3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723   5 LMQRGKAIKLAVFDVDGVLTDGRLYFLEDGSEFKTFNTLDGQGIKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLFQG 84
Cdd:COG1778    1 LLERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  85 REDKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVTQARGGEGAAREFCELIMQAQG 164
Cdd:COG1778   81 VKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQG 160

                        170
                 ....*....|
gi 746575723 165 TLDAANANYL 174
Cdd:COG1778  161 KWDALLAAYL 170

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723   5 LMQRGKAIKLAVFDVDGVLTDGRLYFLEDGSEFKTFNTLDGQGIKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLFQG 84
Cdd:COG1778    1 LLERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  85 REDKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVTQARGGEGAAREFCELIMQAQG 164
Cdd:COG1778   81 VKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQG 160

                        170
                 ....*....|
gi 746575723 165 TLDAANANYL 174
Cdd:COG1778  161 KWDALLAAYL 170

3-deoxy-manno-octulosonate-8-phosphatase KdsC;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723   2 TQNLMQRGKAIKLAVFDVDGVLTDGRLYFLEDGSEFKTFNTLDGQGIKMLMASGVTTAIISGRKTPVVERRAKNLGIPHL 81
Cdd:PRK09484  11 SDDVMAKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVEDRMTTLGITHL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  82 FQGREDKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVTQARGGEGAAREFCELIMQ 161
Cdd:PRK09484  91 YQGQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLLL 170

                 ....*...
gi 746575723 162 AQGTLDAA 169
Cdd:PRK09484 171 AQGKLDEA 178

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 746575723   87 DKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVT 143
Cdd:pfam08282 187 SKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVT 243

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723   5 LMQRGKAIKLAVFDVDGVLTDGRLYFLEDGSEFKTFNTLDGQGIKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLFQG 84
Cdd:COG1778    1 LLERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPAVRRRAEELGITHVYQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  85 REDKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVTQARGGEGAAREFCELIMQAQG 164
Cdd:COG1778   81 VKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELILKAQG 160

                        170
                 ....*....|
gi 746575723 165 TLDAANANYL 174
Cdd:COG1778  161 KWDALLAAYL 170

3-deoxy-manno-octulosonate-8-phosphatase KdsC;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723   2 TQNLMQRGKAIKLAVFDVDGVLTDGRLYFLEDGSEFKTFNTLDGQGIKMLMASGVTTAIISGRKTPVVERRAKNLGIPHL 81
Cdd:PRK09484  11 SDDVMAKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRKSKLVEDRMTTLGITHL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  82 FQGREDKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVTQARGGEGAAREFCELIMQ 161
Cdd:PRK09484  91 YQGQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLLL 170

                 ....*...
gi 746575723 162 AQGTLDAA 169
Cdd:PRK09484 171 AQGKLDEA 178

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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 746575723  14 LAVFDVDGVLTDGRLYFLEDGSEFktfntldgqgIKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLF---QGREDKLV 90
Cdd:cd07514    1 LIAVDIDGTLTDRRRSIDLRAIEA----------IRKLEKAGIPVVLVTGNSLPVARALAKYLGLSGPVvaeNGGVDKGT 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746575723  91 VLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVTQARGGEGAA 152
Cdd:cd07514   71 GLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVL 132

phosphoglycolate phosphatase; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746575723  80 HLFQGREDKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVTQARGGEGAA 152
Cdd:PRK01158 150 HIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVA 222

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  11 AIKLAVFDVDGVLTDGRLYFLEdgsefKTFNTldgqgIKMLMASGVTTAIISGRKTPVVERRAKNLGIP----------- 79
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISP-----RTKEA-----LRRLREKGIKVVIATGRPLRSALPLLEELGLDdplitsngali 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  80 HLFQGRE-------------------------------------------DKLVVLDGLLAELGLSYEQVAYLGDDLPDL 116
Cdd:COG0561   71 YDPDGEVlyerpldpedvreilellrehglhlqvvvrsgpgfleilpkgvSKGSALKKLAERLGIPPEEVIAFGDSGNDL 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 746575723 117 PVIRKVGLGIAVANAAPFVRQHADGVTQARGGEGAAR 153
Cdd:COG0561  151 EMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAE 187

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 746575723  87 DKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVTQ 144
Cdd:cd07516  183 SKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAADYVTL 240

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723   48 IKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLFQGR----EDKLV---------------VLDGLLAELGLSYEQVAY 108
Cdd:TIGR00338  94 VKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRleveDGKLTglvegpivdasykgkTLLILLRKEGISPENTVA 173

                          90       100       110
                  ....*....|....*....|....*....|....
gi 746575723  109 LGDDLPDLPVIRKVGLGIAVaNAAPFVRQHADGV 142
Cdd:TIGR00338 174 VGDGANDLSMIKAAGLGIAF-NAKPKLQQKADIC 206

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 746575723   87 DKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGLGIAVANAAPFVRQHADGVT 143
Cdd:TIGR00099 188 SKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYVT 244

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 746575723   14 LAVFDVDGVLTD---------------------------GRLYF----------------LEDGSEFKTFNTLDGQGIKM 50
Cdd:TIGR01488   1 LAIFDFDGTLTRqdslidllakllgtndevieltrlapsGRISFedalgrrlallhrsrsEEVAKEFLARQVALRPGARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723   51 LM----ASGVTTAIISGRKTPVVERRAKNLGIPHLF---------------------QGREDKLVVLDGLLAELGLSYEQ 105
Cdd:TIGR01488  81 LIswlkERGIDTVIVSGGFDFFVEPVAEKLGIDDVFanrlefddnglltgpiegqvnPEGECKGKVLKELLEESKITLKK 160

                         170
                  ....*....|....*..
gi 746575723  106 VAYLGDDLPDLPVIRKV 122
Cdd:TIGR01488 161 IIAVGDSVNDLPMLKLA 177

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  14 LAVFDVDGVLTDGRLyfledgsefktfntldgqgIKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLFQG--------- 84
Cdd:cd01427    1 AVLFDLDGTLLAVEL-------------------LKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGiigsdgggt 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 746575723  85 REDKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVG-LGIAV 128
Cdd:cd01427   62 PKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGgRTVAV 106

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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 746575723  48 IKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLFQ-------------------GREDKLVVLDGLLAELGLSYEQVAY 108
Cdd:cd07500   79 IQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFAneleikdgkltgkvlgpivDAQRKAETLQELAARLGIPLEQTVA 158

                         90
                 ....*....|....*....
gi 746575723 109 LGDDLPDLPVIRKVGLGIA 127
Cdd:cd07500  159 VGDGANDLPMLKAAGLGIA 177

ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723   48 IKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLFQGR-EDKLVVLDGLLAElglsYEQVAYLGDDLPDLPVIRKVGLGI 126
Cdd:TIGR01494 396 IEALRKAGIKVVMLTGDNVLTAKAIAKELGIDVFARVKpEEKAAIVEALQEK----GRTVAMTGDGVNDAPALKKADVGI 471

                  ....*.
gi 746575723  127 AVANAA 132
Cdd:TIGR01494 472 AMGSGD 477

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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 746575723  12 IKLAVFDVDG------VLTDGRLYF----LEDGSEFKTF----NTLDGQGIKMLMASgvttaiisgrKTPVVER---RAK 74
Cdd:cd07501    1 PKCLVFDLDYtlwpgvVDEHGIPPFkdrgGKEVSLYPDAqeilKELKERGILLAVAS----------RNNEFDHaneVLE 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 746575723  75 NLGIPHLFQGRE----DKLVVLDGLLAELGLSYEQVAYLGDDLPDLPVIRKVGL 124
Cdd:cd07501   71 KLDLKELFDAFEiypgSKSSHFRKIAKELGIGFDSMVFFDDEPRNREEVSEGGV 124

Rhizobium meliloti FixI and related proteins; belongs to P-type heavy metal-transporting ATPase subfamily; FixI may be a pump of a specific cation involved in symbiotic nitrogen fixation. The Rhizobium fixI gene is part of an operon conserved among rhizobia, fixGHIS. FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalyzed by FixG, an iron-sulfur protein. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  48 IKMLMASGVTTAIISGRKTPVVERRAKNLGIPHLFQG--REDKLVVLDGLLAElglsYEQVAYLGDDLPDLPVIRKVGLG 125
Cdd:cd02092  443 ISALRALGLSVEILSGDREPAVRALARALGIEDWRAGltPAEKVARIEELKAQ----GRRVLMVGDGLNDAPALAAAHVS 518

                         90
                 ....*....|....*..
gi 746575723 126 IAVANAAPFVRQHADGV 142
Cdd:cd02092  519 MAPASAVDASRSAADIV 535

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746575723  22 VLTDGRLYFLEDGSEFKTFNTLDgqgiKMLM---ASGVTTAIISGRKTPVVERRAKNLGIPHLFQGRED-----KLVVLD 93
Cdd:cd04303   63 IAKDFRRLMAEAAPELALFPGVE----DMLRalhARGVRLAVVSSNSEENIRRVLGPEELISLFAVIEGsslfgKAKKIR 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 746575723  94 GLLAELGLSYEQVAYLGDDLPDLPVIRKVGLG-IAVA---NAAPFVRQHA 139
Cdd:cd04303  139 RVLRRTKITAAQVIYVGDETRDIEAARKVGLAfAAVSwgyAKPEVLKALA 188