phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        3 KALFFDIDGTLVSFEThRIPSSTIEALEAAHAKGLKIFIATGRPKAIINNLSElqdRNLIDGYITMNGAYCFVGEEVIYK 82
Cdd:cd07517   1 KIVFFDIDGTLLDEDT-TIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVK---ALGIDSYVSYNGQYVFFEGEVIYK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A       83 SAIPQEEVKAMAAFCEKKGVPCIFVEehnisvcqpnemvkkifydflhvnviptvsfeeasnkeviQMTPFITEEEEKEV 162
Cdd:cd07517  77 NPLPQELVERLTEFAKEQGHPVSFYG----------------------------------------QLLLFEDEEEEQKY 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A      163 LPSIPTCEIGRWYPAFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQAKEDVKAAADYV 242
Cdd:cd07517 117 EELRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYV 196

                       250
                ....*....|....*..
1YMQ_A      243 TAPIDEDGISKAMKHFG 259
Cdd:cd07517 197 TKDVDEDGILKALKHFG 213

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        3 KALFFDIDGTLVSFEThRIPSSTIEALEAAHAKGLKIFIATGRPKAIINNLSElqdRNLIDGYITMNGAYCFVGEEVIYK 82
Cdd:cd07517   1 KIVFFDIDGTLLDEDT-TIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVK---ALGIDSYVSYNGQYVFFEGEVIYK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A       83 SAIPQEEVKAMAAFCEKKGVPCIFVEehnisvcqpnemvkkifydflhvnviptvsfeeasnkeviQMTPFITEEEEKEV 162
Cdd:cd07517  77 NPLPQELVERLTEFAKEQGHPVSFYG----------------------------------------QLLLFEDEEEEQKY 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A      163 LPSIPTCEIGRWYPAFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQAKEDVKAAADYV 242
Cdd:cd07517 117 EELRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYV 196

                       250
                ....*....|....*..
1YMQ_A      243 TAPIDEDGISKAMKHFG 259
Cdd:cd07517 197 TKDVDEDGILKALKHFG 213

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A          5 LFFDIDGTLVSfETHRIPSSTIEALEAAHAKGLKIFIATGRP-KAIINNLSELqdrNLIDGYITMNGAYC-FVGEEVIYK 82
Cdd:pfam08282   1 IASDLDGTLLN-SDKKISEKTKEAIKKLKEKGIKFVIATGRPyRAILPVIKEL---GLDDPVICYNGALIyDENGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A         83 SAIPQEEVKAMAAFCEKKGVPCIFVEEHNISVCQPNEMVKKIFYDFLHVNVIPTV-SFEEASNKEVIQMTPFITEEEEKE 161
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIdDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        162 VLPSIP-----TCEIGRWYPAFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQAKEDVK 236
Cdd:pfam08282 157 LEKELKelfgsLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*....
1YMQ_A        237 AAADYVTAPIDEDGISKAM 255
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKAL 255

sugar phosphate phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A         8 DIDGTLVSfETHRIPSSTIEALEAAHAKGLKIFIATGRPKAIINN-LSELQDRNLIDGYITMNGAYC--FVGEEVIYKSA 84
Cdd:PRK10513   9 DMDGTLLL-PDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRyLKELHMEQPGDYCITNNGALVqkAADGETVAQTA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        85 IPQEEVKamaaFCEK--KGVPCIFVEEHNISVCQPNEMVKKIFYDFLHVNVIPTvsfeeaSNKEVIQMTPFITEE----- 157
Cdd:PRK10513  88 LSYDDYL----YLEKlsREVGVHFHALDRNTLYTANRDISYYTVHESFLTGIPL------VFREVEKMDPNLQFPkvmmi 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A       158 EEKEVLPS----IPTCEIGRWY-----PAFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAM 228
Cdd:PRK10513 158 DEPEILDAaiarIPAEVKERYTvlksaPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAM 237

                        250       260       270
                 ....*....|....*....|....*....|
1YMQ_A       229 GQAKEDVKAAADYVTAPIDEDGISKAMKHF 258
Cdd:PRK10513 238 GNAIPSVKEVAQFVTKSNLEDGVAFAIEKY 267

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        3 KALFFDIDGTLVSFEThRIPSSTIEALEAAHAKGLKIFIATGRPKAIINNLSElqdRNLIDGYITMNGAYCFVGEEVIYK 82
Cdd:cd07517   1 KIVFFDIDGTLLDEDT-TIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVK---ALGIDSYVSYNGQYVFFEGEVIYK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A       83 SAIPQEEVKAMAAFCEKKGVPCIFVEehnisvcqpnemvkkifydflhvnviptvsfeeasnkeviQMTPFITEEEEKEV 162
Cdd:cd07517  77 NPLPQELVERLTEFAKEQGHPVSFYG----------------------------------------QLLLFEDEEEEQKY 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A      163 LPSIPTCEIGRWYPAFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQAKEDVKAAADYV 242
Cdd:cd07517 117 EELRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYV 196

                       250
                ....*....|....*..
1YMQ_A      243 TAPIDEDGISKAMKHFG 259
Cdd:cd07517 197 TKDVDEDGILKALKHFG 213

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A          5 LFFDIDGTLVSfETHRIPSSTIEALEAAHAKGLKIFIATGRP-KAIINNLSELqdrNLIDGYITMNGAYC-FVGEEVIYK 82
Cdd:pfam08282   1 IASDLDGTLLN-SDKKISEKTKEAIKKLKEKGIKFVIATGRPyRAILPVIKEL---GLDDPVICYNGALIyDENGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A         83 SAIPQEEVKAMAAFCEKKGVPCIFVEEHNISVCQPNEMVKKIFYDFLHVNVIPTV-SFEEASNKEVIQMTPFITEEEEKE 161
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIdDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        162 VLPSIP-----TCEIGRWYPAFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQAKEDVK 236
Cdd:pfam08282 157 LEKELKelfgsLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*....
1YMQ_A        237 AAADYVTAPIDEDGISKAM 255
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKAL 255

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        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        5 LFFDIDGTLVSfETHRIPSSTIEALEAAHAKGLKIFIATGRP-KAIINNLSELQDRNLIdgyITMNGAYCF-VGEEVIYK 82
Cdd:cd07516   2 IALDLDGTLLN-SDKEISPRTKEAIKKAKEKGIKVVIATGRPlRGAQPYLEELGLDSPL---ITFNGALVYdPTGKEILE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A       83 SAIPQEEVKAMAAFCEKKGVPC-IFVEEHNisvcqpnemvKKIFY-----DFLHVNVIPTVSFEEASNKEVIQM-----T 151
Cdd:cd07516  78 RLISKEDVKELEEFLRKLGIGInIYTNDDW----------ADTIYeenedDEIIKPAEILDDLLLPPDEDITKIlfvgeD 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A      152 PFITEEEEKEVLPSIPTCEIGRWYPAFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQA 231
Cdd:cd07516 148 EELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                       250       260
                ....*....|....*....|....*.
1YMQ_A      232 KEDVKAAADYVTAPIDEDGISKAMKH 257
Cdd:cd07516 228 IDEVKEAADYVTLTNNEDGVAKAIEK 253

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A          4 ALFFDIDGTLVSFETHRIPSSTIEALEAAHAKGLKIFIATGRPKAIINNLseLQDRNLIDGYITMNGAYCFVGEEVIYKS 83
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKEL--LKQLNLPLPLIAENGALIFYPGEILYIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A         84 AIPQEEVkAMAAFCEKKGvpcifVEEHNISVCQPNEMV--KKIFYDFLHVNVIPtvsFEEASNKEVIQMTPFITEEEEKE 161
Cdd:TIGR01484  79 PSDVFEE-ILGIKFEEIG-----AELKSLSEHYVGTFIedKAIAVAIHYVGAEL---GQELDSKMRERLEKIGRNDLELE 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1YMQ_A        162 VLPSIPTCeigrwypafADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAM 228
Cdd:TIGR01484 150 AIYSGKTD---------LEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207

pyridoxal phosphate (PLP) phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A         8 DIDGTLVSFETHRIPSStIEALEAAHAKGLKIFIATGRPKAIINNLseLQDRNLIDGYITMNGAYC--FVGEEVIYKSAI 85
Cdd:PRK10530   9 DLDGTLLTPKKTILPES-LEALARAREAGYKVIIVTGRHHVAIHPF--YQALALDTPAICCNGTYLydYQAKKVLEADPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        86 PQEEVKAMAAFCEKKGVP-CIFVEehnisvcqpNEMVkkifYDFLHVNVIPTV------------------SFEEASnKE 146
Cdd:PRK10530  86 PVQQALQVIEMLDEHQIHgLMYVD---------DAML----YEHPTGHVIRTLnwaqtlppeqrptftqvdSLAQAA-RQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A       147 VIQMTPFITEEEEKEVLPSIpTCEIGR---------WYPAfADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDIS 217
Cdd:PRK10530 152 VNAIWKFALTHEDLPQLQHF-AKHVEHelglecewsWHDQ-VDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDIS 229

                        250       260       270
                 ....*....|....*....|....*....|....*.
1YMQ_A       218 MLRHAAIGVAMGQAKEDVKAAADYVTAPIDEDGISK 253
Cdd:PRK10530 230 MLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAE 265

phosphoglycolate phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A         1 MTKALFFDIDGTLvSFETHRIPSSTIEALEAAHAKGLKIFIATGRPKAIINNLSELqdrnlidgyITMNGAycFVGEE-- 78
Cdd:PRK01158   2 KIKAIAIDIDGTI-TDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKL---------IGTSGP--VIAENgg 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        79 VIYKsaipqeevkamaafceKKGVPCIFVEEhnISVCqpnEMVKKIFYDFLHVNVIPTVSFEEASNKEVIQMTPFITEEE 158
Cdd:PRK01158  70 VISV----------------GFDGKRIFLGD--IEEC---EKAYSELKKRFPEASTSLTKLDPDYRKTEVALRRTVPVEE 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A       159 EKEVLPSIPTcEIGRWYPAFA-DVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQAKEDVKA 237
Cdd:PRK01158 129 VRELLEELGL-DLEIVDSGFAiHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKE 207

                        250       260
                 ....*....|....*....|..
1YMQ_A       238 AADYVTAPIDEDGISKAMKHFG 259
Cdd:PRK01158 208 AADYVTEKSYGEGVAEAIEHLL 229

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1YMQ_A      185 GDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQAKEDVKAAADYVTAPIDEDGISKAMKHF 258
Cdd:cd07514  65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKL 138

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        5 LFFDIDGTLVSfetHRIPSSTIEALEA-----AHAKGLKIFIATGRPKAIInnlSELQDRN--LIDGYITMN-------G 70
Cdd:cd02605   2 LVSDLDETLVG---HDTNLQALERLQDlleqlTADNDVILVYATGRSPESV---LELIKEVmlPKPDFIISDvgteiyyG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A       71 AYCFVGEEVIYKSAIPQ----EEVKAMAAfcekkgvpcIFVEEHNISVCQPNEMvkKIFYdFLHVNVIPTV--SFEEASN 144
Cdd:cd02605  76 ESGYLEPDTYWNEVLSEgwerFLFEAIAD---------LFKQLKPQSELEQNPH--KISF-YLDPQNDAAVieQLEEMLL 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A      145 KEVIQMTPFITeeeekevlpsiptceIGRWYpaFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAI 224
Cdd:cd02605 144 KAGLTVRIIYS---------------SGLAY--DLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTR 206

                       250       260       270
                ....*....|....*....|....*....|....*....
1YMQ_A      225 GVAMGQAKEDVKAAADYVTAPIDED-----GISKAMKHF 258
Cdd:cd02605 207 GVIVGNAQPELLKWADRVTRSRLAKgpyagGILEGLAHF 245

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
1YMQ_A      185 GDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGqAKEDVKAAAD 240
Cdd:COG0560 153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVN-PDPALREAAD 207

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
                ....*....|....*....|....*....|....*....|....*...
1YMQ_A      180 DVTAKGDTKQkgidEIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVA 227
Cdd:cd07500 134 DAQRKAETLQ----ELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1YMQ_A        4 ALFFDIDGTLVSFETH----RIPSSTIEALEA-AHAKGLKIFIATGRPKAIINNLSELQDRNLI 62
Cdd:COG1877   5 LLFLDFDGTLAPIVPDpdaaRPPPELRELLRRlAARPGGAVAIVSGRDLADLDRLLGPLGLPLA 68

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A          3 KALFFDIDGTLVsfETHRIPSSTIEALEAAHAKGLKIFIATGRPKAIINNLSELQdrnlidgyitMNGAYCFVGEEVIYK 82
Cdd:pfam00702   2 KAVVFDLDGTLT--DGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARL----------LLGKRDWLEELDILR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A         83 SAIPQEEVKAMAAFCEKKGVPCIFVEEHnisvcQPNEMVKKIFyDFLHVNVIPTVSfeeASNKEVIQMTPFITEEEEKEV 162
Cdd:pfam00702  70 GLVETLEAEGLTVVLVELLGVIALADEL-----KLYPGAAEAL-KALKERGIKVAI---LTGDNPEAAEALLRLLGLDDY 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        163 LPSIptceigrwypAFADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHA 222
Cdd:pfam00702 141 FDVV----------ISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAA 190

alpha-subunit of Na(+)/K(+)-ATPases and of gastric H(+)/K(+)-ATPase, similar to the human Na(+)/K(+)-ATPase alpha subunits 1-4; This subfamily includes the alpha subunit of Na(+)/K(+)-ATPase a heteromeric transmembrane protein composed of an alpha- and beta-subunit and an optional third subunit belonging to the FXYD proteins which are more tissue specific regulatory subunits of the enzyme. The alpha-subunit is the catalytic subunit responsible for transport activities of the enzyme. This subfamily includes all four isotopes of the human alpha subunit: (alpha1-alpha4, encoded by the ATP1A1- ATP1A4 genes). Na(+)/K(+)-ATPase functions chiefly as an ion pump, hydrolyzing one molecule of ATP to pump three Na(+) out of the cell in exchange for two K(+)entering the cell per pump cycle. In addition Na(+)/K(+)-ATPase acts as a signal transducer. This subfamily also includes Oreochromis mossambicus (tilapia) Na(+)/K(+)-ATPase alpha 1 and alpha 3 subunits, and gastric H(+)/K(+)-ATPase which exchanges hydronium ion with potassium and is responsible for gastric acid secretion. Gastric H(+)/K(+)-ATPase is an alpha,beta-heterodimeric enzyme. 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
                ....*....|....*....|....*....|..
1YMQ_A      210 GDGGNDISMLRHAAIGVAMGQAKEDV-KAAAD 240
Cdd:cd02608 601 GDGVNDSPALKKADIGVAMGIAGSDVsKQAAD 632

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YMQ_A        4 ALFFDIDGTLVSFETH----RIPSSTIEALE--AAHAKGLkIFIATGRPKAIINNLseLQDRNLidGYITMNGAYCFVGE 77
Cdd:cd01627   1 LLFLDYDGTLAPIVPDpdaaVPSPELLEALKklAADPKNA-VAIVSGRDLDDLDKW--LGLPGI--GLAGEHGAEIRLPG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1YMQ_A       78 EVIYKSAIP------QEEVK-AMAAFCEkkGVPCIFVEEHNISVC 115
Cdd:cd01627  76 GGEWVTLAPkadlewKEEVEaIFKYFTE--RTPGSLVEDKGASLA 118

golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. 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
                ....*....|....*....|....*....|....
1YMQ_A      210 GDGGNDISMLRHAAIGVAMGQAKEDV-KAAADYV 242
Cdd:cd02085 551 GDGVNDAVALKSADIGIAMGRTGTDVcKEAADMI 584

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
                  ....*....|....*....|....*....|....*....|....*....
1YMQ_A        194 EIIRHFGIKLEETMSFGDGGNDISMLRHAAIGVAMGQAKEdVKAAADYV 242
Cdd:TIGR01494 439 AIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMGSGDV-AKAAADIV 486

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. 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
                ....*....|....*....|....*....|....*
1YMQ_A      210 GDGGNDISMLRHAAIGVAMGQAKEDVKAAADYVTA 244
Cdd:cd02083 692 GDGVNDAPALKKAEIGIAMGSGTAVAKSASDMVLA 726

sodium or proton efflux -- potassium uptake antiporter, P-type ATPase, alpha subunit; This model describes the P-type ATPases responsible for the exchange of either protons or sodium ions for potassium ions across the plasma membranes of eukaryotes. Unlike most other P-type ATPases, members of this subfamily require a beta subunit for activity. This model encompasses eukaryotes and consists of two functional types, a Na/K antiporter found widely distributed in eukaryotes and a H/K antiporter found only in vertebrates. The Na+ or H+/K+ antiporter P-type ATPases have been characterized as Type IIC based on a published phylogenetic analysis. Sequences from Blastocladiella emersonii (GP|6636502, GP|6636502 and PIR|T43025), C. elegans (GP|2315419, GP|6671808 and PIR|T31763) and Drosophila melanogaster (GP|7291424) score below trusted cutoff, apparently due to long branch length (excessive divergence from the last common ancestor) as evidenced by a phylogenetic tree. Experimental evidence is needed to determine whether these sequences represent ATPases with conserved function. Aside from fragments, other sequences between trusted and noise appear to be bacterial ATPases of unclear lineage, but most likely calcium pumps. [Energy metabolism, ATP-proton motive force interconversion]

                          10        20        30
                  ....*....|....*....|....*....|....
1YMQ_A        210 GDGGNDISMLRHAAIGVAMGQAKEDV-KAAADYV 242
Cdd:TIGR01106 690 GDGVNDSPALKKADIGVAMGIAGSDVsKQAADMI 723

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
                ....*....|....*....|....*....|....*....|....*....|..
1YMQ_A      178 FADVTAKGDTKQKGIDEIIRHFGIKLEETMSFGDGGNDISMLRHA-AIGVAM 228
Cdd:cd01427  55 GSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAgGRTVAV 106

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