NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16131583|ref|NP_418171|]
View 

6-phosphogluconate phosphatase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

6-phosphogluconate phosphatase( domain architecture ID 10793419)

6-phosphogluconate phosphatase catalyzes strongly the dephosphorylation of 6-phosphogluconate (6P-Glu) and slightly the dephosphorylation of dihydroxyacetone phosphate (DHAP) and phosphoenolpyruvate (PEP); also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 1-221 1.73e-180

6-phosphogluconate phosphatase; Provisional


:

Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 492.67  E-value: 1.73e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    1 MSRIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHVYRAEVA 80
Cdd:PRK10563   1 MSQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   81 RLFDSELEAIEGAGALLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMFHAAKAMNVNVE 160
Cdd:PRK10563  81 RLFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131583  161 NCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQLPELWKARGWDITA 221
Cdd:PRK10563 161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
 
Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 1-221 1.73e-180

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 492.67  E-value: 1.73e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    1 MSRIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHVYRAEVA 80
Cdd:PRK10563   1 MSQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   81 RLFDSELEAIEGAGALLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMFHAAKAMNVNVE 160
Cdd:PRK10563  81 RLFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131583  161 NCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQLPELWKARGWDITA 221
Cdd:PRK10563 161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 5-187 3.97e-72

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: 215.65  E-value: 3.97e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   5 EAVFFDCDGTLVDSEVICSRAYVTMFQEFGitldpeevfkrfkgvklyeiidivslehgvtlakteaehvyrAEVARLFD 84
Cdd:cd07526   1 DLVIFDCDGVLVDSEVIAARVLVEVLAELG------------------------------------------ARVLAAFE 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  85 SELEAIEGAGALLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCIL 164
Cdd:cd07526  39 AELQPIPGAAAALSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118

                       170       180
                ....*....|....*....|...
gi 16131583 165 VDDSVAGAQSGIDAGMEVFYFCA 187
Cdd:cd07526 119 IEDSPTGVRAALAAGMTVFGFTG 141
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
3-208 6.03e-58

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 181.95  E-value: 6.03e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   3 RIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEvFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHVYRAEVARL 82
Cdd:COG0637   1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEE-YRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  83 FDS-ELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNVN 158
Cdd:COG0637  80 LAEeGLPLIPGVVELLEALKEagiKIAVATSSPRENAEAVLEAAGLLDYF-DVIVTGDDVARGKPDPDIYLLAAERLGVD 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16131583 159 VENCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQL 208
Cdd:COG0637 159 PEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-179 1.60e-19

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: 82.63  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEF-----------GITLDPEEVFKRFKGVKLYEIIDIVSLEHGVTLAKTEAE 72
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHplakaivaaaeDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    73 HVYRAEVARLF--DSELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPAL 147
Cdd:pfam00702  81 TVVLVELLGVIalADELKLYPGAAEALKALKErgiKVAILTGDNPEAAEALLRLLGLDDYF-DVVISGDDVGVGKPKPEI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 16131583   148 MFHAAKAMNVNVENCILVDDSVAGAQSGIDAG 179
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 4-183 2.67e-18

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: 78.92  E-value: 2.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDpEEVFKRFKGVKLYEII--------DIVSLE--HGVTLAKTEAeh 73
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFD-KQYNESLKGLSREDILrailklrgDGLSLEeiHQLAERKNEL-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    74 vyraeVARLFDSELEAIE-GAGALLSAITA---PMCVVSNGPNNKMqhSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMF 149
Cdd:TIGR02009  78 -----YRELLRLTGVAVLpGIRNLLKRLKAkgiAVGLGSSSKNAPR--ILAKLGLRDYF-DAIVDASEVKNGKPHPETFL 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 16131583   150 HAAKAMNVNVENCILVDDSVAGAQSGIDAGMEVF 183
Cdd:TIGR02009 150 LAAELLGVPPNECIVFEDALAGVQAARAAGMFAV 183
 
Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 1-221 1.73e-180

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 492.67  E-value: 1.73e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    1 MSRIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHVYRAEVA 80
Cdd:PRK10563   1 MSQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   81 RLFDSELEAIEGAGALLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMFHAAKAMNVNVE 160
Cdd:PRK10563  81 RLFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131583  161 NCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQLPELWKARGWDITA 221
Cdd:PRK10563 161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 5-187 3.97e-72

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: 215.65  E-value: 3.97e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   5 EAVFFDCDGTLVDSEVICSRAYVTMFQEFGitldpeevfkrfkgvklyeiidivslehgvtlakteaehvyrAEVARLFD 84
Cdd:cd07526   1 DLVIFDCDGVLVDSEVIAARVLVEVLAELG------------------------------------------ARVLAAFE 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  85 SELEAIEGAGALLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCIL 164
Cdd:cd07526  39 AELQPIPGAAAALSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118

                       170       180
                ....*....|....*....|...
gi 16131583 165 VDDSVAGAQSGIDAGMEVFYFCA 187
Cdd:cd07526 119 IEDSPTGVRAALAAGMTVFGFTG 141
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
3-208 6.03e-58

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 181.95  E-value: 6.03e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   3 RIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEvFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHVYRAEVARL 82
Cdd:COG0637   1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEE-YRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  83 FDS-ELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNVN 158
Cdd:COG0637  80 LAEeGLPLIPGVVELLEALKEagiKIAVATSSPRENAEAVLEAAGLLDYF-DVIVTGDDVARGKPDPDIYLLAAERLGVD 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16131583 159 VENCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQL 208
Cdd:COG0637 159 PEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-211 1.76e-31

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: 114.36  E-value: 1.76e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVK-------------LYEIIDIVSLEHGVTLAKTE 70
Cdd:COG1011   1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEyalwrryergeitFAELLRRLLEELGLDLAEEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  71 AEHVYRAevarlFDSELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPAl 147
Cdd:COG1011  81 AEAFLAA-----LPELVEPYPDALELLEALKArgyRLALLTNGSAELQEAKLRRLGLDDLF-DAVVSSEEVGVRKPDPE- 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131583 148 MF-HAAKAMNVNVENCILVDDS----VAGAQsgiDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQLPEL 211
Cdd:COG1011 154 IFeLALERLGVPPEEALFVGDSpetdVAGAR---AAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLEL 219
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
4-180 3.65e-31

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 113.49  E-value: 3.65e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEIIDIVsLEHGVTLAKTEAEHVYRAEVARLF 83
Cdd:COG0546   1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRL-LGEDPDEELEELLARFRELYEEEL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  84 DSELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNVNVE 160
Cdd:COG0546  80 LDETRLFPGVRELLEALKArgiKLAVVTNKPREFAERLLEALGLDDYF-DAIVGGDDVPPAKPKPEPLLEALERLGLDPE 158

                       170       180
                ....*....|....*....|
gi 16131583 161 NCILVDDSVAGAQSGIDAGM 180
Cdd:COG0546 159 EVLMVGDSPHDIEAARAAGV 178
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 6-208 8.04e-21

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: 86.24  E-value: 8.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   6 AVFFDCDGTLVDSEVICSRAYVTMFQEFGItlDPEEVFKRFKGVKLYEIIDIVSLEHgvtlakTEAEHVYRAEvARLFDS 85
Cdd:cd07527   1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGV--DPEEVLKVSHGRRAIDVIRKLAPDD------ADIELVLALE-TEEPES 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  86 ---ELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHyfPDKLFSGYDIQRWKPDPALMFHAAKAMNVNV 159
Cdd:cd07527  72 ypeGVIAIPGAVDLLASLPAagdRWAIVTSGTRALAEARLEAAGLPH--PEVLVTADDVKNGKPDPEPYLLGAKLLGLDP 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16131583 160 ENCILVDDSVAGAQSGIDAGMEVFYFCAdPHNKPIVHPK--VTTFTHLSQL 208
Cdd:cd07527 150 SDCVVFEDAPAGIKAGKAAGARVVAVNT-SHDLEQLEAAgaDLVVEDLSDI 199
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-179 1.60e-19

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: 82.63  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEF-----------GITLDPEEVFKRFKGVKLYEIIDIVSLEHGVTLAKTEAE 72
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHplakaivaaaeDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    73 HVYRAEVARLF--DSELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPAL 147
Cdd:pfam00702  81 TVVLVELLGVIalADELKLYPGAAEALKALKErgiKVAILTGDNPEAAEALLRLLGLDDYF-DVVISGDDVGVGKPKPEI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 16131583   148 MFHAAKAMNVNVENCILVDDSVAGAQSGIDAG 179
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 4-183 2.67e-18

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: 78.92  E-value: 2.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDpEEVFKRFKGVKLYEII--------DIVSLE--HGVTLAKTEAeh 73
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFD-KQYNESLKGLSREDILrailklrgDGLSLEeiHQLAERKNEL-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    74 vyraeVARLFDSELEAIE-GAGALLSAITA---PMCVVSNGPNNKMqhSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMF 149
Cdd:TIGR02009  78 -----YRELLRLTGVAVLpGIRNLLKRLKAkgiAVGLGSSSKNAPR--ILAKLGLRDYF-DAIVDASEVKNGKPHPETFL 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 16131583   150 HAAKAMNVNVENCILVDDSVAGAQSGIDAGMEVF 183
Cdd:TIGR02009 150 LAAELLGVPPNECIVFEDALAGVQAARAAGMFAV 183
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 6-183 9.16e-18

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: 76.50  E-value: 9.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   6 AVFFDCDGTLVDSEVICSRAYVtmfqefgitldpeevfkrfkgvklyeiidivslehgvtlaktEAEHVYRAEVARLFDS 85
Cdd:cd07505   1 AVIFDMDGVLIDTEPLHRQAWQ------------------------------------------LLERKNALLLELIASE 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  86 ELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMFHAAKAMNVNVENC 162
Cdd:cd07505  39 GLKLKPGVVELLDALKAagiPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                       170       180
                ....*....|....*....|.
gi 16131583 163 ILVDDSVAGAQSGIDAGMEVF 183
Cdd:cd07505 119 LVFEDSLAGIEAAKAAGMTVV 139
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 6-182 2.81e-17

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: 76.30  E-value: 2.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     6 AVFFDCDGTLVDSEvicsRAYVTMFQEFGITLDPEEVFKRFKGvKLYEIIDIVSLEHGVTLAKTEAEHVYRAEVARLFDS 85
Cdd:TIGR01509   1 AILFDLDGVLVDTE----FAIAKLINREELGLVPDELGVSAVG-RLELALRRFKAQYGRTISPEDAQLLYKQLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    86 ELEA--IEGAGALLSAITA---PMCVVSNGPNNkMQHSMGKLNMLHYFPDKLFSGyDIQRWKPDPALMFHAAKAMNVNVE 160
Cdd:TIGR01509  76 EAKLkpLPGVRALLEALRArgkKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSS-DVGLGKPDPDIYLQALKALGLEPS 153

                         170       180
                  ....*....|....*....|..
gi 16131583   161 NCILVDDSVAGAQSGIDAGMEV 182
Cdd:TIGR01509 154 ECVFVDDSPAGIEAAKAAGMHT 175
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
7-182 3.28e-17

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 76.08  E-value: 3.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     7 VFFDCDGTLVDSE--VICSRAYVtmFQEFGITLDPEEVFKRFKGVKLYEIIDIVslehGVTLAKTEAEHVYRAEV-ARLF 83
Cdd:pfam13419   1 IIFDFDGTLLDTEelIIKSFNYL--LEEFGYGELSEEEILKFIGLPLREIFRYL----GVSEDEEEKIEFYLRKYnEELH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    84 DSELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNVNVE 160
Cdd:pfam13419  75 DKLVKPYPGIKELLEELKEqgyKLGIVTSKSRENVEEFLKQLGLEDYF-DVIVGGDDVEGKKPDPDPILKALEQLGLKPE 153

                         170       180
                  ....*....|....*....|..
gi 16131583   161 NCILVDDSVAGAQSGIDAGMEV 182
Cdd:pfam13419 154 EVIYVGDSPRDIEAAKNAGIKV 175
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 6-205 3.87e-16

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: 73.06  E-value: 3.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   6 AVFFDCDGTLVDSEVIcsrayvtmfqefgitldpeevfkrfkgvkLYEIIDIVSLEHGVTLAKTEAEHVYraevarlfds 85
Cdd:cd16423   1 AVIFDFDGVIVDTEPL-----------------------------WYEAWQELLNERRNELIKRQFSEKT---------- 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  86 ELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNVNVENC 162
Cdd:cd16423  42 DLPPIEGVKELLEFLKEkgiKLAVASSSPRRWIEPHLERLGLLDYF-EVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16131583 163 ILVDDSVAGAQSGIDAGMEVFYFcADPHNKPIVHPKVTTFTHL 205
Cdd:cd16423 121 VVIEDSRNGVLAAKAAGMKCVGV-PNPVTGSQDFSKADLVLSS 162
PLN02940 PLN02940
riboflavin kinase
 4-182 7.59e-14

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 69.48  E-value: 7.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFkGVKLYEIIDIVSLEHGVTLAKTEaehvYRAEVARLF 83
Cdd:PLN02940  11 VSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIV-GKTPLEAAATVVEDYGLPCSTDE----FNSEITPLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   84 DSE---LEAIEGAGAL---LSAITAPMCVVSNGPNN----KMQHSMGklnMLHYFPdKLFSGYDIQRWKPDPALMFHAAK 153
Cdd:PLN02940  86 SEQwcnIKALPGANRLikhLKSHGVPMALASNSPRAnieaKISCHQG---WKESFS-VIVGGDEVEKGKPSPDIFLEAAK 161

                        170       180
                 ....*....|....*....|....*....
gi 16131583  154 AMNVNVENCILVDDSVAGAQSGIDAGMEV 182
Cdd:PLN02940 162 RLNVEPSNCLVIEDSLPGVMAGKAAGMEV 190
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 5-180 1.57e-13

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 67.81  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    5 EAVFFDCDGTLVDSEVICSR-AYVTMFQEFGIT---LDPE------EV----------FKRfKGVKLYEIIDIVSLEH-- 62
Cdd:PLN02779  41 EALLFDCDGVLVETERDGHRvAFNDAFKEFGLRpveWDVElydellNIgggkermtwyFNE-NGWPTSTIEKAPKDEEer 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   63 -----GVTLAKTE--------AEHVYRAEVARLFDselEAIEGAGALLSAITAPMCVVSNGPNNKMqhSMGKLNMLhyfp 129
Cdd:PLN02779 120 kelvdSLHDRKTElfkeliesGALPLRPGVLRLMD---EALAAGIKVAVCSTSNEKAVSKIVNTLL--GPERAQGL---- 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16131583  130 dKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDDSVAGAQSGIDAGM 180
Cdd:PLN02779 191 -DVFAGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGM 240
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-211 1.41e-12

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 64.45  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    1 MSRIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRF--KGVKlyeiidiVSLEHGVTLAKTEAEHVYRAE 78
Cdd:PRK13222   3 FMDIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVRTWvgNGAD-------VLVERALTWAGREPDEELLEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   79 VARLFD----------SEL--EAIEGAGALLSAiTAPMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPA 146
Cdd:PRK13222  76 LRELFDrhyaenvaggSRLypGVKETLAALKAA-GYPLAVVTNKPTPFVAPLLEALGIADYF-SVVIGGDSLPNKKPDPA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131583  147 LMFHAAKAMNVNVENCILVDDSVAGAQSGIDAGMEVF-----YfcadPHNKPI--VHPKVtTFTHLSQLPEL 211
Cdd:PRK13222 154 PLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVgvtygY----NYGEPIalSEPDV-VIDHFAELLPL 220
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 6-183 4.46e-12

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: 62.64  E-value: 4.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   6 AVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRF--KGV-KLYEiidiVSLEHGVTLAKTEAEH--------- 73
Cdd:cd16417   1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEETVRTWigNGAdVLVE----RALTGAREAEPDEELFkearalfdr 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  74 VYRAEVA---RLFDselEAIEGAGALLSAiTAPMCVVSNGPNNKMQHSMGKLNMLHYFPDKLfSGYDIQRWKPDPALMFH 150
Cdd:cd16417  77 HYAETLSvhsHLYP---GVKEGLAALKAQ-GYPLACVTNKPERFVAPLLEALGISDYFSLVL-GGDSLPEKKPDPAPLLH 151

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 16131583 151 AAKAMNVNVENCILVDDS---VAGAQSgidAGMEVF 183
Cdd:cd16417 152 ACEKLGIAPAQMLMVGDSrndILAARA---AGCPSV 184
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 6-179 4.68e-12

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: 61.64  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     6 AVFFDCDGTLVDSEVICSRAYVTMFQEFGitlDPEEVFKRFKgvKLYEIIdivslEHGVTLAKTEAEHVYRAEVARLFDS 85
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFG---LDPASFKALK--QAGGLA-----EEEWYRIATSALEELQGRFWSEYDA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    86 ELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFpdKLFSGYDIQRWKPDPALMFHAAKAMNVNvENC 162
Cdd:TIGR01549  71 EEAYIRGAADLLARLKSagiKLGIISNGSLRAQKLLLRLFGLGDYF--ELILVSDEPGSKPEPEIFLAALESLGVP-PEV 147

                         170
                  ....*....|....*..
gi 16131583   163 ILVDDSVAGAQSGIDAG 179
Cdd:TIGR01549 148 LHVGDNLNDIEGARNAG 164
PRK11587 PRK11587
putative phosphatase; Provisional
 9-182 1.37e-11

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 61.55  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    9 FDCDGTLVDSEVICSRAYVTMFQEFGItlDPEEVFKRFKGVKLyeiidIVSLEHGVTLAkTEAEhvYRAEVARLFDSELE 88
Cdd:PRK11587   8 FDLDGTLVDSLPAVERAWSNWADRHGI--APDEVLNFIHGKQA-----ITSLRHFMAGA-SEAE--IQAEFTRLEQIEAT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   89 AIEGAGAL---------LSAITAPMCVVSNG--PNNKMQHSMGKLNMlhyfPDKLFSGYDIQRWKPDPALMFHAAKAMNV 157
Cdd:PRK11587  78 DTEGITALpgaiallnhLNKLGIPWAIVTSGsvPVASARHKAAGLPA----PEVFVTAERVKRGKPEPDAYLLGAQLLGL 153

                        170       180
                 ....*....|....*....|....*
gi 16131583  158 NVENCILVDDSVAGAQSGIDAGMEV 182
Cdd:PRK11587 154 APQECVVVEDAPAGVLSGLAAGCHV 178
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 4-182 3.12e-11

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: 60.05  E-value: 3.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   4 IEAVFFDCDGTLVDSEvicsRAYVTMFQEfgiTLDP------EEVFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHVYRA 77
Cdd:cd07529   1 VTHCIFDMDGLLLDTE----RIYTETTQE---ILARygktytWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  78 EVARLFDSELEAIEGAGALLSAITA---PMCVV--SNGPNNKMQHSMGKLnmLHYFPDKLFSGYD---IQRWKPDPALMF 149
Cdd:cd07529  74 ALAELFMGTAKLMPGAERLLRHLHAhniPIALAtsSCTRHFKLKTSRHKE--LFSLFHHVVTGDDpevKGRGKPAPDIFL 151

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 16131583 150 HAAKAMN---VNVENCILVDDSVAGAQSGIDAGMEV 182
Cdd:cd07529 152 VAAKRFNeppKDPSKCLVFEDSPNGVKAAKAAGMQV 187
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 4-214 1.11e-10

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 59.47  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEF----GITLDPEEVFKRFKGVKLYEIIDIV---SLEHGVTLAKtEAEHVYR 76
Cdd:PLN02770  22 LEAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEEFFVENIAGKHNEDIALGLfpdDLERGLKFTD-DKEALFR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   77 aevaRLFDSELEAIEGAGALLSAIT---APMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAK 153
Cdd:PLN02770 101 ----KLASEQLKPLNGLYKLKKWIEdrgLKRAAVTNAPRENAELMISLLGLSDFF-QAVIIGSECEHAKPHPDPYLKALE 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131583  154 AMNVNVENCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQLPELWKA 214
Cdd:PLN02770 176 VLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRNPESLLMEAKPTFLIKDYEDPKLWAA 236
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 6-182 1.13e-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: 58.55  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   6 AVFFDCDGTLVDSEVICSRAYV-TMFQEFGITLD-PEEVFKRFKGV--------KLYE--------IIDIVSLEHGVTLA 67
Cdd:cd07528   1 ALIFDVDGTLAETEELHRRAFNnAFFAERGLDWYwDRELYGELLRVgggkeriaAYFEkvgwpesaPKDLKELIADLHKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  68 KTE--AEHV------YRAEVARLFDselEAIEgAGALLsAItapmCVVSNGPNnkmqhsmgkLNML--HYFP-------D 130
Cdd:cd07528  81 KTEryAELIaagllpLRPGVARLID---EAKA-AGVRL-AI----ATTTSPAN---------VDALlsALLGperraifD 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16131583 131 KLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDDSVAGAQSGIDAGMEV 182
Cdd:cd07528 143 AIAAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPC 194
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 82-185 2.81e-10

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: 55.63  E-value: 2.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  82 LFDSELEAIEGAGALLSAITA--PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNVNV 159
Cdd:cd04305   3 IFDLDDTLLPGAKELLEELKKgyKLGIITNGPTEVQWEKLEQLGIHKYF-DHIVISEEVGVQKPNPEIFDYALNQLGVKP 81

                        90       100
                ....*....|....*....|....*..
gi 16131583 160 ENCILVDDSV-AGAQSGIDAGMEVFYF 185
Cdd:cd04305  82 EETLMVGDSLeSDILGAKNAGIKTVWF 108
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 8-185 7.65e-10

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 55.85  E-value: 7.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   8 FFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVfkrfkgvklYEIIDIVSLEHgvtLAKTEAE-HVYRAEVARLFDSE 86
Cdd:cd07523   3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETV---------YKIIKESSVQF---AIQYYAEvPDLEEEYKELEAEY 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  87 LEAI---EGAGALLSAITApmcvvSNGPNNKMQHS-------MGKLNMLHYFPDKLFSGYDIQRwKPDPALMFHAAKAMN 156
Cdd:cd07523  71 LAKPilfPGAKAVLRWIKE-----QGGKNFLMTHRdhsaltiLKKDGIASYFTEIVTSDNGFPR-KPNPEAINYLLNKYQ 144

                       170       180
                ....*....|....*....|....*....
gi 16131583 157 VNVENCILVDDSVAGAQSGIDAGMEVFYF 185
Cdd:cd07523 145 LNPEETVMIGDRELDIEAGHNAGISTILF 173
PRK10826 PRK10826
hexitol phosphatase HxpB;
2-171 1.02e-09

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 56.49  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    2 SRIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKlyeiID-IVSLEHgvtlAKTEAEHVYRAEVA 80
Cdd:PRK10826   5 RQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELPDTLGLR----IDqVVDLWY----ARQPWNGPSRQEVV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   81 -RLFDSELEAIEGAGALL----SAITapMC--------VVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPAL 147
Cdd:PRK10826  77 qRIIARVISLIEETRPLLpgvrEALA--LCkaqglkigLASASPLHMLEAVLTMFDLRDYF-DALASAEKLPYSKPHPEV 153

                        170       180
                 ....*....|....*....|....
gi 16131583  148 MFHAAKAMNVNVENCILVDDSVAG 171
Cdd:PRK10826 154 YLNCAAKLGVDPLTCVALEDSFNG 177
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 121-180 1.15e-09

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: 55.38  E-value: 1.15e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583 121 KLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDDSVAGAQSGIDAGM 180
Cdd:cd02598  83 KLGLAEYF-DAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAGF 141
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 4-179 1.61e-09

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: 55.75  E-value: 1.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEFGIT-LDPEEVfKRFKGVKLYEIIDIVSLEHgvtlaKTEAEHVYRAEVARL 82
Cdd:cd02616   1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEgYTREEV-LPFIGPPLRETFEKIDPDK-----LEDMVEEFRKYYREH 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  83 FDSELEAIEGAGALLSAITA---PMCVVSngpnNKMQH----SMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAM 155
Cdd:cd02616  75 NDDLTKEYPGVYETLARLKSqgiKLGVVT----TKLREtalkGLKLLGLDKYF-DVIVGGDDVTHHKPDPEPVLKALELL 149

                       170       180
                ....*....|....*....|....
gi 16131583 156 NVNVENCILVDDSVAGAQSGIDAG 179
Cdd:cd02616 150 GAEPEEALMVGDSPHDILAGKNAG 173
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 5-210 3.03e-09

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: 54.97  E-value: 3.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   5 EAVFFDCDGTLVDSEvicsraYVTMFQEFGITLDPEEVFKRFKGvKLYEIIDIVSL--------------------EHGV 64
Cdd:cd02588   1 KALVFDVYGTLIDWH------SGLAAAERAFPGRGEELSRLWRQ-KQLEYTWLVTLmgpyvdfdeltrdalrataaELGL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  65 TLAKTEAEHVYRAeVARL--F-DSE--LEAIEGAGALLSAItapmcvvSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQ 139
Cdd:cd02588  74 ELDESDLDELGDA-YLRLppFpDVVagLRRLREAGYRLAIL-------SNGSPDLIEDVVANAGLRDLF-DAVLSAEDVR 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131583 140 RWKPDPALMFHAAKAMNVNVENCILVDDS---VAGAQsgiDAGMEVFyFCADPHNKP--IVHPKVTTFTHLSQLPE 210
Cdd:cd02588 145 AYKPAPAVYELAAERLGVPPDEILHVASHawdLAGAR---ALGLRTA-WINRPGEVPdpLGPAPDFVVPDLGELAD 216
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 6-211 4.68e-09

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: 54.24  E-value: 4.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   6 AVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRF--KGVKlyeiidiVSLEHGVTLAKT---EAEH------- 73
Cdd:cd07512   1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAEVRSFvgHGAP-------ALIRRAFAAAGEdldGPLHdallarf 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  74 --VYRAEVA---RLFDSELEAIEGagalLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALM 148
Cdd:cd07512  74 ldHYEADPPgltRPYPGVIEALER----LRAAGWRLAICTNKPEAPARALLSALGLADLF-AAVVGGDTLPQRKPDPAPL 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131583 149 FHAAKAMNVNVENCILVDDSVAGAQSGIDAGMEVFYFCADPHNKPIVH-PKVTTFTHLSQLPEL 211
Cdd:cd07512 149 RAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYRHAPVAElPHDAVFSDFDALPDL 212
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 3-180 8.09e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 55.24  E-value: 8.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     3 RIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEvFKRFKGVKLYEIIDIVSLEHGVTLAKTEAEHvyraevARL 82
Cdd:PLN02919   74 KVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVED-FVPFMGTGEANFLGGVASVKGVKGFDPDAAK------KRF 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    83 FDSELE-------AIEGAGALlSAITA------PMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQRWKPDPALMF 149
Cdd:PLN02919  147 FEIYLEkyakpnsGIGFPGAL-ELITQcknkglKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADAFENLKPAPDIFL 225

                         170       180       190
                  ....*....|....*....|....*....|.
gi 16131583   150 HAAKAMNVNVENCILVDDSVAGAQSGIDAGM 180
Cdd:PLN02919  226 AAAKILGVPTSECVVIEDALAGVQAARAAGM 256
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 7-181 4.54e-08

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 51.96  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    7 VFFDCDGTLVDSEV-ICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEIIDIV-----SLEHGVTLAKTEaEHVY---RA 77
Cdd:PLN03243  27 VVLEWEGVIVEDDSeLERKAWRALAEEEGKRPPPAFLLKRAEGMKNEQAISEVlcwsrDFLQMKRLAIRK-EDLYeymQG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   78 EVARLFDSELEAIEgagaLLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNV 157
Cdd:PLN03243 106 GLYRLRPGSREFVQ----ALKKHEIPIAVASTRPRRYLERAIEAVGMEGFF-SVVLAAEDVYRGKPDPEMFMYAAERLGF 180

                        170       180
                 ....*....|....*....|....
gi 16131583  158 NVENCILVDDSVAGAQSGIDAGME 181
Cdd:PLN03243 181 IPERCIVFGNSNSSVEAAHDGCMK 204
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 7-181 1.14e-07

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 51.41  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    7 VFFDCDGTLV-DSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEII--------DIVSLEHGVTlAKTEAEHVYRA 77
Cdd:PLN02575 134 AIFEWEGVIIeDNPDLENQAWLTLAQEEGKSPPPAFILRRVEGMKNEQAIsevlcwsrDPAELRRMAT-RKEEIYQALQG 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   78 EVARLFDSELEAIEgagaLLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNV 157
Cdd:PLN02575 213 GIYRLRTGSQEFVN----VLMNYKIPMALVSTRPRKTLENAIGSIGIRGFF-SVIVAAEDVYRGKPDPEMFIYAAQLLNF 287

                        170       180
                 ....*....|....*....|....
gi 16131583  158 NVENCILVDDSVAGAQSGIDAGME 181
Cdd:PLN02575 288 IPERCIVFGNSNQTVEAAHDARMK 311
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 4-193 3.99e-07

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 48.87  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     4 IEAVFFDCDGTLVDSEVICSRA-----------YVTMFQ---EFGITLDPEEVFKRFKGVkLYEIIDIVSLEHGVTLAKT 69
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAERAaelyggrgealSQLWRQkqlEYSWLRTLMGPYKDFWDL-TREALRYLLGRLGLEDDES 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    70 EAEHVYRAeVARLfDSELEAIEGAGALLSAItAPMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMF 149
Cdd:TIGR01428  80 AADRLAEA-YLRL-PPHPDVPAGLRALKERG-YRLAILSNGSPAMLKSLVKHAGLDDPF-DAVLSADAVRAYKPAPQVYQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 16131583   150 HAAKAMNVNVENCILVDDS---VAGAQsgiDAGMEVFYFcADPHNKP 193
Cdd:TIGR01428 156 LALEALGVPPDEVLFVASNpwdLGGAK---KFGFKTAWI-NRPGEPP 198
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
3-182 6.05e-07

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 48.15  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    3 RIEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDpEEVFKRFKGVKLYEIIDIVSLEHGVTLAKteaeHVYRAEVARL 82
Cdd:PRK10725   4 RYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFD-EQAMVALNGSPTWRIAQAIIELNQADLDP----HALAREKTEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   83 FDSELEAIEGAGALLSAITA-----PMCVvSNGPNNKM-----QHsmgkLNMLHYFpDKLFSGYDIQRWKPDPALMFHAA 152
Cdd:PRK10725  79 VKSMLLDSVEPLPLIEVVKAwhgrrPMAV-GTGSESAIaeallAH----LGLRRYF-DAVVAADDVQHHKPAPDTFLRCA 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 16131583  153 KAMNVNVENCILVDDSVAGAQSGIDAGMEV 182
Cdd:PRK10725 153 QLMGVQPTQCVVFEDADFGIQAARAAGMDA 182
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 7-180 6.56e-07

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: 48.16  E-value: 6.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   7 VFFDCDGTLVDSEVICSRAYVTMFQEFGI-TLDPEEVfKRFKGVKLYEII-----DIVSLEHGVTLAKTEAEHVYR---A 77
Cdd:cd07533   2 VIFDWDGTLADSQHNIVAAMTAAFADLGLpVPSAAEV-RSIIGLSLDEAIarllpMATPALVAVAERYKEAFDILRllpE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  78 EVARLFDSELEAIE---GAGALLSAITAPMcvvSNGPNNKM-QHSMGklnmlHYF-----PDKLFSgydiqrwKPDPALM 148
Cdd:cd07533  81 HAEPLFPGVREALDalaAQGVLLAVATGKS---RRGLDRVLeQHGLG-----GYFdatrtADDTPS-------KPHPEML 145

                       170       180       190
                ....*....|....*....|....*....|..
gi 16131583 149 FHAAKAMNVNVENCILVDDSVAGAQSGIDAGM 180
Cdd:cd07533 146 REILAELGVDPSRAVMVGDTAYDMQMAANAGA 177
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 1-180 8.02e-07

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 48.32  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    1 MSRIEAVFFDCDGTLVD----SEVicsRAYVTMFQEFGITLDPEE---------------------VFKRFKGVklyeii 55
Cdd:PRK13478   1 MMKIQAVIFDWAGTTVDfgsfAPT---QAFVEAFAQFGVEITLEEargpmglgkwdhirallkmprVAARWQAV------ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   56 divsleHGVTLAKTEAEHVYRAEVARLFDS---ELEAIEGAGALLSAITAP--------------MCVVSngPNNKMQhs 118
Cdd:PRK13478  72 ------FGRLPTEADVDALYAAFEPLQIAKladYATPIPGVLEVIAALRARgikigsttgytremMDVVV--PLAAAQ-- 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131583  119 mGklnmlhYFPDKLFSGYDIQRWKPDPALMFHAAKAMNV-NVENCILVDDSVAGAQSGIDAGM 180
Cdd:PRK13478 142 -G------YRPDHVVTTDDVPAGRPYPWMALKNAIELGVyDVAACVKVDDTVPGIEEGLNAGM 197
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 103-185 1.66e-06

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: 45.08  E-value: 1.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583 103 PMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDDSVAGAQSGIDAGMEV 182
Cdd:cd01427  25 KLAIVTNRSREALRALLEKLGLGDLF-DGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRT 103


                ...
gi 16131583 183 FYF 185
Cdd:cd01427 104 VAV 106
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 4-211 2.53e-06

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: 46.71  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583     4 IEAVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDpEEVFKRFKGV-----KLYEIIDIVSLEhgVTLAKTEA------- 71
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLT-EDMFAQYKEInqglwRAYEEGKITKDE--VVNTRFSAllkeynt 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    72 ---EHVYRAEVARLFDSELEAIEGAGALLSAI--TAPMCVVSNGPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRWKPDPA 146
Cdd:TIGR02254  78 eadEALLNQKYLRFLEEGHQLLPGAFELMENLqqKFRLYIVTNGVRETQYKRLRKSGLFPFF-DDIFVSEDAGIQKPDKE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131583   147 LMFHA-AKAMNVNVENCILVDDSV-AGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTHLSQLPEL 211
Cdd:TIGR02254 157 IFNYAlERMPKFSKEEVLMIGDSLtADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEELYEI 223
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 4-178 3.58e-06

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: 45.80  E-value: 3.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   4 IEAVFFDCDGTLVDsevicsrayvtmfqefgitLDPEEVFKRFK--GVKLYEIIDIVSLEHGVTLA-----KTEAEH--V 74
Cdd:cd02603   1 IRAVLFDFGGVLID-------------------PDPAAAVARFEalTGEPSEFVLDTEGLAGAFLElergrITEEEFweE 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  75 YRAEVARLFDSEL--EAIEGAGAL----------LSAITAPMCVVSN-GPNNKMQHSMGKLNMLHYFpDKLFSGYDIQRW 141
Cdd:cd02603  62 LREELGRPLSAELfeELVLAAVDPnpemldlleaLRAKGYKVYLLSNtWPDHFKFQLELLPRRGDLF-DGVVESCRLGVR 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16131583 142 KPDPALMFHAAKAMNVNVENCILVDDS---VAGAQS-GIDA 178
Cdd:cd02603 141 KPDPEIYQLALERLGVKPEEVLFIDDReenVEAARAlGIHA 181
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 4-180 1.22e-05

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 44.60  E-value: 1.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   4 IEAVFFDCDGTLVDSEVIC-SRAYVTMFQEFGITLDPEEVFKRFKGVKLYEIIDIVSLE---------HGVTLAKTEAEH 73
Cdd:cd02586   1 IEAVIFDWAGTTVDYGSFApVNAFVEAFAQRGVQITLEEARKPMGLLKIDHIRALLEMPrvaeawravFGRLPTEADVDA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  74 VYRAEVARLFDS---ELEAIEGAGALLSAITAP-MCVVSN-GPNNKMQHSMGKLNMLH-YFPDKLFSGYDIQRWKPDPAL 147
Cdd:cd02586  81 LYEEFEPILIASlaeYSSPIPGVLEVIAKLRARgIKIGSTtGYTREMMDIVLPEAAAQgYRPDSLVTPDDVPAGRPYPWM 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 16131583 148 MFHAAKAMNV-NVENCILVDDSVAGAQSGIDAGM 180
Cdd:cd02586 161 CYKNAIELGVyDVAAVVKVGDTVPDIKEGLNAGM 194
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 6-178 5.26e-05

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 42.58  E-value: 5.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   6 AVFFDCDGTLVDSEVICSRAYVTMFQEFGITLDPEEVFKRFKGVKLYEiidivSLEhgvTLAKTEAEHVYRAEVA---RL 82
Cdd:cd04302   1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLED-----SFR---ELLPFDEEEAQRAVDAyreYY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  83 FDS---ELEAIEGAGALLSAITA---PMCVVSNGPNNKMQHSMGKLNMLHYFPDKLFSGYDIQR-WKPDpaLMFHAAKAM 155
Cdd:cd04302  73 KEKglfENEVYPGIPELLEKLKAagyRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRvHKAD--VIRYALDTL 150

                       170       180
                ....*....|....*....|....*..
gi 16131583 156 NVNVENCILVDD---SVAGA-QSGIDA 178
Cdd:cd04302 151 GIAPEQAVMIGDrkhDIIGArANGIDS 177
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 96-182 4.25e-04

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: 38.59  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  96 LLSAIT---APMCVVSNGPNNKMQhsmgklnML--HYFP---DKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDD 167
Cdd:cd16421  15 LLKALRqkgIKLAVLSNKPNEAVQ-------VLveELFPgsfDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGD 87

                        90
                ....*....|....*
gi 16131583 168 SVAGAQSGIDAGMEV 182
Cdd:cd16421  88 SGVDMQTARNAGMDE 102
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 3-175 1.13e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 38.86  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583    3 RIEAVFFDCDGTLVDS-EVIcsrayvtmFQEFGITLDP--------EEVFKrFKGVKLYEiidivslehgvTLAKTEAEH 73
Cdd:PRK13288   2 KINTVLFDLDGTLINTnELI--------ISSFLHTLKTyypnqykrEDVLP-FIGPSLHD-----------TFSKIDESK 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   74 V------YRAEVARLFDSELEAIEGAGALLSAITA---PMCVVSngpnNKMQHS--MG-KLNMLHYFPDKLFSGYDIQRW 141
Cdd:PRK13288  62 VeemittYREFNHEHHDELVTEYETVYETLKTLKKqgyKLGIVT----TKMRDTveMGlKLTGLDEFFDVVITLDDVEHA 137

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 16131583  142 KPDPALMFHAAKAMNVNVENCILVDDS----VAGAQSG 175
Cdd:PRK13288 138 KPDPEPVLKALELLGAKPEEALMVGDNhhdiLAGKNAG 175
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 8-180 2.39e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 37.61  E-value: 2.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583   8 FFDCDGTLVDSEV-----ICSRAYVTMFQEFGItlDPEEVFKRFKGvkLYEiidivslEHGVTLAKTEAEH------VYR 76
Cdd:cd02604   3 FFDLDNTLYPLSTglfdqIQARITEFVATKLGL--SPEEARRLRKS--YYK-------EYGTTLRGLMAEHgidpdeFLD 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131583  77 AEVARLFDSELEAIEGAGALLSAITAPMCVVSNGPNNKMQHSMGKLNMLHYFpDKLF----SGYDIqrwKPDPALMFHAA 152
Cdd:cd02604  72 RVVHLILYDHLKPDPKLRNLLLALPGRKIIFTNASKNHAIRVLKRLGLADLF-DGIFdieyAGPDP---KPHPAAFEKAI 147

                       170       180
                ....*....|....*....|....*...
gi 16131583 153 KAMNVNVENCILVDDSVAGAQSGIDAGM 180
Cdd:cd02604 148 REAGLDPKRAAFFDDSIRNLLAAKALGM 175
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH