGAfleleRG--RITEEEFWEELR----EELGRPLSAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  80 TEKntnylkLVDQMTPdnILPGIKAFLDEIKNGGYLLSLASaskNAPKVLQKLNLT--DYFPKIVDPKTLS----KGKPD 153
Cdd:cd02603    75 FEE------LVLAAVD--PNPEMLDLLEALRAKGYKVYLLS---NTWPDHFKFQLEllPRRGDLFDGVVEScrlgVRKPD 143

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1593647813 154 PEIYLKGAELIDLKPEQCIGVEDAAAGVESINAAGETSI 192
Cdd:cd02603   144 PEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAI 182
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 5-188 2.07e-07

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 49.69  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   5 SDIKGFVFDLDGVITDTSIFHSQAWHQVADKVGAPWSkeLEDGLKGISRMDSLEMIlkagnlqDKYTDDQKVDLATEK-- 82
Cdd:PRK10563    2 SQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLS--LEEVFKRFKGVKLYEII-------DIISKEHGVTLAKAEle 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  83 ---NTNYLKLVD-QMTPdniLPGIKAFLDEIKNGGYLLSLASASKnAPKVLQKLNLTDYFP-KIVDPKTLSKGKPDPEIY 157
Cdd:PRK10563   73 pvyRAEVARLFDsELEP---IAGANALLESITVPMCVVSNGPVSK-MQHSLGKTGMLHYFPdKLFSGYDIQRWKPDPALM 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1593647813 158 LKGAELIDLKPEQCIGVEDAAAGVESINAAG 188
Cdd:PRK10563  149 FHAAEAMNVNVENCILVDDSSAGAQSGIAAG 179
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 96-176 4.40e-07

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: 46.77  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  96 DNILPGIKAFLDEIKnGGYLLSLASaskNAPKVLQK-----LNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKPEQ 170
Cdd:cd04305     8 DTLLPGAKELLEELK-KGYKLGIIT---NGPTEVQWekleqLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEE 83


                  ....*.
gi 1593647813 171 CIGVED 176
Cdd:cd04305    84 TLMVGD 89
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 102-194 4.69e-07

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: 46.62  E-value: 4.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813 102 IKAFLDEIKNGGYLLSLASASKNAP--KVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKPEQCIGVEDAAA 179
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREAlrALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                          90
                  ....*....|....*
gi 1593647813 180 GVESINAAGETSIGI 194
Cdd:cd01427    92 DIEAARAAGGRTVAV 106
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 101-219 1.57e-06

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 47.94  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813 101 GIKAFLDEIKNggYLLSLASASKNAPKVLQK----LNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKPEQCIGVED 176
Cdd:PLN02575  220 GSQEFVNVLMN--YKIPMALVSTRPRKTLENaigsIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGN 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1593647813 177 AAAGVESINAAGETSIGIGDQTI---LKAADIHFADTSEMT------LANIE 219
Cdd:PLN02575  298 SNQTVEAAHDARMKCVAVASKHPiyeLGAADLVVRRLDELSivdlknLADIE 349
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 103-176 9.73e-06

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: 43.43  E-value: 9.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1593647813 103 KAFLDEIKNGGYLLSLASaskNA----PKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAELIDLKPEQCIGVED 176
Cdd:cd16415    13 VETLKDLKEKGLKLAVVS---NFdrrlRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGD 87
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 7-195 1.29e-05

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 44.64  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   7 IKGFVFDLDGVITDT------SIFHSQAWHqvadkvgAPWSKELEDGLK--GISRMDSLEMIlkagnlqdkytDDQKVDl 78
Cdd:PRK13288    3 INTVLFDLDGTLINTneliisSFLHTLKTY-------YPNQYKREDVLPfiGPSLHDTFSKI-----------DESKVE- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  79 atEKNTNYLKLVDQMTPDNIL--PGIKAFLDEIKNGGYLLSLAS--ASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDP 154
Cdd:PRK13288   64 --EMITTYREFNHEHHDELVTeyETVYETLKTLKKQGYKLGIVTtkMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDP 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1593647813 155 EIYLKGAELIDLKPEQCIGVEDAAAGVESINAAGETSIGIG 195
Cdd:PRK13288  142 EPVLKALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVA 182
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 11-188 1.57e-04

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 41.15  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSI-FHSQAWHQVADKVGAPWSkelEDGLKGISRMDSLEMILKAGNLQDKYTDDQKVDLAtekntnYLKL 89
Cdd:cd07512     3 IFDLDGTLIDSAPdLHAALNAVLAAEGLAPLS---LAEVRSFVGHGAPALIRRAFAAAGEDLDGPLHDAL------LARF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  90 VDQMTPD-----NILPGIKAFLDEIKNGGYLLSLAS--ASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAE 162
Cdd:cd07512    74 LDHYEADppgltRPYPGVIEALERLRAAGWRLAICTnkPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIR 153

                         170       180
                  ....*....|....*....|....*.
gi 1593647813 163 LIDLKPEQCIGVEDAAAGVESINAAG 188
Cdd:cd07512   154 RLGGDVSRALMVGDSETDAATARAAG 179
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 91-188 3.46e-04

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 39.92  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  91 DQMTPDNILpgiKAFLDEIKngGYLLSLASASKN-APKVLQKLNLTDYFPKIVDPKTLS-KGKPDPEIYLKGAELIDLKP 168
Cdd:cd02604    80 DHLKPDPKL---RNLLLALP--GRKIIFTNASKNhAIRVLKRLGLADLFDGIFDIEYAGpDPKPHPAAFEKAIREAGLDP 154

                          90       100
                  ....*....|....*....|
gi 1593647813 169 EQCIGVEDAAAGVESINAAG 188
Cdd:cd02604   155 KRAAFFDDSIRNLLAAKALG 174
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 9-169 3.61e-04

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: 39.69  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813   9 GFVFDLDGVITDTSIFHSQAWHQVADKVGapWSKELEDGLKGISRMDSLEMILKAGNLQDKYTDDQKVDLATEKNTnylk 88
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFG--LDPASFKALKQAGGLAEEEWYRIATSALEELQGRFWSEYDAEEAY---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  89 lvdqmtpdniLPGIKAFLDEIKNGGYLLSLASA--SKNAPKVLQKLNLTDYFpKIVDPKTLSKGKPDPEIYLKGAELIDL 166
Cdd:TIGR01549  75 ----------IRGAADLLARLKSAGIKLGIISNgsLRAQKLLLRLFGLGDYF-ELILVSDEPGSKPEPEIFLAALESLGV 143


                  ...
gi 1593647813 167 KPE 169
Cdd:TIGR01549 144 PPE 146
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 86-192 1.41e-03

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


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 38.13  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  86 YLKLVDQMTPDNIL-PGIKAFLDEIKN-GGYLLSLASASKNAPKVLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKGAEL 163
Cdd:cd07523    63 YKELEAEYLAKPILfPGAKAVLRWIKEqGGKNFLMTHRDHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNK 142

                          90       100
                  ....*....|....*....|....*....
gi 1593647813 164 IDLKPEQCIGVEDAAAGVESINAAGETSI 192
Cdd:cd07523   143 YQLNPEETVMIGDRELDIEAGHNAGISTI 171
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 11-194 2.43e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 37.92  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  11 VFDLDGVITDTSIFHSQAWHQVADKVGAPWSkeledGLKGISRM--DSLEMILK---AGNLQDKYTDDQKVDLATEKNTN 85
Cdd:PRK13223   17 MFDLDGTLVDSVPDLAAAVDRMLLELGRPPA-----GLEAVRHWvgNGAPVLVRralAGSIDHDGVDDELAEQALALFME 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593647813  86 YLKLVDQMTPdnILPGIKAFLDEIKNGGYLLSLASaskNAPK-----VLQKLNLTDYFPKIVDPKTLSKGKPDPEIYLKG 160
Cdd:PRK13223   92 AYADSHELTV--VYPGVRDTLKWLKKQGVEMALIT---NKPErfvapLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFV 166

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1593647813 161 AELIDLKPEQCIGVEDAAAGVESINAAGETSIGI 194
Cdd:PRK13223  167 MKMAGVPPSQSLFVGDSRSDVLAAKAAGVQCVAL 200
 
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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