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Conserved domains on  [gi|504921285|ref|WP_015108387|]
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YqeG family HAD IIIA-type phosphatase [Cyanobium gracile]

Protein Classification

YqeG family HAD IIIA-type phosphatase( domain architecture ID 11450658)

YqeG family HAD (haloacid dehalogenase) IIIA-type phosphatase similar to Bacillus subtilis YqeG, which may be involved in the hydrolysis of the phosphate group of 5'-nucleotides and is necessary for normal colony formation on solid medium

CATH:  3.30.1240.10
EC:  3.1.3.-
Gene Ontology:  GO:0042578
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
4-147 5.57e-55

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


:

Pssm-ID: 441782  Cd Length: 164  Bit Score: 170.70  E-value: 5.57e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285   4 DLLTPDWFpGTSLAHLPLQELVDRGIRALVLDVDRTLLPRRQATMPLQAEVWLRHARER-MPLHLLSNNpSRRRIGAVAD 82
Cdd:COG2179    2 KLLKPDEY-VKSIYDIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAgFKVCIVSNN-SEKRVKRFAE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504921285  83 TMGLPYTTSAGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVKPIDPDGEP 147
Cdd:COG2179   80 KLGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKEFW 144
 
Name Accession Description Interval E-value
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
4-147 5.57e-55

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 170.70  E-value: 5.57e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285   4 DLLTPDWFpGTSLAHLPLQELVDRGIRALVLDVDRTLLPRRQATMPLQAEVWLRHARER-MPLHLLSNNpSRRRIGAVAD 82
Cdd:COG2179    2 KLLKPDEY-VKSIYDIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAgFKVCIVSNN-SEKRVKRFAE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504921285  83 TMGLPYTTSAGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVKPIDPDGEP 147
Cdd:COG2179   80 KLGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKEFW 144
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 31-138 5.98e-35

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: 118.14  E-value: 5.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  31 ALVLDVDRTLLPRRQATMPLQAEVWLRHARER-MPLHLLSNNPSRRRIgAVADTMGLPYTTSAGKPRRAALRKVLQDLAL 109
Cdd:cd16416    1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAgIKVVLVSNNNERRVA-KVIEKLDLPFVARAGKPRPRAFRRALKEMDL 79

                         90       100
                 ....*....|....*....|....*....
gi 504921285 110 PPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:cd16416   80 PPEQVAMVGDQLFTDILGGNRAGLYTILV 108
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 14-166 4.01e-32

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: 112.88  E-value: 4.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285   14 TSLAHLPLQELVDRGIRALVLDVDRTLLP--RRQATMPLqaEVWLRHARE-RMPLHLLSNNPSRRRIGAVADTMGLPYTT 90
Cdd:TIGR01668  10 KTLNDLTIDLLKKVGIKGVVLDKDNTLVYpdHNEAYPAL--RDWIEELKAaGRKLLIVSNNAGEQRAKAVEKALGIPVLP 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504921285   91 SAGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVKPIDPDGEPCRQDRLQNLELRMARWVGS 166
Cdd:TIGR01668  88 HAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQWFIKRIWRRVERTVLKFLVS 163
Hydrolase_like pfam13242
HAD-hyrolase-like;
92-139 5.09e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 53.00  E-value: 5.09e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 504921285   92 AGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVK 139
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVL 49
PLN02645 PLN02645
phosphoglycolate phosphatase
 93-138 5.77e-05

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 42.01  E-value: 5.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 504921285  93 GKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:PLN02645 229 GKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCKTLLV 274
 
Name Accession Description Interval E-value
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
4-147 5.57e-55

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 170.70  E-value: 5.57e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285   4 DLLTPDWFpGTSLAHLPLQELVDRGIRALVLDVDRTLLPRRQATMPLQAEVWLRHARER-MPLHLLSNNpSRRRIGAVAD 82
Cdd:COG2179    2 KLLKPDEY-VKSIYDIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAgFKVCIVSNN-SEKRVKRFAE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504921285  83 TMGLPYTTSAGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVKPIDPDGEP 147
Cdd:COG2179   80 KLGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKEFW 144
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 31-138 5.98e-35

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: 118.14  E-value: 5.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  31 ALVLDVDRTLLPRRQATMPLQAEVWLRHARER-MPLHLLSNNPSRRRIgAVADTMGLPYTTSAGKPRRAALRKVLQDLAL 109
Cdd:cd16416    1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAgIKVVLVSNNNERRVA-KVIEKLDLPFVARAGKPRPRAFRRALKEMDL 79

                         90       100
                 ....*....|....*....|....*....
gi 504921285 110 PPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:cd16416   80 PPEQVAMVGDQLFTDILGGNRAGLYTILV 108
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 14-166 4.01e-32

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: 112.88  E-value: 4.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285   14 TSLAHLPLQELVDRGIRALVLDVDRTLLP--RRQATMPLqaEVWLRHARE-RMPLHLLSNNPSRRRIGAVADTMGLPYTT 90
Cdd:TIGR01668  10 KTLNDLTIDLLKKVGIKGVVLDKDNTLVYpdHNEAYPAL--RDWIEELKAaGRKLLIVSNNAGEQRAKAVEKALGIPVLP 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504921285   91 SAGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVKPIDPDGEPCRQDRLQNLELRMARWVGS 166
Cdd:TIGR01668  88 HAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQWFIKRIWRRVERTVLKFLVS 163
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
90-138 2.53e-10

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 57.04  E-value: 2.53e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 504921285  90 TSAGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:COG0647  182 LVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLV 230
Hydrolase_like pfam13242
HAD-hyrolase-like;
92-139 5.09e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 53.00  E-value: 5.09e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 504921285   92 AGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVK 139
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVL 49
PGP_phosphatase pfam09419
Mitochondrial PGP phosphatase; This is a family of proteins that acts as a mitochondrial ...
 15-139 8.48e-10

Mitochondrial PGP phosphatase; This is a family of proteins that acts as a mitochondrial phosphatase in cardiolipin biosynthesis. Cardiolipin is a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes. The inverted phosphatase motif includes the highly conserved DKD triad.


Pssm-ID: 430598  Cd Length: 168  Bit Score: 54.65  E-value: 8.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285   15 SLAHLPLQ--ELVDRGIRALVLDVDRTLlprrqaTMPLQAEVW------LRHARERMP---LHLLSNnpsrrRIGAVADT 83
Cdd:pfam09419  25 TFNQLPIPinGLKGVGIKAVVLDKDNCF------ALPHDDKVWppykekWEELRAAYPgkrLLIVSN-----SAGSNDDK 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504921285   84 -----------MGLP-YTTSAGKPR-----RAALRKvlQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVK 139
Cdd:pfam09419  94 dgeqakaleksTGIPvLRHPVKKPGcgeevLEYFKE--RGVVTRPSEIAVVGDRLFTDILMANMMGSWGVWLT 164
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 18-150 4.77e-09

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: 53.49  E-value: 4.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  18 HLPLQELVDRGIRALVLDVDRTLLPRRQATMPLQAEVW------LRHARER-MPLHLLSNNPsRRRIGAVADTMGL-PY- 88
Cdd:COG1011   58 EITFAELLRRLLEELGLDLAEELAEAFLAALPELVEPYpdalelLEALKARgYRLALLTNGS-AELQEAKLRRLGLdDLf 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504921285  89 ---TTS----AGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVKPIDPDGEPCRQ 150
Cdd:COG1011  137 davVSSeevgVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPR 205
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 30-140 1.93e-08

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: 50.48  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285   30 RALVLDVDRTLLPRR-------QATMPLQAEVWLRHARER-MPLHLLSNN-------PSRRRIGAVADT--------MGL 86
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVpyvsdedERILYPEVPDALAELKEAgYKVVIVTNQsgigrgyFSRSFSGRVARRleelgvpiDIL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504921285   87 PYTTSAGKPRRAALRKVLQDL-ALPPAQVALVGDRLFTDVLVGNRMGLFTVLVKP 140
Cdd:TIGR01662  81 YACPGCRKPKPGMFLEALKRFnEIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 26-138 3.04e-08

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: 51.40  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285   26 DRGIRALVLDVDR--TLLPRRQATMPLQAEVWLRHARERMPLHLLSNN---PSRRRIGAVADTMGLPYTTSAGKPRRAAL 100
Cdd:TIGR01452 129 DERVGAVVVGYDEhfSYVKLMEACAHLREPGCLFVATNRDPWHPLSDGsrtPGTGSLVAAIETASGRQPLVVGKPSPYMF 208

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 504921285  101 RKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:TIGR01452 209 NCITEKFSIDPARTLMVGDRLETDILFGHRCGMTTVLV 246
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 91-138 9.06e-08

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: 49.90  E-value: 9.06e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504921285  91 SAGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:cd07530  174 FIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLV 221
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 23-138 3.66e-07

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: 48.20  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  23 ELVDRGIRALVLDVDRTLLPRRQATmplqAEVWLRHARERMPLHLLSNNPSRRRIGAVADTMGLPYTTS--------AGK 94
Cdd:cd16422  102 TLDGDDIDVVVLGFDTELTYEKLRT----ACLLLRRGIPYIATHPDINCPSEEGPIPDAGSIIALIETStgrrpdlvIGK 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 504921285  95 PRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:cd16422  178 PNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILV 221
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 26-138 6.26e-07

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: 47.77  E-value: 6.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  26 DRGIRALVLDVDR--TLLPRRQATMPLQAEVWLRHARERMPLHLLSNNpsrrRIGAVADTMGLPYTTSA-------GKPR 96
Cdd:cd07510  131 DPDVGAVLVGLDEhvNYLKLAKATQYLRDPGCLFVATNRDPWHPLSDG----SFIPGTGSLVAALETASgrqaivvGKPS 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 504921285  97 RAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:cd07510  207 RFMFDCISSKFSIDPARTCMVGDRLDTDILFGQNCGLKTLLV 248
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 13-138 9.28e-07

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: 47.36  E-value: 9.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  13 GTSLAHLPLQELV-----DRGIRALVLDVDRTLlprrQATMPLQAEVWLRH------ARERMPLHLLSNNpsrRRIGAVA 81
Cdd:cd07508  106 GPSKGIETYAELVehledDENVDAVIVGSDFKL----NFAKLRKACRYLRNpgclfiATAPDRIHPLKDG---GPIPGTG 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504921285  82 DTMGLPYTTS------AGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:cd07508  179 AFAAAVEAATgrqplvLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLLV 241
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 31-136 3.61e-06

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: 43.68  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  31 ALVLDVDRTLLPRRQATmplqaevwLRHARERMPLHLLSNNPS---RRRIgavaDTMGL-PY----TTS----AGKPRRA 98
Cdd:cd04305    1 AIIFDLDDTLLPGAKEL--------LEELKKGYKLGIITNGPTevqWEKL----EQLGIhKYfdhiVISeevgVQKPNPE 68

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504921285  99 ALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTV 136
Cdd:cd04305   69 IFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
56-138 1.27e-05

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 43.76  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  56 LRHARER-MPLHLLSNNPsRRRIGAVADTMGL-PY--------TTSAGKPRRAALRKVLQDLALPPAQVALVGDRLFtDV 125
Cdd:COG0546   93 LEALKARgIKLAVVTNKP-REFAERLLEALGLdDYfdaivggdDVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPH-DI 170

                         90
                 ....*....|...
gi 504921285 126 LVGNRMGLFTVLV 138
Cdd:COG0546  171 EAARAAGVPFIGV 183
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 31-138 4.32e-05

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: 40.46  E-value: 4.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  31 ALVLDVDRTLLprrqatmplqAEVWLRHARER-MPLHLLSNNpSRRRIGAVADTMGLPY---------TTSAGKPRRAAL 100
Cdd:cd01427    1 AVLFDLDGTLL----------AVELLKRLRAAgIKLAIVTNR-SREALRALLEKLGLGDlfdgiigsdGGGTPKPKPKPL 69

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504921285 101 RKVLQDLALPPAQVALVGDRLfTDVLVGNRMGLFTVLV 138
Cdd:cd01427   70 LLLLLKLGVDPEEVLFVGDSE-NDIEAARAAGGRTVAV 106
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 77-138 4.52e-05

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: 42.17  E-value: 4.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504921285  77 IGAVADTMGLPYTTSAGKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:cd07531  163 IGAIEWCTGREPEVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALV 224
PLN02645 PLN02645
phosphoglycolate phosphatase
 93-138 5.77e-05

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 42.01  E-value: 5.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 504921285  93 GKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:PLN02645 229 GKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCKTLLV 274
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 8-132 6.98e-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: 41.42  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285    8 PDWFPGTSLAHLPLQELVDRGIRALVLDVDRTLLPRRQAT-MPLQAEVwLRHARER-MPLHLLSNNpSRRRIGAVADTMG 85
Cdd:pfam00702  59 RDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKlYPGAAEA-LKALKERgIKVAILTGD-NPEAAEALLRLLG 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 504921285   86 LP---------YTTSAGKPRRAALRKVLQDLALPPAQVALVGDRLfTDVLVGNRMG 132
Cdd:pfam00702 137 LDdyfdvvisgDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 93-138 8.69e-05

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: 41.42  E-value: 8.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 504921285   93 GKPRRAALRKVLQDLALPPA-QVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:TIGR01459 194 GKPYPAIFHKALKECSNIPKnRMLMVGDSFYTDILGANRLGIDTALV 240
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 85-139 2.10e-04

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: 40.39  E-value: 2.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 504921285   85 GLPYTTSAGKPRRAALRKVLQDLALPPAQVAL-VGDRLFTDVLVGNRMGLFTVLVK 139
Cdd:TIGR01460 179 SGREPTVVGKPSPAIYRAALNLLQARPERRDVmVGDNLRTDILGAKNAGFDTLLVL 234
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 56-138 1.65e-03

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: 37.69  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504921285  56 LRHARERmPLHLLSNNP-------SRRRI--GAVAD---TMGlPYTTSAGKPRRAALRKVLQDLALPP-AQVALVGDRLF 122
Cdd:cd07525  135 LKAAAAR-GLPLICANPdlvvprgGKLIYcaGALAElyeELG-GEVIYFGKPHPPIYDLALARLGRPAkARILAVGDGLH 212

                         90
                 ....*....|....*.
gi 504921285 123 TDVLVGNRMGLFTVLV 138
Cdd:cd07525  213 TDILGANAAGLDSLFV 228
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 93-139 2.08e-03

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: 37.26  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 504921285  93 GKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLVK 139
Cdd:cd07509  171 GKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVR 217
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 93-138 3.42e-03

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: 36.90  E-value: 3.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 504921285  93 GKPRRAALRKVLQDLALPPAQVALVGDRLFTDVLVGNRMGLFTVLV 138
Cdd:cd07532  205 GKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFANNCGFQSLLV 250
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 94-140 3.54e-03

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: 36.23  E-value: 3.54e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 504921285  94 KPRRAALRKVLQDLALPPAQVALVGDRLfTDVLVGNRMGLFTVLVKP 140
Cdd:COG0241  102 KPKPGMLLQAAERLGIDLSNSYMIGDRL-SDLQAAKAAGCKGILVLT 147
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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