Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  11 IVFDNDGVLtYPTDESVLtEASQRAFAAFDV-DPTPSDVRSLVDDLSVETVRRLAKRYEVDAD--AFWRRHETErtarql 87
Cdd:pfam13419   1 IIFDFDGTL-LDTEELII-KSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKieFYLRKYNEE------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  88 aaIRDGEKPLYDDV----ETLADLAVPTAIVSNNQHATIEHIVAEFGLEAMFEAYYGREPslrgLERRKPDPSYLEAALD 163
Cdd:pfam13419  73 --LHDKLVKPYPGIkellEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDD----VEGKKPDPDPILKALE 146

                         170
                  ....*....|....*
gi 1565817571 164 ELGV--ESALYVGDS 176
Cdd:pfam13419 147 QLGLkpEEVIYVGDS 161

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571   6 TQYNAIVFDNDGVLTyptdESV--LTEASQRAFAAFDVDPTPSD-VRSLVDDlsveTVRRLAKRyevdadAF-WRRHETE 81
Cdd:PRK13222    4 MDIRAVAFDLDGTLV----DSApdLAAAVNAALAALGLPPAGEErVRTWVGN----GADVLVER------ALtWAGREPD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  82 ----RTARQL-----AAIRDGEKPLYDDV-ETLADLA---VPTAIVSNNQHATIEHIVAEFGLEAMFEAYYGrepslrG- 147
Cdd:PRK13222   70 eellEKLRELfdrhyAENVAGGSRLYPGVkETLAALKaagYPLAVVTNKPTPFVAPLLEALGIADYFSVVIG------Gd 143

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1565817571 148 -LERRKPDPSYLEAALDELGV--ESALYVGDSRV 178
Cdd:PRK13222  144 sLPNKKPDPAPLLLACEKLGLdpEEMLFVGDSRN 177

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  11 IVFDNDGVLtYPTDESVLtEASQRAFAAFDV-DPTPSDVRSLVDDLSVETVRRLAKRYEVDAD--AFWRRHETErtarql 87
Cdd:pfam13419   1 IIFDFDGTL-LDTEELII-KSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKieFYLRKYNEE------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  88 aaIRDGEKPLYDDV----ETLADLAVPTAIVSNNQHATIEHIVAEFGLEAMFEAYYGREPslrgLERRKPDPSYLEAALD 163
Cdd:pfam13419  73 --LHDKLVKPYPGIkellEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDD----VEGKKPDPDPILKALE 146

                         170
                  ....*....|....*
gi 1565817571 164 ELGV--ESALYVGDS 176
Cdd:pfam13419 147 QLGLkpEEVIYVGDS 161

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 1565817571   8 YNAIVFDNDGVLTYPtdESVLTEASQRAFAAFDVDPTPSDVRSLVDDLSVETVRRLAkRYEVDADAFWRR-------HET 80
Cdd:COG1011     1 IKAVLFDLDGTLLDF--DPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYE-RGEITFAELLRRlleelglDLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  81 ERTARQLAAIRDGEKPLYDDV-ETLADLA---VPTAIVSNNQHATIEHIVAEFGLEAMFEAYYGREPslrgLERRKPDPS 156
Cdd:COG1011    78 EELAEAFLAALPELVEPYPDAlELLEALKargYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEE----VGVRKPDPE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1565817571 157 YLEAALDELGV--ESALYVGDSrvdvaaaraagvDAAFVNRPHRRGYR------------LDIRPTYRLDSLAELASL 220
Cdd:COG1011   154 IFELALERLGVppEEALFVGDS------------PETDVAGARAAGMRtvwvnrsgepapAEPRPDYVISDLAELLEL 219

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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 1565817571  11 IVFDNDGVLTYPTDESVltEASQRAFAAFDV-DPTPSDVRSLVDDLSVETVRRLAKRYEVDADAFWRRhETERtARQLAA 89
Cdd:cd07533     2 VIFDWDGTLADSQHNIV--AAMTAAFADLGLpVPSAAEVRSIIGLSLDEAIARLLPMATPALVAVAER-YKEA-FDILRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  90 IRDGEKPLYDDV-ETLADLAVP---TAIVSNNQHATIEHIVAEFGLEAMFEAYY--GREPSlrglerrKPDPSYLEAALD 163
Cdd:cd07533    78 LPEHAEPLFPGVrEALDALAAQgvlLAVATGKSRRGLDRVLEQHGLGGYFDATRtaDDTPS-------KPHPEMLREILA 150

                         170
                  ....*....|....*
gi 1565817571 164 ELGVE--SALYVGDS 176
Cdd:cd07533   151 ELGVDpsRAVMVGDT 165

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  10 AIVFDNDGVLtYPTDESVLtEASQRAFAAFDVDPtpsdvrslvddlsvETVRRLAKRYEVDADAFWRrHETERTARQL-- 87
Cdd:TIGR01549   1 AILFDIDGTL-VDIKFAIR-RAFPQTFEEFGLDP--------------ASFKALKQAGGLAEEEWYR-IATSALEELQgr 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  88 --AAIRDGEK---PLYDDVETLADLAVPTAIVSNNQHATIEHIVAEFGLEAMFEayygrEPSLRGLERRKPDPSYLEAAL 162
Cdd:TIGR01549  64 fwSEYDAEEAyirGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFE-----LILVSDEPGSKPEPEIFLAAL 138

                         170
                  ....*....|....*
gi 1565817571 163 DELGVES-ALYVGDS 176
Cdd:TIGR01549 139 ESLGVPPeVLHVGDN 153

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 1565817571   8 YNAIVFDNDGVLTYPTDesVLTEASQRAFAAF-DVDPTPSDVRSLVDDLSVETVRRLAKRYEVDADAFWRRHEtertarq 86
Cdd:cd02616     1 ITTILFDLDGTLIDTNE--LIIKSFNHTLKEYgLEGYTREEVLPFIGPPLRETFEKIDPDKLEDMVEEFRKYY------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  87 lAAIRDGEKPLYDDV-ETLADL---AVPTAIVSNNQHATIEHIVAEFGLEAMFEAYYGREpslrGLERRKPDPSYLEAAL 162
Cdd:cd02616    72 -REHNDDLTKEYPGVyETLARLksqGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGD----DVTHHKPDPEPVLKAL 146

                         170
                  ....*....|....*.
gi 1565817571 163 DELGV--ESALYVGDS 176
Cdd:cd02616   147 ELLGAepEEALMVGDS 162

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 1565817571  10 AIVFDNDGVLTyptdESV--LTEASQRAFAAFDVDPTPSDV--------------RSLVDDLSVETVRRLAKRYEVDADA 73
Cdd:cd16417     1 LVAFDLDGTLV----DSApdLAEAANAMLAALGLPPLPEETvrtwigngadvlveRALTGAREAEPDEELFKEARALFDR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  74 FWRRHETERTArqlaairdgekpLYDDV-ETLADLA---VPTAIVSNNQHATIEHIVAEFGLEAMFEAYYGrepslrG-- 147
Cdd:cd16417    77 HYAETLSVHSH------------LYPGVkEGLAALKaqgYPLACVTNKPERFVAPLLEALGISDYFSLVLG------Gds 138

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1565817571 148 LERRKPDPSYLEAALDELGV--ESALYVGDSRV 178
Cdd:cd16417   139 LPEKKPDPAPLLHACEKLGIapAQMLMVGDSRN 171

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 1565817571  92 DGEKPLYDDVETLADLAVPTAIVSNNQHATIEHIVAEFGlEAMFEAYYGREPSLRglerRKPDPSYLEAALDELGV--ES 169
Cdd:cd16421     7 DGTLLILELLKALRQKGIKLAVLSNKPNEAVQVLVEELF-PGSFDFVLGEKEGIR----RKPDPT*ALECAKVLGVppDE 81

                  ....*..
gi 1565817571 170 ALYVGDS 176
Cdd:cd16421    82 VLYVGDS 88

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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 1565817571   9 NAIVFDNDGVLTYPTDESVLteasqRAFAAFDVDPTPSDVRSLVDDLsvetVRRLAKRYEVDADAFWR--RHETER---- 82
Cdd:cd02603     2 RAVLFDFGGVLIDPDPAAAV-----ARFEALTGEPSEFVLDTEGLAG----AFLELERGRITEEEFWEelREELGRplsa 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  83 --TARQLAAIRDGEKPLYDDVETLADLAVPTAIVSNNQHATIEHIVAEF-GLEAMFEAYYgrEPSLRGLerRKPDPSYLE 159
Cdd:cd02603    73 elFEELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLpRRGDLFDGVV--ESCRLGV--RKPDPEIYQ 148

                         170
                  ....*....|....*....
gi 1565817571 160 AALDELGV--ESALYVGDS 176
Cdd:cd02603   149 LALERLGVkpEEVLFIDDR 167

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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 1565817571  53 DDLSVETVRRLAKRYEVDADAFWRRHETERtARQLaairdgekPLYDDV----ETLADLAVPTAIVSNNQHATIEHIVAE 128
Cdd:cd02588    57 DELTRDALRATAAELGLELDESDLDELGDA-YLRL--------PPFPDVvaglRRLREAGYRLAILSNGSPDLIEDVVAN 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571 129 FGLEAMFEAYYGREpslrGLERRKPDPSYLEAALDELGV--ESALYVGDSRVDVAAARAAGVDAAFVNRPHRRGYRLDIR 206
Cdd:cd02588   128 AGLRDLFDAVLSAE----DVRAYKPAPAVYELAAERLGVppDEILHVASHAWDLAGARALGLRTAWINRPGEVPDPLGPA 203

                         170
                  ....*....|...
gi 1565817571 207 PTYRLDSLAELAS 219
Cdd:cd02588   204 PDFVVPDLGELAD 216

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 1565817571  11 IVFDNDGVLTYPTDEsvLTEASQRAFAAFDVDPTPSD-VRSLVDDLSVETVRRL--AKRYEVDADA-------FWRRHET 80
Cdd:TIGR01449   1 VLFDLDGTLVDSAPD--IAAAVNMALAALGLPPATLArVIGFIGNGVPVLMERVlaWAGQEPDAQRvaelrklFDRHYEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565817571  81 erTARQLAAIRDGEKplyDDVETLADLAVPTAIVSNNQHATIEHIVAEFGLEAMFEAYYGREpslrGLERRKPDPSYLEA 160
Cdd:TIGR01449  79 --VAGELTSVFPGVE---ATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGD----SLAQRKPHPDPLLL 149

                         170
                  ....*....|....*....
gi 1565817571 161 ALDELGVESA--LYVGDSR 177
Cdd:TIGR01449 150 AAERLGVAPQqmVYVGDSR 168

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
                  ....*....|....*....|....*..
gi 1565817571 152 KPDPSYLEAALDELGV--ESALYVGDS 176
Cdd:cd04305    64 KPNPEIFDYALNQLGVkpEETLMVGDS 90