D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193    3 KSVPAIFLDRDGTINVDH-GYVHEIDNFEFIDGVIDAMRELKKMGFALVVVTNQSGIARGKFTEAQFETLTEWMDWSLAD 81
Cdd:PRK08942   1 KSMKAIFLDRDGVINVDSdGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193   82 RDVDLDGIYYCPHHPQGSveefrqvCDCRKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANVgTKVLVRTGKPI 161
Cdd:PRK08942  81 RGGRLDGIYYCPHHPEDG-------CDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGV-TPVLVRTGKGV 152

                        170       180
                 ....*....|....*....|....*....
gi 16128193  162 TPEAENAA--DWVLNSLADLPQAIKKQQK 188
Cdd:PRK08942 153 TTLAEGAApgTWVLDSLADLPQALKKQQK 181

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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 16128193   6 PAIFLDRDGTINVDHGYVHEIDNFEFIDGVIDAMRELKKMGFALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRDVD 85
Cdd:cd07503   1 KALFLDRDGVINVDVPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128193  86 LDGIYYCPHHPQgsveefrQVCDCRKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANVGT 151
Cdd:cd07503  81 IDDIYYCPHHPD-------DGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKG 139

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193    3 KSVPAIFLDRDGTINVDH-GYVHEIDNFEFIDGVIDAMRELKKMGFALVVVTNQSGIARGKFTEAQFETLTEWMDWSLAD 81
Cdd:PRK08942   1 KSMKAIFLDRDGVINVDSdGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193   82 RDVDLDGIYYCPHHPQGSveefrqvCDCRKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANVgTKVLVRTGKPI 161
Cdd:PRK08942  81 RGGRLDGIYYCPHHPEDG-------CDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGV-TPVLVRTGKGV 152

                        170       180
                 ....*....|....*....|....*....
gi 16128193  162 TPEAENAA--DWVLNSLADLPQAIKKQQK 188
Cdd:PRK08942 153 TTLAEGAApgTWVLDSLADLPQALKKQQK 181

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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 16128193   6 PAIFLDRDGTINVDHGYVHEIDNFEFIDGVIDAMRELKKMGFALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRDVD 85
Cdd:cd07503   1 KALFLDRDGVINVDVPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128193  86 LDGIYYCPHHPQgsveefrQVCDCRKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANVGT 151
Cdd:cd07503  81 IDDIYYCPHHPD-------DGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKG 139

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193     6 PAIFLDRDGTINVDHGYVHEIDNFEFIDGVIDAMRELKKMGFALVVVTNQSGIARGKFTEAqfetLTEWMDWSLADRDVD 85
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRS----FSGRVARRLEELGVP 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193    86 LDGIYYCPHhpqgsveefrqvcdCRKPHPGMLLSA-RDYLHIDMAASYMVGDK-LEDMQAavAANVGTKV 153
Cdd:TIGR01662  77 IDILYACPG--------------CRKPKPGMFLEAlKRFNEIDPEESVYVGDQdLTDLQA--AKRVGLAT 130

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193    6 PAIFLDRDGTInvdhgyVHE------IDNFE---FIDGVIDAMRELKKMGFALVVVTNQSGIARGKFTEAQFETLTEWMD 76
Cdd:PRK05446   3 KILFIDRDGTL------IEEpptdfqVDSLDklaFEPGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLMM 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128193   77 WSLADRDVDLDGIYYCPHHPQgsveefrQVCDCRKPHPGMLlsaRDYLH---IDMAASYMVGDKLEDMQaaVAANVGTK 152
Cdd:PRK05446  77 QIFESQGIKFDEVLICPHFPE-------DNCSCRKPKTGLV---EEYLAegaIDLANSYVIGDRETDVQ--LAENMGIK 143

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193  24 HEIDNFEFIDGVIDAMRELKKMGFALVVVTNqsgiargkFTEAQFETLTEWMDWsladrDVDLDGIYYCPHHPQgsveef 103
Cdd:COG0546  78 ELLDETRLFPGVRELLEALKARGIKLAVVTN--------KPREFAERLLEALGL-----DDYFDAIVGGDDVPP------ 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193 104 rqvcdcRKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANVGTkVLVRTGkPITPE--AENAADWVLNSLADLPQ 181
Cdd:COG0546 139 ------AKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPF-IGVTWG-YGSAEelEAAGADYVIDSLAELLA 210

                ....
gi 16128193 182 AIKK 185
Cdd:COG0546 211 LLAE 214

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193  27 DNFEFIDGVIDAMRELKKMGFALVVVTNqsgiargkfteAQFETLTEWMDWS-LADRdvdLDGIYycphhpqgSVEEFRq 105
Cdd:COG1011  90 ELVEPYPDALELLEALKARGYRLALLTN-----------GSAELQEAKLRRLgLDDL---FDAVV--------SSEEVG- 146

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128193 106 vcdCRKPHPGMLLSARDYLHIDMAASYMVGDKLE-DMQAAVAANVGTkVLVrTGKPITPEAENAADWVLNSLADLPQAI 183
Cdd:COG1011 147 ---VRKPDPEIFELALERLGVPPEEALFVGDSPEtDVAGARAAGMRT-VWV-NRSGEPAPAEPRPDYVISDLAELLELL 220

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193  33 DGVIDAMRELKKMGFALVVVTNQSGIArgkfTEAQFETLtewmdwSLADRdvdldgiyycphhpqgsveeFRQVC--DC- 109
Cdd:cd07512  89 PGVIEALERLRAAGWRLAICTNKPEAP----ARALLSAL------GLADL--------------------FAAVVggDTl 138

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128193 110 --RKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANVGTkVLVRTGKPITPEAENAADWVLNSLADLPQAI 183
Cdd:cd07512 139 pqRKPDPAPLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPF-VLVTFGYRHAPVAELPHDAVFSDFDALPDLL 213

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193    27 DNFEFIDGVIDAMRELKKMGFALVVVTNQS-GIARGKFTEAQFETLtewmdwsladrdvdLDGIYycphhpqGSVEEFRq 105
Cdd:pfam13419  76 KLVKPYPGIKELLEELKEQGYKLGIVTSKSrENVEEFLKQLGLEDY--------------FDVIV-------GGDDVEG- 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 16128193   106 vcdcRKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANV 149
Cdd:pfam13419 134 ----KKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGI 173

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193    33 DGVIDAMRELKKMGFALVVVTNQSgiargKFTEAQFETLTEWMDWSladrDVDLDGiyycphhpqGSVEEfrqvcdcRKP 112
Cdd:TIGR01449  88 PGVEATLGALRAKGLRLGLVTNKP-----TPLARPLLELLGLAKYF----SVLIGG---------DSLAQ-------RKP 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128193   113 HPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANVGTKVLVRTGKPITPEAENAADWVLNSLADLPQAI 183
Cdd:TIGR01449 143 HPDPLLLAAERLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYGYRYGEAIDLLPPDVLYDSLNELPPLL 213

Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193     8 IFLDRDGT-INVDHGYVHEI--DNFEFI-DGVIDAMRELKKMGFALVVVTNQSGIARGkfTEAQFETLTEWMDWSLADRD 83
Cdd:pfam08645   3 AAFDLDGTlIKTKSGKVFPRnpDDWKWLyPSVPEKLKKLHEDGYKIVIFTNQGGIGRK--GKKSLEKFKNKIEAILKKLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128193    84 VDL-------DGIYycphhpqgsveefrqvcdcRKPHPGMLLS-ARDYLH---IDMAASYMVGD 136
Cdd:pfam08645  81 VPLqvyaatkKDIY-------------------RKPNTGMWDEmKKDYNDgveIDLEKSFYVGD 125

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 16128193   7 AIFLDRDGTInvdhgYVHEidnfefidgvidAMRELKKMGFALVVVTNQSGiargKFTEAQFETLtewmdwslaDRDVDL 86
Cdd:cd01427   1 AVLFDLDGTL-----LAVE------------LLKRLRAAGIKLAIVTNRSR----EALRALLEKL---------GLGDLF 50

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128193  87 DGIYYCPHHPQgsveefrqvcdcRKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANvGTKVLV 155
Cdd:cd01427  51 DGIIGSDGGGT------------PKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAG-GRTVAV 106

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. 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 16128193  33 DGVIDAMRELKKMGFALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRDVdldgIYYCPHhpqgsVEEFrqvcdcRKP 112
Cdd:cd01625  32 PSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTPEVFKGKIEAILEKLGVPIQ----VYAATK-----KGKY------RKP 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128193 113 HPGM----LLSARDYLHIDMAASYMVGD---KLEDMQAA---VAANVGTKVlvrtgkpITPE 164
Cdd:cd01625  97 VTGMwdhlKEDLNSGIPINLKDSFYVGDaagRPKDFSDSdrlFAENVGLKF-------FTPE 151

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128193     8 IFLDRDGTINVDHgyvheidnfEFIDGVIDAMRELKKMGFALVVVTNQSGIARGKFTEaQFETL 71
Cdd:pfam13344   1 FLFDIDGVLWRGG---------EPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAE-KLRKL 54

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193  24 HEIDNFEFIDGVIDAMRELKKMGFALVVVTNqsgiaRGKFTEAQFETLTEWMDWslADRDVDLDgiyycphhpqgSVEEf 103
Cdd:cd02616  74 HNDDLTKEYPGVYETLARLKSQGIKLGVVTT-----KLRETALKGLKLLGLDKY--FDVIVGGD-----------DVTH- 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128193 104 rqvcdcRKPHPGMLLSARDYLHIDMAASYMVGDKLEDMQAAVAANVGTKVLVRTGKPITPEAENAADWVLNSLADL 179
Cdd:cd02616 135 ------HKPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFNPDFIIDKMSDL 204

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It 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        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128193 104 RQVCDCRKPHPGMLLSARDYLHIDMAASYMVGDKLE-DMQAAVAANVGTkVLVRTGKPITPEAEN------AADWVLNSL 176
Cdd:cd07510 197 RQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDtDILFGQNCGLKT-LLVLTGVSTLEEALAklsndlVPDYYVESL 275

                ...
gi 16128193 177 ADL 179
Cdd:cd07510 276 ADL 278

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 16128193  31 FIDGVIDAMRELKKMGFALVVVTNqsgiarGKFTEAQFETLTEWMDWSLAD 81
Cdd:COG1180  87 QPEFLLDLAKLAKELGLHTALDTN------GYIPEEALEELLPYLDAVNID 131