NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1481093421|gb|AYB35003|]
View 

HAD family hydrolase [Chryseolinea soli]

Protein Classification

HAD-IIA family hydrolase( domain architecture ID 11576402)

haloacid dehalogenase (HAD)-IIA family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
3-249 2.28e-106

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 307.98  E-value: 2.28e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:cd07530     1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDPS-PKKKGWnNLGIAA 161
Cdd:cd07530    81 PGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTlPTERGL-LPGNGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 162 TTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPD 241
Cdd:cd07530   160 VVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYRPT 239

                  ....*...
gi 1481093421 242 LVVNSVND 249
Cdd:cd07530   240 YIVPSLRE 247
 
Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
3-249 2.28e-106

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 307.98  E-value: 2.28e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:cd07530     1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDPS-PKKKGWnNLGIAA 161
Cdd:cd07530    81 PGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTlPTERGL-LPGNGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 162 TTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPD 241
Cdd:cd07530   160 VVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYRPT 239

                  ....*...
gi 1481093421 242 LVVNSVND 249
Cdd:cd07530   240 YIVPSLRE 247
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
3-252 8.66e-105

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 304.34  E-value: 8.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:COG0647     9 DAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLV-DTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDPSPKKKGWNNLGIAA 161
Cdd:COG0647    89 PGARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAGA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 162 TTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPD 241
Cdd:COG0647   169 LAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPIRPD 248
                         250
                  ....*....|.
gi 1481093421 242 LVVNSVNDIEL 252
Cdd:COG0647   249 YVLDSLAELLL 259
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-252 6.18e-66

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 205.03  E-value: 6.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:PRK10444    2 KNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKgTAYVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDP-----SPkkkgwnnl 157
Cdd:PRK10444   82 GK-KAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDThgrgfYP-------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 158 GIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYA 237
Cdd:PRK10444  153 ACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMP 232
                         250
                  ....*....|....*
gi 1481093421 238 FKPDLVVNSVNDIEL 252
Cdd:PRK10444  233 FRPSWIYPSVADIDV 247
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
3-249 7.98e-58

HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 130524  Cd Length: 249  Bit Score: 184.67  E-value: 7.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:TIGR01457   2 KGYLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDPS-PKKKGWNNlGIAA 161
Cdd:TIGR01457  82 KDASVYVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFISTNGDIAiPTERGLLP-GNGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 162 TTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPD 241
Cdd:TIGR01457 161 LTSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHTGVTKREHMTDDMEKPT 240

                  ....*...
gi 1481093421 242 LVVNSVND 249
Cdd:TIGR01457 241 HAIDSLAE 248
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
5-105 2.58e-34

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 119.11  E-value: 2.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   5 LLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQVPK 84
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80
                          90       100
                  ....*....|....*....|.
gi 1481093421  85 GTAYVLGEGGLISSLHDHGIT 105
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
 
Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
3-249 2.28e-106

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 307.98  E-value: 2.28e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:cd07530     1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDPS-PKKKGWnNLGIAA 161
Cdd:cd07530    81 PGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTlPTERGL-LPGNGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 162 TTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPD 241
Cdd:cd07530   160 VVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYRPT 239

                  ....*...
gi 1481093421 242 LVVNSVND 249
Cdd:cd07530   240 YIVPSLRE 247
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
3-252 8.66e-105

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 304.34  E-value: 8.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:COG0647     9 DAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLV-DTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDPSPKKKGWNNLGIAA 161
Cdd:COG0647    89 PGARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAGA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 162 TTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPD 241
Cdd:COG0647   169 LAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPIRPD 248
                         250
                  ....*....|.
gi 1481093421 242 LVVNSVNDIEL 252
Cdd:COG0647   249 YVLDSLAELLL 259
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-252 6.18e-66

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 205.03  E-value: 6.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:PRK10444    2 KNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKgTAYVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDP-----SPkkkgwnnl 157
Cdd:PRK10444   82 GK-KAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDThgrgfYP-------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 158 GIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYA 237
Cdd:PRK10444  153 ACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMP 232
                         250
                  ....*....|....*
gi 1481093421 238 FKPDLVVNSVNDIEL 252
Cdd:PRK10444  233 FRPSWIYPSVADIDV 247
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
4-249 5.84e-63

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 198.36  E-value: 5.84e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   4 GLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQVP 83
Cdd:cd07508     1 LVISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  84 KGTAYVLGEGGLISSLHDHGITLV-------------------DTEPDFVVLGEGRNFTLEMVQRAVDMILA-GAKFITT 143
Cdd:cd07508    81 GKKVYVLGEEGLKEELRAAGFRIAggpskgietyaelvehledDENVDAVIVGSDFKLNFAKLRKACRYLRNpGCLFIAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 144 NRDPS-PKKKGWNNLGIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTIL 222
Cdd:cd07508   161 APDRIhPLKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLL 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1481093421 223 VLSGISKNEELKKYA---FKPDLVVNSVND 249
Cdd:cd07508   241 VLTGVTTLEDLQAYIdheLVPDYYADSLAD 270
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
3-250 1.69e-59

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319833 [Multi-domain]  Cd Length: 252  Bit Score: 188.93  E-value: 1.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:cd07531     1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLAREK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLVDT--EPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDPSPKKKGWNNLGIA 160
Cdd:cd07531    81 PNAKVFVTGEEGLIEELRLAGLEIVDKydEAEYVVVGSNRKITYELLTKAFRACLRGARYIATNPDRIFPAEDGPIPDTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 161 ATTAMIEEATGIKA-FVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFK 239
Cdd:cd07531   161 AIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTGVTTRENLDRHGYK 240
                         250
                  ....*....|.
gi 1481093421 240 PDLVVNSVNDI 250
Cdd:cd07531   241 PDYVLNSIKDL 251
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
3-249 7.98e-58

HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 130524  Cd Length: 249  Bit Score: 184.67  E-value: 7.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQV 82
Cdd:TIGR01457   2 KGYLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRDPS-PKKKGWNNlGIAA 161
Cdd:TIGR01457  82 KDASVYVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFISTNGDIAiPTERGLLP-GNGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 162 TTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPD 241
Cdd:TIGR01457 161 LTSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHTGVTKREHMTDDMEKPT 240

                  ....*...
gi 1481093421 242 LVVNSVND 249
Cdd:TIGR01457 241 HAIDSLAE 248
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
6-247 2.87e-52

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 170.31  E-value: 2.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   6 LIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQVPKG 85
Cdd:cd16422     3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  86 TAYVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMILAGAKFITTNRD---PSPKKKGWNnlgIAAT 162
Cdd:cd16422    83 KIFLLGTKSLREEFEKAGFTLDGDDIDVVVLGFDTELTYEKLRTACLLLRRGIPYIATHPDincPSEEGPIPD---AGSI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 163 TAMIEEATGIKA-FVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPD 241
Cdd:cd16422   160 IALIETSTGRRPdLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSGETTREDLEDLERKPT 239

                  ....*.
gi 1481093421 242 LVVNSV 247
Cdd:cd16422   240 YVFDNV 245
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
4-250 3.67e-42

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 145.22  E-value: 3.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   4 GLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEV-TENHIYTSAMATAKFLASQV 82
Cdd:cd07510     3 TFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGlKEEEIFSSAYCAARYLRQRL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 P---KGTAYVLGEGGLISSLHDHGITLVDTEPDF--------------------VVLGEGRNFTLEMVQRAVDMIL-AGA 138
Cdd:cd07510    83 PgpaDGKVYVLGGEGLRAELEAAGVAHLGGPDDGlrraapkdwllagldpdvgaVLVGLDEHVNYLKLAKATQYLRdPGC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 139 KFITTNRDPS-PKKKGWNNLGIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMG 217
Cdd:cd07510   163 LFVATNRDPWhPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQNCG 242
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1481093421 218 YRTILVLSGISKNEELKKYAFK---PDLVVNSVNDI 250
Cdd:cd07510   243 LKTLLVLTGVSTLEEALAKLSNdlvPDYYVESLADL 278
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
6-226 4.29e-41

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 140.92  E-value: 4.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   6 LIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKL-GIEVTENHIYTSAMATAKFLASQVPK 84
Cdd:TIGR01460   2 LFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLlGVDVSPDQIITSGSVTKDLLRQRFEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  85 GTAYVLGEGGLISSLHDHGITLVDTE----------PDFVVLGEGRNFTLEMVQRAVDMILAG-AKFITTNRDPSPKKK- 152
Cdd:TIGR01460  82 EKVYVIGVGELRESLEGLGFRNDFFDdidhlaiekiPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDLVRLGd 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1481093421 153 GWNNLGIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTV-IGDTMDTDIQGGVQMGYRTILVLSG 226
Cdd:TIGR01460 162 GRFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRDVmVGDNLRTDILGAKNAGFDTLLVLTG 236
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
2-250 7.94e-41

phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d


Pssm-ID: 273635 [Multi-domain]  Cd Length: 279  Bit Score: 141.54  E-value: 7.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   2 AKGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQ 81
Cdd:TIGR01452   2 AQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLRQP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  82 VPKGTA-YVLGEGGLISSLHDHGITLVDTEPDF--------------------VVLGEGRNFTLEMVQRAVDMIL-AGAK 139
Cdd:TIGR01452  82 PDAGKAvYVIGEEGLRAELDAAGIRLAGDPGEKkqdeadgfmydikldervgaVVVGYDEHFSYVKLMEACAHLRePGCL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 140 FITTNRDP-SPKKKGWNNLGIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGY 218
Cdd:TIGR01452 162 FVATNRDPwHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRCGM 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1481093421 219 RTILVLSGISKNEELKKYA------FKPDLVVNSVNDI 250
Cdd:TIGR01452 242 TTVLVLSGVSQLEEAQEYLmagqddLVPDYVVESLADL 279
PLN02645 PLN02645
phosphoglycolate phosphatase
6-250 2.22e-39

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 138.69  E-value: 2.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   6 LIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQ--VP 83
Cdd:PLN02645   32 IFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLKSInfPK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  84 KGTAYVLGEGGLISSLHDHGITL----------VDTEPDF----------VVLGEGRNFTLEMVQRAVDMIL--AGAKFI 141
Cdd:PLN02645  112 DKKVYVIGEEGILEELELAGFQYlggpedgdkkIELKPGFlmehdkdvgaVVVGFDRYINYYKIQYATLCIRenPGCLFI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 142 TTNRDPS---PKKKGWNnlGIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGY 218
Cdd:PLN02645  192 ATNRDAVthlTDAQEWA--GAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGC 269
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1481093421 219 RTILVLSGISKNEELKKYAFK--PDLVVNSVNDI 250
Cdd:PLN02645  270 KTLLVLSGVTSESMLLSPENKiqPDFYTSKISDF 303
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
3-249 4.33e-39

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 136.26  E-value: 4.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLAS-Q 81
Cdd:cd07509     1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEkG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  82 VPKgtaYVLGEGGLISSLhdhgITLVDTEPDFVVLGE-GRNFTLEMVQRAVDMILAGAKFITTNRDPSPKKKGWNNLGIA 160
Cdd:cd07509    81 LRP---HLLVDDDALEDF----IGIDTSDPNAVVIGDaGEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 161 ATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKP 240
Cdd:cd07509   154 AFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPNVPP 233

                  ....*....
gi 1481093421 241 DLVVNSVND 249
Cdd:cd07509   234 DLTADSFAD 242
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
5-105 2.58e-34

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 119.11  E-value: 2.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   5 LLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQVPK 84
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80
                          90       100
                  ....*....|....*....|.
gi 1481093421  85 GTAYVLGEGGLISSLHDHGIT 105
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
6-250 3.54e-33

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319834 [Multi-domain]  Cd Length: 286  Bit Score: 122.03  E-value: 3.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   6 LIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLASQVPKG 85
Cdd:cd07532    10 IFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLKEKGFKK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  86 TAYVLGEGGLISSLHDHGI---------------------TLVDTEPDFVVLGEGRNFTLEMVQRAVDMIL-AGAKFITT 143
Cdd:cd07532    90 KVYVIGEEGIRKELEEAGIvscggdgedekddsmgdfahnLELDPDVGAVVVGRDEHFSYPKLMKACNYLRnPDVLFLAT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 144 NRD---PSPKKKgwNNLGIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRT 220
Cdd:cd07532   170 NMDatfPGPVGR--VIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFANNCGFQS 247
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1481093421 221 ILVLSGISKNEEL---------KKYAFKPDLVVNSVNDI 250
Cdd:cd07532   248 LLVGTGVNSLEDAekikkegdpKKKDLVPDTYLPSLGHL 286
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
3-249 5.17e-29

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 110.34  E-value: 5.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIY----GGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFL 78
Cdd:TIGR01458   2 KGVLLDISGVLYisdaGGGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  79 ASQvpKGTAYVLGEGGLISSLHDhgitlVDT-EPDFVVLGE-GRNFTLEMVQRAVDMILAGAK--FITTNRDPSPKKKGW 154
Cdd:TIGR01458  82 EEK--QLRPMLLVDDRVLPDFDG-----IDTsDPNCVVMGLaPEHFSYQILNQAFRLLLDGAKpvLIAIGKGRYYKRKDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 155 NNLGIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELK 234
Cdd:TIGR01458 155 LALDVGPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPSDEE 234
                         250
                  ....*....|....*
gi 1481093421 235 KYAFKPDLVVNSVND 249
Cdd:TIGR01458 235 KINVPPDLTCDSLPH 249
Hydrolase_like pfam13242
HAD-hyrolase-like;
176-249 2.85e-24

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 92.29  E-value: 2.85e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1481093421 176 VVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFKPDLVVNSVND 249
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAE 74
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
4-225 2.91e-09

HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily model)


Pssm-ID: 130526 [Multi-domain]  Cd Length: 242  Bit Score: 56.05  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   4 GLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRT-PLEAvrKLRKLGIEVTE-NHIYTSA-MATAKFLAS 80
Cdd:TIGR01459  10 VFLLDLWGVIIDGNHTYPGAVQNLNKIIAQGKPVYFVSNSPRNIfSLHK--TLKSLGINADLpEMIISSGeIAVQMILES 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  81 ----QVPKGTAYVLGEG--------GLISSLHDHG-----ITLVDTEPDFVVLGEGRNFTLEMVQRAVdmilagaKFITT 143
Cdd:TIGR01459  88 kkrfDIRNGIIYLLGHLendiinlmQCYTTDDENKanaslITIYRSENEKLDLDEFDELFAPIVARKI-------PNICA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 144 NRDPSPKKKGWNNLGIAATTAMIEEATGiKAFVVGKPGPVMMRSSRKHIGLETADTTV-IGDTMDTDIQGGVQMGYRTIL 222
Cdd:TIGR01459 161 NPDRGINQHGIYRYGAGYYAELIKQLGG-KVIYSGKPYPAIFHKALKECSNIPKNRMLmVGDSFYTDILGANRLGIDTAL 239

                  ...
gi 1481093421 223 VLS 225
Cdd:TIGR01459 240 VLT 242
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
5-243 1.12e-08

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 54.25  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   5 LLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPlEAVRKLRKLGIE-VTENHIYTSAMATAKFLA-SQV 82
Cdd:cd07525     3 FLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPRPAE-SVVRQLAKLGVPpSTYDAIITSGEVTRELLArEAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 PKGTAYVLGEGGLISSLHDHGITLVDTEP--DFVVLGEGRNFTLEMVQRAVDMILA----GAKFITTNRD---PSPKKKG 153
Cdd:cd07525    82 LGRKVYHLGPERDANVLEGLDVVATDDAEkaEFILCTGLYDDETETPEDYRKLLKAaaarGLPLICANPDlvvPRGGKLI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 154 WnnlgIAATTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTV-IGDTMDTDIQGGVQMGYRTILVLSGISKN-- 230
Cdd:cd07525   162 Y----CAGALAELYEELGGEVIYFGKPHPPIYDLALARLGRPAKARILaVGDGLHTDILGANAAGLDSLFVTGGIHRRla 237
                         250
                  ....*....|....
gi 1481093421 231 EELK-KYAFKPDLV 243
Cdd:cd07525   238 AEAGiKSQIVPDFV 251
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
150-250 2.47e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 53.01  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 150 KKKGWNnLGIA-----ATTAMIEEATGIK---AFVVG-------KPGPVMMRSSRKHIGLETADTTVIGDTmDTDIQGGV 214
Cdd:COG0546    97 KARGIK-LAVVtnkprEFAERLLEALGLDdyfDAIVGgddvppaKPKPEPLLEALERLGLDPEEVLMVGDS-PHDIEAAR 174
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1481093421 215 QMGYRTILVLSGISKNEELKkyAFKPDLVVNSVNDI 250
Cdd:COG0546   175 AAGVPFIGVTWGYGSAEELE--AAGADYVIDSLAEL 208
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
166-239 2.75e-07

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 49.32  E-value: 2.75e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1481093421 166 IEEATGIKAFVVG-KPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSGISKNEELKKYAFK 239
Cdd:TIGR01668  77 VEKALGIPVLPHAvKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQWFIKRIWR 151
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
178-223 1.18e-05

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 43.41  E-value: 1.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1481093421 178 GKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILV 223
Cdd:cd16416    63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
4-70 3.57e-05

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5); 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: 319814  Cd Length: 136  Bit Score: 42.38  E-value: 3.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1481093421   4 GLLIDMDGVIYGGDILIPGADTFITRLLNENIPFTFMTNNSQRTPLEAVRKLRK-LGIEVTENHIYTS 70
Cdd:cd07511     2 GFAFDIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLSKlLGVEVSPDQVIQS 69
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
164-233 3.68e-05

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 42.81  E-value: 3.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1481093421 164 AMIEEATGIKA-FVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILVLSgISKNEEL 233
Cdd:COG2179    75 KRFAEKLGIPYiARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKP-LVDKEFW 144
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
3-217 5.31e-05

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: 42.96  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDiliPGADTFITRLLNENIPFtfmtnnsqrtpLEAVRKLRKLGIEVTENHIyTSAMATAKFLASqv 82
Cdd:pfam00702   2 KAVVFDLDGTLTDGE---PVVTEAIAELASEHPLA-----------KAIVAAAEDLPIPVEDFTA-RLLLGKRDWLEE-- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 pkgtayVLGEGGLISSLHDHGITLVDTEPDFVVLGEGRNFTLEMVQRAVDMI-LAGAK-FITTNRDPSPKKKGWNNLGIa 160
Cdd:pfam00702  65 ------LDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALkERGIKvAILTGDNPEAAEALLRLLGL- 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1481093421 161 atTAMIEEATGIKAFVVGKPGPVMMRSSRKHIGLETADTTVIGDTMDtDIQGGVQMG 217
Cdd:pfam00702 138 --DDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVN-DIPAAKAAG 191
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
179-250 7.04e-05

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 42.39  E-value: 7.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1481093421 179 KPGPVMMRSSRKHIGLETADTTVIGDTMdTDIQGGVQMGYRTILVLSGISKNEELKKyafKPDLVVNSVNDI 250
Cdd:COG0241   102 KPKPGMLLQAAERLGIDLSNSYMIGDRL-SDLQAAKAAGCKGILVLTGKGAEELAEA---LPDTVADDLAEA 169
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
178-250 1.40e-04

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: 41.62  E-value: 1.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1481093421 178 GKPGPVMMRSSRKHIGLETADTTVIGDTMdTDIQGGVQMGYRTILVLSGISKNEELKKyaFKPDLVVNSVNDI 250
Cdd:cd07533   138 SKPHPEMLREILAELGVDPSRAVMVGDTA-YDMQMAANAGAHAVGVAWGYHSLEDLRS--AGADAVVDHFSEL 207
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
3-250 1.86e-04

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: 41.55  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421   3 KGLLIDMDGVIYGGDiliPGADTFITRLLNEnipftFMTNNSQRTPLEAVRKLRKLGIEVTENHIYTSAMATAKFLAsqv 82
Cdd:COG1011     2 KAVLFDLDGTLLDFD---PVIAEALRALAER-----LGLLDEAEELAEAYRAIEYALWRRYERGEITFAELLRRLLE--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421  83 pkgtayvlgegglisslhDHGITLVDTEPDfvVLGEGRNFTLEMVQRAVDMI--LAGA---KFITTNrdpspkkkgwnnl 157
Cdd:COG1011    71 ------------------ELGLDLAEELAE--AFLAALPELVEPYPDALELLeaLKARgyrLALLTN------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481093421 158 GIAATTAMIEEATGIKAFV----------VGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTILvlsgI 227
Cdd:COG1011   118 GSAELQEAKLRRLGLDDLFdavvsseevgVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVW----V 193
                         250       260
                  ....*....|....*....|...
gi 1481093421 228 SKNEELKKYAFKPDLVVNSVNDI 250
Cdd:COG1011   194 NRSGEPAPAEPRPDYVISDLAEL 216
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
179-250 2.35e-04

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 40.96  E-value: 2.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1481093421 179 KPGPVMMRSSRKHIGLETADTTVIGDTMDtDIQGGVQMGYRTILVLSGisKNE-ELKKYAFKPDLVVNSVNDI 250
Cdd:PRK08942  103 KPKPGMLLSIAERLNIDLAGSPMVGDSLR-DLQAAAAAGVTPVLVRTG--KGVtTLAEGAAPGTWVLDSLADL 172
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
179-223 5.69e-04

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 39.05  E-value: 5.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1481093421 179 KPGPVMMRSSRKHIGLETADTTVIGDTmDTDIQGGVQMGYRTILV 223
Cdd:cd07503    99 KPKPGMLLDAAKELGIDLARSFVIGDR-LSDIQAARNAGCKGILV 142
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
4-70 3.37e-03

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 38.32  E-value: 3.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1481093421   4 GLLIDMDGVIYGGDILIPGADTFITRLLNEN----IPFTFMTNN---SQRTPLEAVRKLrkLGIEVTENHIYTS 70
Cdd:TIGR01456   2 GFAFDIDGVLFRGKKPIAGASDALRRLNRNQgqlkIPYIFLTNGggfSERARAEEISSL--LGVDVSPLQVIQS 73
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
166-221 6.20e-03

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: 35.60  E-value: 6.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1481093421 166 IEEATGikafvVGKPGPVMMRSSRKHIGLETADTTVIGDTMDTDIQGGVQMGYRTI 221
Cdd:cd04305    56 ISEEVG-----VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
179-225 6.65e-03

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 35.84  E-value: 6.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1481093421 179 KPGPVMMRSSRKH-IGLETADTTVIGDTMDTDIQGGVQMGYRTILVLS 225
Cdd:TIGR01662  88 KPKPGMFLEALKRfNEIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
 
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