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 979879538   3 KALFLDRDGILNKVVirnGTVSSPwflSEFEIMNEAIRVVEAAKALGYMTIVVTNQPDIERKKMNISELEKIHELLNRIF 82
Cdd:cd07503    1 KALFLDRDGVINVDV---PYVHKP---EDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELL 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 979879538  83 -----PLDAILVCTSCDNSD-FRRKPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKTILL 144
Cdd:cd07503   75 asqgvEIDDIYYCPHHPDDGcPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142

D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD resembles the histidinol phosphatase domain of the bifunctional protein HisB. The member from E. coli has been characterized as D,D-heptose 1,7-bisphosphate phosphatase, GmhB, involved in inner core LPS assembly (). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538    3 KALFLDRDGILNkvvIRNGTVSSpwfLSEFEIMNEAIRVVEAAKALGYMTIVVTNQPDIERKKMNISELEKIHE-----L 77
Cdd:TIGR00213   2 KAIFLDRDGTIN---IDHGYVHE---IDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEwmdwsL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538   78 LNRIFPLDAILVC--TSCDNSDFR-----RKPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKT-ILLQTDYN 149
Cdd:TIGR00213  76 AERDVDLDGIYYCphHPEGVEEFRqvcdcRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVAAKVKTnVLVRTGKP 155

                         170       180
                  ....*....|....*....|
gi 979879538  150 TNIHG--IADYNINTLSEVI 167
Cdd:TIGR00213 156 ITPEAenIADWVLNSLADLP 175

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 979879538   3 KALFLDRDGILNKVVirnGTVSSPwflSEFEIMNEAIRVVEAAKALGYMTIVVTNQPDIERKKMNISELEKIHELLNRIF 82
Cdd:cd07503    1 KALFLDRDGVINVDV---PYVHKP---EDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELL 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 979879538  83 -----PLDAILVCTSCDNSD-FRRKPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKTILL 144
Cdd:cd07503   75 asqgvEIDDIYYCPHHPDDGcPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142

D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD resembles the histidinol phosphatase domain of the bifunctional protein HisB. The member from E. coli has been characterized as D,D-heptose 1,7-bisphosphate phosphatase, GmhB, involved in inner core LPS assembly (). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538    3 KALFLDRDGILNkvvIRNGTVSSpwfLSEFEIMNEAIRVVEAAKALGYMTIVVTNQPDIERKKMNISELEKIHE-----L 77
Cdd:TIGR00213   2 KAIFLDRDGTIN---IDHGYVHE---IDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEwmdwsL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538   78 LNRIFPLDAILVC--TSCDNSDFR-----RKPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKT-ILLQTDYN 149
Cdd:TIGR00213  76 AERDVDLDGIYYCphHPEGVEEFRqvcdcRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVAAKVKTnVLVRTGKP 155

                         170       180
                  ....*....|....*....|
gi 979879538  150 TNIHG--IADYNINTLSEVI 167
Cdd:TIGR00213 156 ITPEAenIADWVLNSLADLP 175

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 979879538    3 KALFLDRDGILNKVVIRNGTVSspwflsEFEIMNEAIRVVEAAKALGYMTIVVTNQPDIERKKMNISELEKIHELLNRI- 81
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDED------ERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFSGRVARRLEELg 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 979879538   82 FPLDAILVCTSCdnsdfrRKPNPGMLFEAAKRF-KINLEDSFFLGD-SEKDIIAGKRAGVKTILL 144
Cdd:TIGR01662  75 VPIDILYACPGC------RKPKPGMFLEALKRFnEIDPEESVYVGDqDLTDLQAAKRVGLATILV 133

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538  38 AIRVVEAAKALGYMTIVVTNqpdierkkmniseleKIHELLNRI---FPLDAILVCTSCDNSDFRRKPNPGMLFEAAKRF 114
Cdd:COG0546   89 VRELLEALKARGIKLAVVTN---------------KPREFAERLleaLGLDDYFDAIVGGDDVPPAKPKPEPLLEALERL 153

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538 115 KINLEDSFFLGDSEKDIIAGKRAGVKTILLQTDYNT----NIHGiADYNINTLSEVINIL 170
Cdd:COG0546  154 GLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSaeelEAAG-ADYVIDSLAELLALL 212

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538  31 EFEIMNEAIRVVEAAKALGYMTIVVTNqpdierkkmniSELEKIHELLNR--IFPL-DAILvctSCDnsDFRR-KPNPGM 106
Cdd:COG0637   84 GLPLIPGVVELLEALKEAGIKIAVATS-----------SPRENAEAVLEAagLLDYfDVIV---TGD--DVARgKPDPDI 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 979879538 107 LFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKTILLQTDYNTNIH-GIADYNINTLSEV 166
Cdd:COG0637  148 YLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEElAGADLVVDDLAEL 208

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 979879538  38 AIRVVEAAKALGYMTIVVTNQPDIErkkmniseLEKIHELLNRIFPLDAILvctsCDNSDFRRKPNPGMLFEAAKRFKIN 117
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREA--------LRALLEKLGLGDLFDGII----GSDGGGTPKPKPKPLLLLLLKLGVD 79

                         90       100
                 ....*....|....*....|....*..
gi 979879538 118 LEDSFFLGDSEKDIIAGKRAGVKTILL 144
Cdd:cd01427   80 PEEVLFVGDSENDIEAARAAGGRTVAV 106

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538   1 MKKALFLDRDGILNKVVIRNGTVSSpwfLSEFEIMNEAIRVVEAAKALGYMTIVVTNQPDIERKKMNISELEKIHELLNR 80
Cdd:PRK05446   1 MQKILFIDRDGTLIEEPPTDFQVDS---LDKLAFEPGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLMMQ 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 979879538  81 IFP-----LDAILVCTSC--DNSDFRrKPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKTILLQTDYNT 150
Cdd:PRK05446  78 IFEsqgikFDEVLICPHFpeDNCSCR-KPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIKGIRYARETLN 153

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538   41 VVEAAKALGYMTIVVTNqpdierkKMNiSELEKIHELLNRIFPLDAILvctsCDNSDFRRKPNPGMLFEAAKRFKINLED 120
Cdd:pfam13419  87 LLEELKEQGYKLGIVTS-------KSR-ENVEEFLKQLGLEDYFDVIV----GGDDVEGKKPDPDPILKALEQLGLKPEE 154

                          90       100
                  ....*....|....*....|..
gi 979879538  121 SFFLGDSEKDIIAGKRAGVKTI 142
Cdd:pfam13419 155 VIYVGDSPRDIEAAKNAGIKVI 176

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538  43 EAAKALGYMTIVVTNQPdiERKKMNISELEKIHELLNRIFPLDAILVctscdnsdfrRKPNPGMLFEAAKRFKINLEDSF 122
Cdd:cd16417   97 AALKAQGYPLACVTNKP--ERFVAPLLEALGISDYFSLVLGGDSLPE----------KKPDPAPLLHACEKLGIAPAQML 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 979879538 123 FLGDSEKDIIAGKRAGVKTILLQTDYNtniHG--IADYN----INTLSEVI 167
Cdd:cd16417  165 MVGDSRNDILAARAAGCPSVGLTYGYN---YGedIAASGpdavIDSLAELL 212

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 979879538  38 AIRVVEAAKALGYMTIVVTNQPDierkkmniselEKIHELLNRIFPLDAILVCTSCDNSDFRrKPNPGMLFEAAKRFKIN 117
Cdd:cd07512   91 VIEALERLRAAGWRLAICTNKPE-----------APARALLSALGLADLFAAVVGGDTLPQR-KPDPAPLRAAIRRLGGD 158

                         90       100       110
                 ....*....|....*....|....*....|.
gi 979879538 118 LEDSFFLGDSEKDIIAGKRAGVKTILLQTDY 148
Cdd:cd07512  159 VSRALMVGDSETDAATARAAGVPFVLVTFGY 189

phosphoglycolate phosphatase; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 979879538  99 RRKPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKTILLQTDYNtniHG--IADYN 159
Cdd:PRK13223 155 QKKPDPAALLFVMKMAGVPPSQSLFVGDSRSDVLAAKAAGVQCVALSYGYN---HGrpIAEES 214

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        40
                 ....*....|....*....|....*....|....*....|....*..
gi 979879538 101 KPNPGMLFEAAKRFKINLEDSFFLGDS-EKDIIAGKRAGVKTILLQT 146
Cdd:cd07530  177 KPEPIMMRAALEKLGLKSEETLMVGDRlDTDIAAGIAAGIDTLLVLT 223

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 979879538   20 NGTVSSPwflseFEIMNEAIRVVEAAkalGYMTIVVTNQPdiERKKMNISELEKIHELLNRIFPLDAILvctscdnsdfR 99
Cdd:TIGR01449  80 AGELTSV-----FPGVEATLGALRAK---GLRLGLVTNKP--TPLARPLLELLGLAKYFSVLIGGDSLA----------Q 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 979879538  100 RKPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKTILLQTDYN 149
Cdd:TIGR01449 140 RKPHPDPLLLAAERLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYGYR 189

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 979879538 101 KPNPGMLFEAAKRFKINLEDSFFLGDS-EKDIIAGKRAGVKTILLQT 146
Cdd:COG0647  186 KPSPPIYELALERLGVDPERVLMVGDRlDTDILGANAAGLDTLLVLT 232

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 979879538  40 RVVEAAKAL---GYMTIVVTNQPDIERKKMNISELE-KIHELLNRIfpLDAILVCTSCdNSDFRRKPNPGM----LFEAA 111
Cdd:cd01625   33 SVPEKLKALhkdGYKIVIFTNQGGIVRGKLTPEVFKgKIEAILEKL--GVPIQVYAAT-KKGKYRKPVTGMwdhlKEDLN 109

                         90
                 ....*....|....*
gi 979879538 112 KRFKINLEDSFFLGD 126
Cdd:cd01625  110 SGIPINLKDSFYVGD 124

pyrophosphatase PpaX; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538  28 FLSEFEIMNEAIRVVeaaKALGYMTIVVTNQpdIERKKMNISELEKIHELLNRIFPLDAILvctscdnsdfRRKPNPGML 107
Cdd:PRK13288  80 LVTEYETVYETLKTL---KKQGYKLGIVTTK--MRDTVEMGLKLTGLDEFFDVVITLDDVE----------HAKPDPEPV 144

                         90       100       110
                 ....*....|....*....|....*....|....
gi 979879538 108 FEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKT 141
Cdd:PRK13288 145 LKALELLGAKPEEALMVGDNHHDILAGKNAGTKT 178

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538  35 MNEAIRVVEAAKALGYMTI---VVTNQPDIERKKMniselekIHELLNRIFplDAILvctsCDNSDFRRKPNPGMLFEAA 111
Cdd:cd16421    6 LDGTLLILELLKALRQKGIklaVLSNKPNEAVQVL-------VEELFPGSF--DFVL----GEKEGIRRKPDPT*ALECA 72

                         90       100
                 ....*....|....*....|....*...
gi 979879538 112 KRFKINLEDSFFLGDSEKDIIAGKRAGV 139
Cdd:cd16421   73 KVLGVPPDEVLYVGDSGVDMQTARNAGM 100

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 979879538   2 KKALFLDRDGILNKVVIRNGTVsspwflsefEIMNEAIRVVEAAKALGYMTIVVTNqpdierkkmniSELEKIHELLNRI 81
Cdd:cd16423   22 QELLNERRNELIKRQFSEKTDL---------PPIEGVKELLEFLKEKGIKLAVASS-----------SPRRWIEPHLERL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 979879538  82 FPLDAILVCTSCDnsDFRR-KPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKTI 142
Cdd:cd16423   82 GLLDYFEVIVTGD--DVEKsKPDPDLYLEAAERLGVNPEECVVIEDSRNGVLAAKAAGMKCV 141

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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
                 ....*....|....*....|....*....|....*....|....*....|.
gi 979879538 101 KPNPGMLFEAAKRFKINLEDSFFLGDS-EKDIIAGKRAGVKTILLQTDYNT 150
Cdd:cd07508  197 KPSPWLGELALEKFGIDPERVLFVGDRlATDVLFGKACGFQTLLVLTGVTT 247

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 979879538  91 TSCDNSDFRRKPNPGMLFEAAKRFKINLEDSFFLGDSEKDIIAGKRAGVKTIL 143
Cdd:cd02604  127 FDIEYAGPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVL 179