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Conserved domains on  [gi|15234236|ref|NP_192894|]
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Haloacid dehalogenase-like hydrolase (HAD) superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 1-373 0e+00

haloacid dehalogenase-like hydrolase


:

Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 709.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236    1 MAEAIGAVSLVGHRPSIVRITVKNELKTQKSQSIVRFPVKVDYSAKGVLSHLMTQSVKKNRMSVFPIRALAMELTKEK-- 78
Cdd:PLN02575   1 MADSIAATSLVGHRPLCGRLSVKDESYRRKSQSSCRFPVKEFVGRRLVASSPMLQRVKKDRLVVTSIKALAMELTKEAys 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   79 -KKDDRLPKTWNY-LDSGADDKPSLWPPENKADKPSLHNPLLRQERMGCGWLGAIFEWEGVLIEDNPDLDNQSWLTLAQE 156
Cdd:PLN02575  81 yREEERIPRTWNYrLDTGADRKPGLWPPENRADNPSLHNPLLRQERMGCGWLGAIFEWEGVIIEDNPDLENQAWLTLAQE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  157 EGKSPPPAFMLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKALHGGVYRLRDGSQEFVNVLMNNKIPMALVST 236
Cdd:PLN02575 161 EGKSPPPAFILRRVEGMKNEQAISEVLCWSRDPAELRRMATRKEEIYQALQGGIYRLRTGSQEFVNVLMNYKIPMALVST 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  237 RPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVASKHP 316
Cdd:PLN02575 241 RPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDARMKCVAVASKHP 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  317 IYELGAAELVVRRLDELSIIDLKKLADTDLTEF---EPELEMEKEDERELPSSAVAVDDF 373
Cdd:PLN02575 321 IYELGAADLVVRRLDELSIVDLKNLADIESPEFgppEPELEMEKEEDRELPSSAGVDDIF 380
 
Name Accession Description Interval E-value
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 1-373 0e+00

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 709.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236    1 MAEAIGAVSLVGHRPSIVRITVKNELKTQKSQSIVRFPVKVDYSAKGVLSHLMTQSVKKNRMSVFPIRALAMELTKEK-- 78
Cdd:PLN02575   1 MADSIAATSLVGHRPLCGRLSVKDESYRRKSQSSCRFPVKEFVGRRLVASSPMLQRVKKDRLVVTSIKALAMELTKEAys 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   79 -KKDDRLPKTWNY-LDSGADDKPSLWPPENKADKPSLHNPLLRQERMGCGWLGAIFEWEGVLIEDNPDLDNQSWLTLAQE 156
Cdd:PLN02575  81 yREEERIPRTWNYrLDTGADRKPGLWPPENRADNPSLHNPLLRQERMGCGWLGAIFEWEGVIIEDNPDLENQAWLTLAQE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  157 EGKSPPPAFMLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKALHGGVYRLRDGSQEFVNVLMNNKIPMALVST 236
Cdd:PLN02575 161 EGKSPPPAFILRRVEGMKNEQAISEVLCWSRDPAELRRMATRKEEIYQALQGGIYRLRTGSQEFVNVLMNYKIPMALVST 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  237 RPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVASKHP 316
Cdd:PLN02575 241 RPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDARMKCVAVASKHP 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  317 IYELGAAELVVRRLDELSIIDLKKLADTDLTEF---EPELEMEKEDERELPSSAVAVDDF 373
Cdd:PLN02575 321 IYELGAADLVVRRLDELSIVDLKNLADIESPEFgppEPELEMEKEEDRELPSSAGVDDIF 380
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
129-333 3.36e-44

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 151.52  E-value: 3.36e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 129 GAIFEWEGVLIEDNPdLDNQSWLTLAQEEGKSPPPAFmLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKAL-- 206
Cdd:COG0637   4 AVIFDMDGTLVDSEP-LHARAWREAFAELGIDLTEEE-YRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELla 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 207 HGGVyRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPE 286
Cdd:COG0637  82 EEGL-PLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15234236 287 RCIVFGNSNQTIEAAHDGRMKCVAVASKHPI-YELGAAELVVRRLDEL 333
Cdd:COG0637 161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAeEELAGADLVVDDLAEL 208
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 191-313 9.93e-38

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family 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. It 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.


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 132.74  E-value: 9.93e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 191 QVRRMAKRKEEIFKALH-GGVYRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGI-RKFFSVIVASEDVYRGK 268
Cdd:cd07505  19 QAWQLLERKNALLLELIaSEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDDVERGK 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15234236 269 PDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVAS 313
Cdd:cd07505  99 PAPDIYLLAAERLGVDPERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 129-311 1.29e-25

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 101.65  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   129 GAIFEWEGVLIeDNPDLDNQSWLTLAQEEGKSpppaF---MLRRVEGMKNE---QAISEVLCWSRDPVQVRRMAKRKEEI 202
Cdd:TIGR02009   3 AVIFDMDGVIT-DTAPLHAQAWKHIAAKYGIS----FdkqYNESLKGLSREdilRAILKLRGDGLSLEEIHQLAERKNEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   203 FKAL--HGGVYRLrDGSQEFVNVLMNNKIPMALVSTRpretlENA---VGSIGIRKFFSVIVASEDVYRGKPDPEMFIYA 277
Cdd:TIGR02009  78 YRELlrLTGVAVL-PGIRNLLKRLKAKGIAVGLGSSS-----KNApriLAKLGLRDYFDAIVDASEVKNGKPHPETFLLA 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 15234236   278 AQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAV 311
Cdd:TIGR02009 152 AELLGVPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
131-311 2.18e-20

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 87.25  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   131 IFEWEGVLIeDNPDLDNQSWLTLAQEEGKSPPPAFMLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKALHggv 210
Cdd:pfam13419   2 IFDFDGTLL-DTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKL--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   211 YRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIV 290
Cdd:pfam13419  78 VKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIY 157

                         170       180
                  ....*....|....*....|.
gi 15234236   291 FGNSNQTIEAAHDGRMKCVAV 311
Cdd:pfam13419 158 VGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 1-373 0e+00

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 709.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236    1 MAEAIGAVSLVGHRPSIVRITVKNELKTQKSQSIVRFPVKVDYSAKGVLSHLMTQSVKKNRMSVFPIRALAMELTKEK-- 78
Cdd:PLN02575   1 MADSIAATSLVGHRPLCGRLSVKDESYRRKSQSSCRFPVKEFVGRRLVASSPMLQRVKKDRLVVTSIKALAMELTKEAys 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   79 -KKDDRLPKTWNY-LDSGADDKPSLWPPENKADKPSLHNPLLRQERMGCGWLGAIFEWEGVLIEDNPDLDNQSWLTLAQE 156
Cdd:PLN02575  81 yREEERIPRTWNYrLDTGADRKPGLWPPENRADNPSLHNPLLRQERMGCGWLGAIFEWEGVIIEDNPDLENQAWLTLAQE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  157 EGKSPPPAFMLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKALHGGVYRLRDGSQEFVNVLMNNKIPMALVST 236
Cdd:PLN02575 161 EGKSPPPAFILRRVEGMKNEQAISEVLCWSRDPAELRRMATRKEEIYQALQGGIYRLRTGSQEFVNVLMNYKIPMALVST 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  237 RPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVASKHP 316
Cdd:PLN02575 241 RPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDARMKCVAVASKHP 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  317 IYELGAAELVVRRLDELSIIDLKKLADTDLTEF---EPELEMEKEDERELPSSAVAVDDF 373
Cdd:PLN02575 321 IYELGAADLVVRRLDELSIVDLKNLADIESPEFgppEPELEMEKEEDRELPSSAGVDDIF 380
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 104-360 9.85e-145

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 410.58  E-value: 9.85e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  104 PENKADKPSLHNPLLRQERMGCGWLGAIFEWEGVLIEDNPDLDNQSWLTLAQEEGKSPPPAFMLRRVEGMKNEQAISEVL 183
Cdd:PLN03243   1 PRDRADDLSLNNPLLRQHRLGCGWLGVVLEWEGVIVEDDSELERKAWRALAEEEGKRPPPAFLLKRAEGMKNEQAISEVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  184 CWSRDPVQVRRMAKRKEEIFKALHGGVYRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASED 263
Cdd:PLN03243  81 CWSRDFLQMKRLAIRKEDLYEYMQGGLYRLRPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  264 VYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVASKHPIYELGAAELVVRRLDELSIIDLKKLAD 343
Cdd:PLN03243 161 VYRGKPDPEMFMYAAERLGFIPERCIVFGNSNSSVEAAHDGCMKCVAVAGKHPVYELSAGDLVVRRLDDLSVVDLKNLSD 240

                        250       260
                 ....*....|....*....|
gi 15234236  344 TDLTEF---EPELEMEKEDE 360
Cdd:PLN03243 241 LDSPEFqipEPQLEEEVEEE 260
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
129-333 3.36e-44

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 151.52  E-value: 3.36e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 129 GAIFEWEGVLIEDNPdLDNQSWLTLAQEEGKSPPPAFmLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKAL-- 206
Cdd:COG0637   4 AVIFDMDGTLVDSEP-LHARAWREAFAELGIDLTEEE-YRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELla 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 207 HGGVyRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPE 286
Cdd:COG0637  82 EEGL-PLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15234236 287 RCIVFGNSNQTIEAAHDGRMKCVAVASKHPI-YELGAAELVVRRLDEL 333
Cdd:COG0637 161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAeEELAGADLVVDDLAEL 208
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 191-313 9.93e-38

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family 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. It 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.


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 132.74  E-value: 9.93e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 191 QVRRMAKRKEEIFKALH-GGVYRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGI-RKFFSVIVASEDVYRGK 268
Cdd:cd07505  19 QAWQLLERKNALLLELIaSEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDDVERGK 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15234236 269 PDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVAS 313
Cdd:cd07505  99 PAPDIYLLAAERLGVDPERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
131-333 4.70e-29

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 111.94  E-value: 4.70e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 131 IFEWEGVLIEDNPDLDNqSWLTLAQEEGKSPPPAFMLRRVEGMKNEQAIsEVLCWSRDPVQVRRMAKRKEEIFKALHGGV 210
Cdd:COG0546   5 LFDLDGTLVDSAPDIAA-ALNEALAELGLPPLDLEELRALIGLGLRELL-RRLLGEDPDEELEELLARFRELYEEELLDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 211 YRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIV 290
Cdd:COG0546  83 TRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLM 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15234236 291 FGNSNQTIEAAHDGRMKCVAVA----SKHPIYELGaAELVVRRLDEL 333
Cdd:COG0546 163 VGDSPHDIEAARAAGVPFIGVTwgygSAEELEAAG-ADYVIDSLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 129-311 1.29e-25

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 101.65  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   129 GAIFEWEGVLIeDNPDLDNQSWLTLAQEEGKSpppaF---MLRRVEGMKNE---QAISEVLCWSRDPVQVRRMAKRKEEI 202
Cdd:TIGR02009   3 AVIFDMDGVIT-DTAPLHAQAWKHIAAKYGIS----FdkqYNESLKGLSREdilRAILKLRGDGLSLEEIHQLAERKNEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   203 FKAL--HGGVYRLrDGSQEFVNVLMNNKIPMALVSTRpretlENA---VGSIGIRKFFSVIVASEDVYRGKPDPEMFIYA 277
Cdd:TIGR02009  78 YRELlrLTGVAVL-PGIRNLLKRLKAKGIAVGLGSSS-----KNApriLAKLGLRDYFDAIVDASEVKNGKPHPETFLLA 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 15234236   278 AQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAV 311
Cdd:TIGR02009 152 AELLGVPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 195-314 3.98e-23

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.


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 94.63  E-value: 3.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 195 MAKRKEEIFKALHGGVY--RLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPE 272
Cdd:cd16423  25 LNERRNELIKRQFSEKTdlPPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPD 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15234236 273 MFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVASK 314
Cdd:cd16423 105 LYLEAAERLGVNPEECVVIEDSRNGVLAAKAAGMKCVGVPNP 146
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
131-311 2.18e-20

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 87.25  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   131 IFEWEGVLIeDNPDLDNQSWLTLAQEEGKSPPPAFMLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKALHggv 210
Cdd:pfam13419   2 IFDFDGTLL-DTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKL--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   211 YRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIV 290
Cdd:pfam13419  78 VKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIY 157

                         170       180
                  ....*....|....*....|.
gi 15234236   291 FGNSNQTIEAAHDGRMKCVAV 311
Cdd:pfam13419 158 VGDSPRDIEAAKNAGIKVIAV 178
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 129-335 1.81e-18

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong 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), 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.


Pssm-ID: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 82.78  E-value: 1.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 129 GAIFEWEGVLIEDNPDLDnQSWLTLAQEEGksPPPAFMLRRVEGMkneQAISEVLCWSRDPVQVRRMAKRKEEIFKALHG 208
Cdd:cd07527   1 ALLFDMDGTLVDSTPAVE-RAWHKWAKEHG--VDPEEVLKVSHGR---RAIDVIRKLAPDDADIELVLALETEEPESYPE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 209 GVYRLrDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFfSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERC 288
Cdd:cd07527  75 GVIAI-PGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGLPHP-EVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDC 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15234236 289 IVFGNSNQTIEAAHDGRMKCVAVASKH--PIYELGAAELVVRRLDELSI 335
Cdd:cd07527 153 VVFEDAPAGIKAGKAAGARVVAVNTSHdlEQLEAAGADLVVEDLSDISV 201
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 129-311 7.87e-17

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 77.73  E-value: 7.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   129 GAIFEWEGVlIEDNPDLDNQSWLTLAQEEGKSPPPAF--MLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKAL 206
Cdd:TIGR01990   1 AVIFDLDGV-ITDTAEYHYLAWKHLADELGIPFDEEFneSLKGVSREESLERILDLGGKKYSEEEKEELAERKNDYYVEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   207 HGGVYR--LRDGSQEFVNVLMNNKIPMAL--VSTRPRETLENavgsIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLD 282
Cdd:TIGR01990  80 LKELTPadVLPGIKSLLADLKKNNIKIALasASKNAPTILEK----LELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLG 155

                         170       180
                  ....*....|....*....|....*....
gi 15234236   283 FIPERCIVFGNSNQTIEAAHDGRMKCVAV 311
Cdd:TIGR01990 156 VSPSECIGIEDAQAGIEAIKAAGMFAVGV 184
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 131-311 3.36e-16

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; 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, (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 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the 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 related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 75.92  E-value: 3.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   131 IFEWEGVLI---EDNPDLDNQSWLTLAQEEgkspppafmlrrvegMKNEQAISEVLCWSRDPVQV-RRMAKRKEEIFKA- 205
Cdd:TIGR01509   3 LFDLDGVLVdteFAIAKLINREELGLVPDE---------------LGVSAVGRLELALRRFKAQYgRTISPEDAQLLYKq 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   206 ------LHGGVYRLRDGSQEFVNVLMNNKIPMALVSTRPReTLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQ 279
Cdd:TIGR01509  68 lfyeqiEEEAKLKPLPGVRALLEALRARGKKLALLTNSPR-AHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALK 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 15234236   280 LLDFIPERCIVFGNSNQTIEAAHDGRMKCVAV 311
Cdd:TIGR01509 147 ALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 194-341 6.75e-15

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include 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.


Pssm-ID: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 71.94  E-value: 6.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 194 RMAKRKEEIFKAL--HGGVYRLRDGSQEFVNVLMNNKIPMAL--VSTRPRETLEnavgSIGIRKFFSVIVASEDVYRGKP 269
Cdd:cd02598  29 ELAARKNRIYVELieELTPVDVLPGIASLLVDLKAKGIKIALasASKNAPKILE----KLGLAEYFDAIVDGAVLAKGKP 104

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234236 270 DPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVASkhPIYELGAAELVVRRLDELSIIDLKKL 341
Cdd:cd02598 105 DPDIFLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAGFLVVGVGR--EEDLLGADIVVPDTTADLTIEELLEV 174
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 211-301 2.16e-14

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.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 71.08  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   211 YRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIV 290
Cdd:pfam00702  97 LKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLM 176

                          90
                  ....*....|.
gi 15234236   291 FGNSNQTIEAA 301
Cdd:pfam00702 177 VGDGVNDIPAA 187
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 200-333 5.65e-14

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


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 70.44  E-value: 5.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 200 EEIFKALHGGVyRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQ 279
Cdd:COG1011  82 EAFLAALPELV-EPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALE 160

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15234236 280 LLDFIPERCIVFGNSNQT-IEAAHD-GrMKCVAVASKHPIYELGA-AELVVRRLDEL 333
Cdd:COG1011 161 RLGVPPEEALFVGDSPETdVAGARAaG-MRTVWVNRSGEPAPAEPrPDYVISDLAEL 216
PLN02940 PLN02940
riboflavin kinase
 216-313 9.87e-14

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 71.79  E-value: 9.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  216 GSQEFVNVLMNNKIPMALVSTRPRETLENAVG-SIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNS 294
Cdd:PLN02940  97 GANRLIKHLKSHGVPMALASNSPRANIEAKIScHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSNCLVIEDS 176

                         90
                 ....*....|....*....
gi 15234236  295 NQTIEAAHDGRMKCVAVAS 313
Cdd:PLN02940 177 LPGVMAGKAAGMEVIAVPS 195
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 218-311 1.51e-13

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.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 66.27  E-value: 1.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 218 QEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQT 297
Cdd:cd01427  13 VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEND 92

                        90
                ....*....|....
gi 15234236 298 IEAAHDGRMKCVAV 311
Cdd:cd01427  93 IEAARAAGGRTVAV 106
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 188-312 3.71e-13

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 67.75  E-value: 3.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  188 DPVQVRRMAKRKEEIFKALHGGVYRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRG 267
Cdd:PRK13288  58 DESKVEEMITTYREFNHEHHDELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHA 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15234236  268 KPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVA 312
Cdd:PRK13288 138 KPDPEPVLKALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVA 182
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 130-333 7.90e-13

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.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 66.65  E-value: 7.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 130 AIFEWEGVLIednpdlDNQSWLTLAQEE-----GKSPPPAFMLRRVEGMKNEQAISEVLCWSrdPVQVRRMAKRKEEIF- 203
Cdd:cd07533   2 VIFDWDGTLA------DSQHNIVAAMTAafadlGLPVPSAAEVRSIIGLSLDEAIARLLPMA--TPALVAVAERYKEAFd 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 204 --KALHGGVYRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFsVIVASEDVYRGKPDPEMFIYAAQLL 281
Cdd:cd07533  74 ilRLLPEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYF-DATRTADDTPSKPHPEMLREILAEL 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15234236 282 DFIPERCIVFGNSNQTIEAAHDGRMKCVAVA-SKHPIYEL--GAAELVVRRLDEL 333
Cdd:cd07533 153 GVDPSRAVMVGDTAYDMQMAANAGAHAVGVAwGYHSLEDLrsAGADAVVDHFSEL 207
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
230-311 1.82e-12

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 65.48  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  230 PMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCV 309
Cdd:PRK10725 104 PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAV 183


                 ..
gi 15234236  310 AV 311
Cdd:PRK10725 184 DV 185
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 180-308 2.42e-12

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. 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. 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.


Pssm-ID: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 63.88  E-value: 2.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 180 SEVLCwsrDPVQVRRMAKRKEEIFKALHGGVyRLRDGSQEFVNVLmnnKIPMALVSTRPRETLENAVGSIGIRKFF-SVI 258
Cdd:cd07526  14 SEVIA---ARVLVEVLAELGARVLAAFEAEL-QPIPGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFeGRI 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15234236 259 VASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKC 308
Cdd:cd07526  87 FSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIEDSPTGVRAALAAGMTV 136
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 229-333 4.77e-11

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.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 61.53  E-value: 4.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 229 IPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKC 308
Cdd:cd02616  97 IKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGVKT 176

                        90       100
                ....*....|....*....|....*...
gi 15234236 309 VAVA-SKHPIYELGAAE--LVVRRLDEL 333
Cdd:cd02616 177 VGVTwGYKGREYLKAFNpdFIIDKMSDL 204
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 197-309 2.96e-10

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. 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.


Pssm-ID: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 59.32  E-value: 2.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 197 KRKEEIFKALHG-GVYRLRDGSQEFVNVLMNNKIPMALVSTRPRET----LENAvgsIGIRKF--FSVIVASEDVYRGKP 269
Cdd:cd07528  79 KAKTERYAELIAaGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANvdalLSAL---LGPERRaiFDAIAAGDDVAEKKP 155

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15234236 270 DPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCV 309
Cdd:cd07528 156 DPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
229-333 3.20e-10

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 59.44  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  229 IPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKC 308
Cdd:PRK13222 110 YPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPS 189

                         90       100
                 ....*....|....*....|....*....
gi 15234236  309 VAV----ASKHPIYELGaAELVVRRLDEL 333
Cdd:PRK13222 190 VGVtygyNYGEPIALSE-PDVVIDHFAEL 217
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 131-333 4.65e-10

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.


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 58.79  E-value: 4.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 131 IFEWEGVLIEDNPDLDNQSWLTLaQEEGKSPPPAFMLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKAL---H 207
Cdd:cd16417   3 AFDLDGTLVDSAPDLAEAANAML-AALGLPPLPEETVRTWIGNGADVLVERALTGAREAEPDEELFKEARALFDRHyaeT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 208 GGVY-RLRDGSQEFVNVLMNNKIPMALVSTRPR----ETLEnavgSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLD 282
Cdd:cd16417  82 LSVHsHLYPGVKEGLAALKAQGYPLACVTNKPErfvaPLLE----ALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15234236 283 FIPERCIVFGNSNQTIEAAHDGRMKCVAV----ASKHPIYELGaAELVVRRLDEL 333
Cdd:cd16417 158 IAPAQMLMVGDSRNDILAARAAGCPSVGLtygyNYGEDIAASG-PDAVIDSLAEL 211
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 131-311 4.05e-09

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. 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.


Pssm-ID: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 55.82  E-value: 4.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 131 IFEWEGVLIednpdlDNQSWLTLAQEE-----GKSPPPAfMLRRVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKA 205
Cdd:cd07529   5 IFDMDGLLL------DTERIYTETTQEilaryGKTYTWD-VKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 206 LHGGVYRLRDGSQEFVNVLMNNKIPMAL-VSTRPRETLENAVGSIGIRKFFSVIVASED---VYRGKPDPEMFIYAAQLL 281
Cdd:cd07529  78 LFMGTAKLMPGAERLLRHLHAHNIPIALaTSSCTRHFKLKTSRHKELFSLFHHVVTGDDpevKGRGKPAPDIFLVAAKRF 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 15234236 282 D---FIPERCIVFGNSNQTIEAAHDGRMKCVAV 311
Cdd:cd07529 158 NeppKDPSKCLVFEDSPNGVKAAKAAGMQVVMV 190
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 217-333 4.55e-09

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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.


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 54.22  E-value: 4.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 217 SQEFVNVLMNNKIPMALVS---TRPRETLENavgsIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGN 293
Cdd:cd16415  12 AVETLKDLKEKGLKLAVVSnfdRRLRELLEA----LGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGD 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15234236 294 SNQT-IEAAHDGRMKCVAVASKHPIYELGAAELVVRRLDEL 333
Cdd:cd16415  88 DLKNdYLGARAVGWHALLVDREGALHELPSLANLLERLLEL 128
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 218-309 5.04e-09

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.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 53.31  E-value: 5.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 218 QEFVNVLMN--NKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSN 295
Cdd:cd04305  12 PGAKELLEElkKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDSL 91

                        90
                ....*....|....*
gi 15234236 296 QT-IEAAHDGRMKCV 309
Cdd:cd04305  92 ESdILGAKNAGIKTV 106
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 131-301 7.28e-09

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]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 54.32  E-value: 7.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   131 IFEWEGVLIeDNPDLDNQSWLTLAQEEGKSPPPafmlrrVEGMKNEQAISEVLCWSRDPVQVRRMAKRKEEIFKALHGgv 210
Cdd:TIGR01549   3 LFDIDGTLV-DIKFAIRRAFPQTFEEFGLDPAS------FKALKQAGGLAEEEWYRIATSALEELQGRFWSEYDAEEA-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   211 yrLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRgKPDPEMFIYAAQLLDfIPERCIV 290
Cdd:TIGR01549  74 --YIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGS-KPEPEIFLAALESLG-VPPEVLH 149

                         170
                  ....*....|.
gi 15234236   291 FGNSNQTIEAA 301
Cdd:TIGR01549 150 VGDNLNDIEGA 160
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 192-309 3.55e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 54.33  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  192 VRRMAKRKEEIFKAL-HGGVYRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSV--IVASEDVYRGK 268
Cdd:PLN02779 123 VDSLHDRKTELFKELiESGALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVNTLLGPERAQGldVFAGDDVPKKK 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15234236  269 PDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCV 309
Cdd:PLN02779 203 PDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCI 243
Hydrolase_like pfam13242
HAD-hyrolase-like;
266-333 4.33e-07

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 46.84  E-value: 4.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234236   266 RGKPDPEMFIYAAQLLDFIPERCIVFGNSNQT-IEAAHDGRMKCVAVAS-KHPIYELGAAE----LVVRRLDEL 333
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDTdILGAREAGARTILVLTgVTRPADLEKAPirpdYVVDDLAEA 75
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 132-294 6.93e-07

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 49.69  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  132 FEWEGVLIeDNPDLDNQSWLTLAQEEGKSPPPAFMLRRVEGMKNEQAISEVLcwSRDPVQVRrmakrKEEIFKALHGGVY 211
Cdd:PRK10563   9 FDCDGTLV-DSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIIS--KEHGVTLA-----KAELEPVYRAEVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  212 RLRDGSQEF---VNVLMNN-KIPMALVSTRPRETLENAVGSIGIRKFFS-VIVASEDVYRGKPDPEMFIYAAQLLDFIPE 286
Cdd:PRK10563  81 RLFDSELEPiagANALLESiTVPMCVVSNGPVSKMQHSLGKTGMLHYFPdKLFSGYDIQRWKPDPALMFHAAEAMNVNVE 160


                 ....*...
gi 15234236  287 RCIVFGNS 294
Cdd:PRK10563 161 NCILVDDS 168
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 216-343 1.27e-06

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 50.62  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   216 GSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGI-RKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNS 294
Cdd:PLN02919  165 GALELITQCKNKGLKVAVASSADRIKVDANLAAAGLpLSMFDAIVSADAFENLKPAPDIFLAAAKILGVPTSECVVIEDA 244

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15234236   295 NQTIEAAHDGRMKCVAVASKHPIYELGAA--ELVVRRLDELSIIDLKKLAD 343
Cdd:PLN02919  245 LAGVQAARAAGMRCIAVTTTLSEEILKDAgpSLIRKDIGNISLSDILTGGS 295
PRK11587 PRK11587
putative phosphatase; Provisional
 216-335 2.11e-06

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 48.07  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  216 GSQEFVNVLMNNKIPMALVS--TRPRETLENAVGSIGIRKFFsviVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGN 293
Cdd:PRK11587  87 GAIALLNHLNKLGIPWAIVTsgSVPVASARHKAAGLPAPEVF---VTAERVKRGKPEPDAYLLGAQLLGLAPQECVVVED 163

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15234236  294 SNQTIEAAHDGRMKCVAVASKHPIYELGAAELVVRRLDELSI 335
Cdd:PRK11587 164 APAGVLSGLAAGCHVIAVNAPADTPRLDEVDLVLHSLEQLTV 205
PRK10826 PRK10826
hexitol phosphatase HxpB;
233-315 4.90e-06

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 47.25  E-value: 4.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  233 LVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVA 312
Cdd:PRK10826 113 LASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVP 192


                 ...
gi 15234236  313 SKH 315
Cdd:PRK10826 193 APE 195
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 224-333 5.48e-06

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.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 46.88  E-value: 5.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 224 LMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHD 303
Cdd:cd02588 103 LREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASHAWDLAGARA 182

                        90       100       110
                ....*....|....*....|....*....|..
gi 15234236 304 GRMKCVAVA--SKHPIYELGAAELVVRRLDEL 333
Cdd:cd02588 183 LGLRTAWINrpGEVPDPLGPAPDFVVPDLGEL 214
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 129-334 7.97e-06

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.


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 46.54  E-value: 7.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 129 GAIFEWEGVLIEDNPDLDNQSWLTLAQEEGKSPPPAfmlrRVEGMKNEQAisevlcwsrdPVQVRR-MAKRKEEIFKALH 207
Cdd:cd07512   1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLA----EVRSFVGHGA----------PALIRRaFAAAGEDLDGPLH 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 208 GGVY---------------RLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPE 272
Cdd:cd07512  67 DALLarfldhyeadppgltRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPA 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234236 273 MFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVA---SKHPIYELGAAeLVVRRLDELS 334
Cdd:cd07512 147 PLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTfgyRHAPVAELPHD-AVFSDFDALP 210
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 130-301 1.59e-05

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.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 45.03  E-value: 1.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 130 AIFEWEGVLIEDNPDLDNQSWLTLAQEegkspPPAFMLRRV-------EGMKNEQAISEVLCwsrdpvQVRRMAKRK--E 200
Cdd:cd02603   4 VLFDFGGVLIDPDPAAAVARFEALTGE-----PSEFVLDTEglagaflELERGRITEEEFWE------ELREELGRPlsA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 201 EIFKALHGGVYRLRDGSQEFVNVLMNNKIPMALVS-TRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAAQ 279
Cdd:cd02603  73 ELFEELVLAAVDPNPEMLDLLEALRAKGYKVYLLSnTWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALE 152

                       170       180
                ....*....|....*....|..
gi 15234236 280 LLDFIPERCIVFGNSNQTIEAA 301
Cdd:cd02603 153 RLGVKPEEVLFIDDREENVEAA 174
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 229-311 2.31e-05

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.


Pssm-ID: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 42.83  E-value: 2.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236 229 IPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRgKPDPEMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKC 308
Cdd:cd16421  24 IKLAVLSNKPNEAVQVLVEELFPGSFDFVLGEKEGIRR-KPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQTARNAGMDE 102


                ...
gi 15234236 309 VAV 311
Cdd:cd16421 103 IGV 105
PLN02811 PLN02811
hydrolase
 216-311 1.10e-04

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 42.82  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  216 GSQEFVNVLMNNKIPMALVSTRPRETLEnaVGSIGIRKFFSV---IVASED--VYRGKPDPEMFIYAA---QLLDFIPER 287
Cdd:PLN02811  82 GAERLVRHLHAKGIPIAIATGSHKRHFD--LKTQRHGELFSLmhhVVTGDDpeVKQGKPAPDIFLAAArrfEDGPVDPGK 159

                         90       100
                 ....*....|....*....|....
gi 15234236  288 CIVFGNSNQTIEAAHDGRMKCVAV 311
Cdd:PLN02811 160 VLVFEDAPSGVEAAKNAGMSVVMV 183
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 131-312 1.36e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 43.31  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  131 IFEWEGVLIEDNPDLDNQSWLTLAqEEGKspPPAfmlrrvegmkneqAISEVLCWSRD--PVQVRR-------------- 194
Cdd:PRK13223  17 MFDLDGTLVDSVPDLAAAVDRMLL-ELGR--PPA-------------GLEAVRHWVGNgaPVLVRRalagsidhdgvdde 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  195 MAKRKEEIFKALHGGVYRLR---DGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDP 271
Cdd:PRK13223  81 LAEQALALFMEAYADSHELTvvyPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDP 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15234236  272 EMFIYAAQLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVA 312
Cdd:PRK13223 161 AALLFVMKMAGVPPSQSLFVGDSRSDVLAAKAAGVQCVALS 201
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 199-316 2.66e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 42.13  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236  199 KEEIFKALHGGVYRLRDGSQEFVNVLMNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYAA 278
Cdd:PLN02770  95 KEALFRKLASEQLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKAL 174

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15234236  279 QLLDFIPERCIVFGNSNQTIEAAHDGRMKCVAVASKHP 316
Cdd:PLN02770 175 EVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRNP 212
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 212-294 3.92e-04

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 41.32  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234236   212 RLRDGSQEFVNVLmNNKIPMALVSTRPRETLENAVGSIGIRKFFSVIVASEDVYRGKPDPEMFIYA-AQLLDFIPERCIV 290
Cdd:TIGR02254  97 QLLPGAFELMENL-QQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFNYAlERMPKFSKEEVLM 175


                  ....
gi 15234236   291 FGNS 294
Cdd:TIGR02254 176 IGDS 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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