phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489504783 188 EELAGFADQAKKQNLAADVGatqqvgtQQVDGYI--RVYPQMKDLIGTLQAHGIDTWVVSASPEPIVKVWAGEVGLDdqH 265
Cdd:cd02612   55 EALLGFATAGLAGELAALVE-------EFVEEYIlrVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGID--N 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489504783 266 VVGVRSVADQsGKLTAHLVGcggvrdgddsVMTYLDGKrcwanqvifgvtgPQAFNQLAADRRQVL----AAGDSNSD 339
Cdd:cd02612  126 VLGTQLETED-GRYTGRIIG----------PPCYGEGK-------------VKRLREWLAEEGIDLkdsyAYSDSIND 179

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489504783  152 LDGeTTTGQPAFVgNNVRRLAGPYAWSNALSAGY---TAEELAGFADQAKKQNLAADVGATQQVGTQQV--DGYIRvypq 226
Cdd:TIGR01488   6 FDG-TLTRQDSLI-DLLAKLLGTNDEVIELTRLApsgRISFEDALGRRLALLHRSRSEEVAKEFLARQValRPGAR---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489504783  227 mkDLIGTLQAHGIDTWVVSASPEPIVKVWAGEVGLDDqhVVGVRSVADQSGKLTAHLVGCGGV-RDGDDSVMTYLdgkrc 305
Cdd:TIGR01488  80 --ELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDD--VFANRLEFDDNGLLTGPIEGQVNPeGECKGKVLKEL----- 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 489504783  306 wanqvifgvtgpqaFNQLAADRRQVLAAGDSNSD 339
Cdd:TIGR01488 151 --------------LEESKITLKKIIAVGDSVND 170

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489504783 188 EELAGFADQAKKQNLAADVGatqqvgtQQVDGYI--RVYPQMKDLIGTLQAHGIDTWVVSASPEPIVKVWAGEVGLDdqH 265
Cdd:cd02612   55 EALLGFATAGLAGELAALVE-------EFVEEYIlrVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGID--N 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489504783 266 VVGVRSVADQsGKLTAHLVGcggvrdgddsVMTYLDGKrcwanqvifgvtgPQAFNQLAADRRQVL----AAGDSNSD 339
Cdd:cd02612  126 VLGTQLETED-GRYTGRIIG----------PPCYGEGK-------------VKRLREWLAEEGIDLkdsyAYSDSIND 179

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489504783  152 LDGeTTTGQPAFVgNNVRRLAGPYAWSNALSAGY---TAEELAGFADQAKKQNLAADVGATQQVGTQQV--DGYIRvypq 226
Cdd:TIGR01488   6 FDG-TLTRQDSLI-DLLAKLLGTNDEVIELTRLApsgRISFEDALGRRLALLHRSRSEEVAKEFLARQValRPGAR---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489504783  227 mkDLIGTLQAHGIDTWVVSASPEPIVKVWAGEVGLDDqhVVGVRSVADQSGKLTAHLVGCGGV-RDGDDSVMTYLdgkrc 305
Cdd:TIGR01488  80 --ELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDD--VFANRLEFDDNGLLTGPIEGQVNPeGECKGKVLKEL----- 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 489504783  306 wanqvifgvtgpqaFNQLAADRRQVLAAGDSNSD 339
Cdd:TIGR01488 151 --------------LEESKITLKKIIAVGDSVND 170