Mitochondrial PGP phosphatase; This is a family of proteins that acts as a mitochondrial phosphatase in cardiolipin biosynthesis. Cardiolipin is a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes. The inverted phosphatase motif includes the highly conserved DKD triad.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7630078    151 KDRQFVLPHVSVKDLRYIDWEV--LKRKGFKGVVFDKDNTLTAPYSLAIWPPLRPSIERCKAVFGHD-IAVFSNSAGLTE 227
Cdd:pfam09419  12 KNPSLCLPHLTVPTFNQLPIPIngLKGVGIKAVVLDKDNCFALPHDDKVWPPYKEKWEELRAAYPGKrLLIVSNSAGSND 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7630078    228 yDHDDSKAKALEAEIGIRVLRHRVKKPaGTAEEVEKHFGCTS-----SELIMVGDRPFTDIVYGNRNG-FLTVLTEPLS 300
Cdd:pfam09419  92 -DKDGEQAKALEKSTGIPVLRHPVKKP-GCGEEVLEYFKERGvvtrpSEIAVVGDRLFTDILMANMMGsWGVWLTDGVG 168

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7630078  180 GVVFDKDNTLTAPYSLAIWPPLRPSIERCKAVfGHDIAVFSNsaglteyDHDDSKAKALEAeIGIRVLrHRVKKPAGTA- 258
Cdd:cd16416   1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEA-GIKVVLVSN-------NNERRVAKVIEK-LDLPFV-ARAGKPRPRAf 70

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 7630078  259 EEVEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTVL 295
Cdd:cd16416  71 RRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTIL 107

Mitochondrial PGP phosphatase; This is a family of proteins that acts as a mitochondrial phosphatase in cardiolipin biosynthesis. Cardiolipin is a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes. The inverted phosphatase motif includes the highly conserved DKD triad.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7630078    151 KDRQFVLPHVSVKDLRYIDWEV--LKRKGFKGVVFDKDNTLTAPYSLAIWPPLRPSIERCKAVFGHD-IAVFSNSAGLTE 227
Cdd:pfam09419  12 KNPSLCLPHLTVPTFNQLPIPIngLKGVGIKAVVLDKDNCFALPHDDKVWPPYKEKWEELRAAYPGKrLLIVSNSAGSND 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7630078    228 yDHDDSKAKALEAEIGIRVLRHRVKKPaGTAEEVEKHFGCTS-----SELIMVGDRPFTDIVYGNRNG-FLTVLTEPLS 300
Cdd:pfam09419  92 -DKDGEQAKALEKSTGIPVLRHPVKKP-GCGEEVLEYFKERGvvtrpSEIAVVGDRLFTDILMANMMGsWGVWLTDGVG 168

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7630078  157 LPHVSVKDLRYIDWEVLKRKGFKGVVFDKDNTLTAPYSLAIWPPLRPSIERCKAVfGHDIAVFSNSAglteydhdDSKAK 236
Cdd:COG2179   5 KPDEYVKSIYDIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEA-GFKVCIVSNNS--------EKRVK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7630078  237 ALEAEIGIRVLrHRVKKPAGTA-EEVEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTVLTEPLSRAEEPFIvRQVRRLE 315
Cdd:COG2179  76 RFAEKLGIPYI-ARAKKPLPRGfRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKEFWFT-RINRFLE 153

                       170
                ....*....|.
gi 7630078  316 LALLKRWLRKG 326
Cdd:COG2179 154 RRILKRLKKKG 164

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7630078  235 AKALEAEIGIRVLRhrVKKPAGTA-EEVEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTVL 295
Cdd:COG0647 170 AAALEAATGGEPLV--VGKPSPPIyELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLL 229

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and 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
                ....*....|....*....|....*....|....*
gi 7630078  261 VEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTVL 295
Cdd:cd16422 186 VLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSIL 220

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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
                ....*....|....*....|....*....|....*...
gi 7630078  259 EEVEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTVLT 296
Cdd:cd07530 184 RAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLV 221

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7630078  181 VVFDKDNTLtapyslaiWPPLRPSIERCKAvfGHDIAVFSNsaGLTEydHDDSKAKALEA-----------EIGirvlrh 249
Cdd:cd04305   2 IIFDLDDTL--------LPGAKELLEELKK--GYKLGIITN--GPTE--VQWEKLEQLGIhkyfdhiviseEVG------ 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 7630078  250 rVKKPAGTA-EEVEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTV 294
Cdd:cd04305  62 -VQKPNPEIfDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106

phosphoglycolate/pyridoxal phosphate phosphatase family; 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 mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 7630078    251 VKKPAGTA-EEVEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTVLT 296
Cdd:TIGR01452 200 VGKPSPYMfNCITEKFSIDPARTLMVGDRLETDILFGHRCGMTTVLV 246