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Conserved domains on  [gi|488258061|ref|WP_002329269|]
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MULTISPECIES: HAD-IA family hydrolase [Enterococcus]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 3-177 7.01e-56

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd07523:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 173  Bit Score: 174.87  E-value: 7.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   3 NYIWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINESNlDANEFNEWFHRYEKKSKEASRPFPE 82
Cdd:cd07523    1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYA-EVPDLEEEYKELEAEYLAKPILFPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  83 TKQVLESLKINEGRHFILTHRlTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIGDRRL 162
Cdd:cd07523   80 AKAVLRWIKEQGGKNFLMTHR-DHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIGDREL 158

                        170
                 ....*....|....*
gi 488258061 163 DIEAGKNAGVVTCLY 177
Cdd:cd07523  159 DIEAGHNAGISTILF 173
 
Name Accession Description Interval E-value
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 3-177 7.01e-56

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


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 174.87  E-value: 7.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   3 NYIWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINESNlDANEFNEWFHRYEKKSKEASRPFPE 82
Cdd:cd07523    1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYA-EVPDLEEEYKELEAEYLAKPILFPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  83 TKQVLESLKINEGRHFILTHRlTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIGDRRL 162
Cdd:cd07523   80 AKAVLRWIKEQGGKNFLMTHR-DHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIGDREL 158

                        170
                 ....*....|....*
gi 488258061 163 DIEAGKNAGVVTCLY 177
Cdd:cd07523  159 DIEAGHNAGISTILF 173
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1-201 1.18e-41

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 140.06  E-value: 1.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   1 MKNYIWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINES-NLDANE-----FNEWFHRYEKKSK 74
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLlGEDPDEeleelLARFRELYEEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  75 EASRPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDT 154
Cdd:COG0546   81 DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488258061 155 MMIGDRRLDIEAGKNAGV----VTCLYDIDHFLGEIPADHVVGNLNEILSL 201
Cdd:COG0546  161 LMVGDSPHDIEAARAAGVpfigVTWGYGSAEELEAAGADYVIDSLAELLAL 211
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
4-172 8.24e-28

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 103.43  E-value: 8.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061    4 YIWDFDGTLFDTYPAMVDGAQQALKDFG-INMDKKEIYFKMK---KYSTSYLINESNLDANeFNEWFHRYEKKSKEAS-R 78
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGlplREIFRYLGVSEDEEEK-IEFYLRKYNEELHDKLvK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   79 PFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIG 158
Cdd:pfam13419  80 PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVG 159

                         170
                  ....*....|....
gi 488258061  159 DRRLDIEAGKNAGV 172
Cdd:pfam13419 160 DSPRDIEAAKNAGI 173
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
7-201 6.78e-22

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 89.10  E-value: 6.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   7 DFDGTLFDTYPAMVDGAQQALKDFGI-NMDKKEIyfkmkkysTSY-------LI------NESNLDANEF----NEWFHR 68
Cdd:PRK13222  12 DLDGTLVDSAPDLAAAVNAALAALGLpPAGEERV--------RTWvgngadvLVeraltwAGREPDEELLeklrELFDRH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  69 YEKKSKEASRPFPETKQVLESLKineGRHFIL---THRLTESTWELLKEYQLAHLIEEVVGIDqDFP-RKPNPASLNYLI 144
Cdd:PRK13222  84 YAENVAGGSRLYPGVKETLAALK---AAGYPLavvTNKPTPFVAPLLEALGIADYFSVVIGGD-SLPnKKPDPAPLLLAC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488258061 145 DTFHLERTDTMMIGDRRLDIEAGKNAGV----VTCLYDIDHFLGEIPADHVVGNLNEILSL 201
Cdd:PRK13222 160 EKLGLDPEEMLFVGDSRNDIQAARAAGCpsvgVTYGYNYGEPIALSEPDVVIDHFAELLPL 220
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 4-171 3.07e-14

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 67.42  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061    4 YIWDFDGTLFDTYPAMVDGAQQALKDFGINM-DKKEIYFKMKKYSTS-YLINESNLDAnEFNEWFHRYEKKSKEasrpFP 81
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPaSFKALKQAGGLAEEEwYRIATSALEE-LQGRFWSEYDAEEAY----IR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   82 ETKQVLESLKINEGRHFILTHRLTESTwELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLErTDTMMIGDRR 161
Cdd:TIGR01549  77 GAADLLARLKSAGIKLGIISNGSLRAQ-KLLLRLFGLGDYFELILVSDEPGSKPEPEIFLAALESLGVP-PEVLHVGDNL 154

                         170
                  ....*....|
gi 488258061  162 LDIEAGKNAG 171
Cdd:TIGR01549 155 NDIEGARNAG 164
 
Name Accession Description Interval E-value
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 3-177 7.01e-56

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


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 174.87  E-value: 7.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   3 NYIWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINESNlDANEFNEWFHRYEKKSKEASRPFPE 82
Cdd:cd07523    1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYA-EVPDLEEEYKELEAEYLAKPILFPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  83 TKQVLESLKINEGRHFILTHRlTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIGDRRL 162
Cdd:cd07523   80 AKAVLRWIKEQGGKNFLMTHR-DHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIGDREL 158

                        170
                 ....*....|....*
gi 488258061 163 DIEAGKNAGVVTCLY 177
Cdd:cd07523  159 DIEAGHNAGISTILF 173
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1-201 1.18e-41

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 140.06  E-value: 1.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   1 MKNYIWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINES-NLDANE-----FNEWFHRYEKKSK 74
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLlGEDPDEeleelLARFRELYEEELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  75 EASRPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDT 154
Cdd:COG0546   81 DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488258061 155 MMIGDRRLDIEAGKNAGV----VTCLYDIDHFLGEIPADHVVGNLNEILSL 201
Cdd:COG0546  161 LMVGDSPHDIEAARAAGVpfigVTWGYGSAEELEAAGADYVIDSLAELLAL 211
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
4-172 8.24e-28

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 103.43  E-value: 8.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061    4 YIWDFDGTLFDTYPAMVDGAQQALKDFG-INMDKKEIYFKMK---KYSTSYLINESNLDANeFNEWFHRYEKKSKEAS-R 78
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGlplREIFRYLGVSEDEEEK-IEFYLRKYNEELHDKLvK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   79 PFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIG 158
Cdd:pfam13419  80 PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVG 159

                         170
                  ....*....|....
gi 488258061  159 DRRLDIEAGKNAGV 172
Cdd:pfam13419 160 DSPRDIEAAKNAGI 173
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 1-201 1.81e-24

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: 95.87  E-value: 1.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   1 MKNYIWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIY-------------FKMKKYSTSYLINE--SNLDANEFNEW 65
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAeayraieyalwrrYERGEITFAELLRRllEELGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  66 FHRYEKKSKEASRPFPETKQVLESLKINEGRHFILT--HRltESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYL 143
Cdd:COG1011   81 AEAFLAALPELVEPYPDALELLEALKARGYRLALLTngSA--ELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488258061 144 IDTFHLERTDTMMIGDR-RLDIEAGKNAGVVTCLYD--IDHFLGEIPADHVVGNLNEILSL 201
Cdd:COG1011  159 LERLGVPPEEALFVGDSpETDVAGARAAGMRTVWVNrsGEPAPAEPRPDYVISDLAELLEL 219
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
7-201 6.78e-22

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 89.10  E-value: 6.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   7 DFDGTLFDTYPAMVDGAQQALKDFGI-NMDKKEIyfkmkkysTSY-------LI------NESNLDANEF----NEWFHR 68
Cdd:PRK13222  12 DLDGTLVDSAPDLAAAVNAALAALGLpPAGEERV--------RTWvgngadvLVeraltwAGREPDEELLeklrELFDRH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  69 YEKKSKEASRPFPETKQVLESLKineGRHFIL---THRLTESTWELLKEYQLAHLIEEVVGIDqDFP-RKPNPASLNYLI 144
Cdd:PRK13222  84 YAENVAGGSRLYPGVKETLAALK---AAGYPLavvTNKPTPFVAPLLEALGIADYFSVVIGGD-SLPnKKPDPAPLLLAC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488258061 145 DTFHLERTDTMMIGDRRLDIEAGKNAGV----VTCLYDIDHFLGEIPADHVVGNLNEILSL 201
Cdd:PRK13222 160 EKLGLDPEEMLFVGDSRNDIQAARAAGCpsvgVTYGYNYGEPIALSEPDVVIDHFAELLPL 220
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 5-199 6.64e-21

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 86.13  E-value: 6.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   5 IWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEiyfKMKKY-------------STSYLINESNLDANEFNEWFHR-YE 70
Cdd:cd16417    3 AFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEE---TVRTWigngadvlveralTGAREAEPDEELFKEARALFDRhYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  71 KKSKEASRPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDqDFP-RKPNPASLNYLIDTFHL 149
Cdd:cd16417   80 ETLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGD-SLPeKKPDPAPLLHACEKLGI 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488258061 150 ERTDTMMIGDRRLDIEAGKNAGV-VTCL-----YDIDhfLGEIPADHVVGNLNEIL 199
Cdd:cd16417  159 APAQMLMVGDSRNDILAARAAGCpSVGLtygynYGED--IAASGPDAVIDSLAELL 212
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 1-171 1.16e-18

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: 79.94  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061    1 MKNYIWDFDGTLFDTYPAMVDGAQQALKDF----GINMDKKEIYFKMKKYSTSYLINESNLDANEFNEWFHRYEKKSK-- 74
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHplakAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEgl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   75 --------------EASRPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASL 140
Cdd:pfam00702  81 tvvlvellgvialaDELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 488258061  141 NYLIDTFHLERTDTMMIGDRRLDIEAGKNAG 171
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 2-201 4.80e-17

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 75.78  E-value: 4.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   2 KNYIWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINESNLD-ANEFNEWFHRYEKKSKEA-SRP 79
Cdd:cd02616    2 TTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGPPLRETFEKIDPDkLEDMVEEFRKYYREHNDDlTKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  80 FPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIGD 159
Cdd:cd02616   82 YPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEALMVGD 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488258061 160 RRLDIEAGKNAGVVTCL----YDIDHFLGEIPADHVVGNLNEILSL 201
Cdd:cd02616  162 SPHDILAGKNAGVKTVGvtwgYKGREYLKAFNPDFIIDKMSDLLTI 207
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 5-178 4.04e-15

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


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 70.81  E-value: 4.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   5 IWDFDGTLFDTYPAMVDGAQQALKDFGIN-MDKKEIyfkmkkysTSY-------LIN------ESNLDANEFNEWFHR-- 68
Cdd:cd07512    3 IFDLDGTLIDSAPDLHAALNAVLAAEGLApLSLAEV--------RSFvghgapaLIRrafaaaGEDLDGPLHDALLARfl 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  69 --YEKKSKEASRPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDqDFP-RKPNPASLNYLID 145
Cdd:cd07512   75 dhYEADPPGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGD-TLPqRKPDPAPLRAAIR 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488258061 146 TFHLERTDTMMIGDRRLDIEAGKNAGVVTCLYD 178
Cdd:cd07512  154 RLGGDVSRALMVGDSETDAATARAAGVPFVLVT 186
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 4-171 3.07e-14

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 67.42  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061    4 YIWDFDGTLFDTYPAMVDGAQQALKDFGINM-DKKEIYFKMKKYSTS-YLINESNLDAnEFNEWFHRYEKKSKEasrpFP 81
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPaSFKALKQAGGLAEEEwYRIATSALEE-LQGRFWSEYDAEEAY----IR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   82 ETKQVLESLKINEGRHFILTHRLTESTwELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLErTDTMMIGDRR 161
Cdd:TIGR01549  77 GAADLLARLKSAGIKLGIISNGSLRAQ-KLLLRLFGLGDYFELILVSDEPGSKPEPEIFLAALESLGVP-PEVLHVGDNL 154

                         170
                  ....*....|
gi 488258061  162 LDIEAGKNAG 171
Cdd:TIGR01549 155 NDIEGARNAG 164
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
5-198 3.11e-14

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 68.31  E-value: 3.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   5 IWDFDGTLFDTYPAMVDGAQQALKDFGINMDkKEIYFKMK----KYSTSYLINESNLD------ANEFNEWFHryEKKSK 74
Cdd:COG0637    6 IFDMDGTLVDSEPLHARAWREAFAELGIDLT-EEEYRRLMgrsrEDILRYLLEEYGLDlpeeelAARKEELYR--ELLAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  75 EASRPFPETKQVLESLKiNEGRHFIL----THRLTEstwELLKEYQLAHLIEEVVGIDqDFPR-KPNPASlnYL--IDTF 147
Cdd:COG0637   83 EGLPLIPGVVELLEALK-EAGIKIAVatssPRENAE---AVLEAAGLLDYFDVIVTGD-DVARgKPDPDI--YLlaAERL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488258061 148 HLERTDTMMIGDRRLDIEAGKNAG----VVTCLYDIDHFLGEipADHVVGNLNEI 198
Cdd:COG0637  156 GVDPEECVVFEDSPAGIRAAKAAGmrvvGVPDGGTAEEELAG--ADLVVDDLAEL 208
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 83-177 1.24e-12

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: 61.64  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  83 TKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIGDRRL 162
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                         90
                 ....*....|....*
gi 488258061 163 DIEAGKNAGVVTCLY 177
Cdd:cd01427   92 DIEAARAAGGRTVAV 106
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 3-201 3.95e-11

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


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 59.91  E-value: 3.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   3 NYIWDFDGTLFDTYPAMVDGAQQALKDFGIN-MDKKEIYFKMK---KYSTSYLINESNLDANEFNEWFH-RYEKKSKEAS 77
Cdd:cd04302    1 TILFDLDGTLTDSAEGITASVQYALEELGIPvPDESELRRFIGpplEDSFRELLPFDEEEAQRAVDAYReYYKEKGLFEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  78 RPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMI 157
Cdd:cd04302   81 EVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAVMI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488258061 158 GDRRLDIEAGKNAGV----VTCLYDIDHFLGEIPADHVVGNLNEILSL 201
Cdd:cd04302  161 GDRKHDIIGARANGIdsigVLYGYGSEDELEEAGATYIVETPAELLEL 208
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 2-199 6.66e-11

HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 59.34  E-value: 6.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061    2 KNYIWDFDGTLFDTYPAMVDGAQQA---LKDFGINMDKKEIYFKMKK----------YSTSYLINESNLDAN-----EFN 63
Cdd:TIGR02253   3 KAIFFDLDDTLIDTSGLAEKARRNAievLIEAGLNVDFEEAYEELLKlikeygsnypTHFDYLIRRLWEEYNpklvaAFV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   64 EWFHRYEKKSkeaSRPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVgIDQDFP-RKPNPASLNY 142
Cdd:TIGR02253  83 YAYHKLKFAY---LRVYPGVRDTLMELRESGYRLGIITDGLPVKQWEKLERLGVRDFFDAVI-TSEEEGvEKPHPKIFYA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488258061  143 LIDTFHLERTDTMMIGDR-RLDIEAGKNAGVVTCLYD----IDHFLGEIP-ADHVVGNLNEIL 199
Cdd:TIGR02253 159 ALKRLGVKPEEAVMVGDRlDKDIKGAKNAGMKTVWINqgksSKMEDDVYPyPDYEISSLRELL 221
Hydrolase_like pfam13242
HAD-hyrolase-like;
133-197 1.22e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 55.31  E-value: 1.22e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488258061  133 RKPNPASLNYLIDTFHLERTDTMMIGDRRL-DIEAGKNAGVVTCLY--------DIDHFlgEIPADHVVGNLNE 197
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVltgvtrpaDLEKA--PIRPDYVVDDLAE 74
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 5-200 4.75e-10

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


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 56.60  E-value: 4.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   5 IWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINESNLDANEFnEWFHRYEKKSKEASRP----F 80
Cdd:cd04303    3 IFDFDGTLADSFPWFLSILNQLAARHGFKTVDEEEIEQLRQLSSREILKQLGVPLWKL-PLIAKDFRRLMAEAAPelalF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  81 PETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQdFPRkpnPASLNYLIDTFHLERTDTMMIGDR 160
Cdd:cd04303   82 PGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFAVIEGSSL-FGK---AKKIRRVLRRTKITAAQVIYVGDE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488258061 161 RLDIEAGKNAGV----VTCLYDIDHFLGEIPADHVVGNLNEILS 200
Cdd:cd04303  158 TRDIEAARKVGLafaaVSWGYAKPEVLKALAPDHMLEDPEDLIQ 201
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 80-177 4.88e-10

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 54.86  E-value: 4.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  80 FPETKQVLESLKiNEGRHFILTHRLTESTWELLKEYQLAHLIEEVVgIDQDFP-RKPNPASLNYLIDTFHLERTDTMMIG 158
Cdd:cd04305   11 LPGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIV-ISEEVGvQKPNPEIFDYALNQLGVKPEETLMVG 88

                         90       100
                 ....*....|....*....|
gi 488258061 159 DR-RLDIEAGKNAGVVTCLY 177
Cdd:cd04305   89 DSlESDILGAKNAGIKTVWF 108
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
117-199 1.76e-09

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 55.89  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061 117 LAHLIEEVVGIDqdfPR---KPNPASLNYLIDTFHLERTDTMMIGDR-RLDIEAGKNAGVVTCL--------YDIDHFlg 184
Cdd:COG0647  169 LAAALEAATGGE---PLvvgKPSPPIYELALERLGVDPERVLMVGDRlDTDILGANAAGLDTLLvltgvttaEDLEAA-- 243

                         90
                 ....*....|....*
gi 488258061 185 EIPADHVVGNLNEIL 199
Cdd:COG0647  244 PIRPDYVLDSLAELL 258
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 5-177 2.07e-09

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 54.73  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061    5 IWDFDGTLFDTYPAMVDGAQQA---------LKDFGINMDKKEIYFKMKKYSTSYLINESNLDANEFNEWFHRYEKkske 75
Cdd:TIGR01509   3 LFDLDGVLVDTEFAIAKLINREelglvpdelGVSAVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQIEEEAK---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   76 aSRPFPETKQVLESLKINEGRHFILT--HRLTESTWELLKeyqLAHLIEEVVgIDQDFPR-KPNPASLNYLIDTFHLERT 152
Cdd:TIGR01509  79 -LKPLPGVRALLEALRARGKKLALLTnsPRAHKLVLALLG---LRDLFDVVI-DSSDVGLgKPDPDIYLQALKALGLEPS 153

                         170       180
                  ....*....|....*....|....*
gi 488258061  153 DTMMIGDRRLDIEAGKNAGVVTCLY 177
Cdd:TIGR01509 154 ECVFVDDSPAGIEAAKAAGMHTVGV 178
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 133-198 2.80e-09

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: 53.95  E-value: 2.80e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488258061 133 RKPNPASLNYLIDTFHLERTDTMMIGDRRLDIEAGKNAGVVTCLYDIDH---FLGEIPADHVVGNLNEI 198
Cdd:COG0241  101 RKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKgaeELAEALPDTVADDLAEA 169
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 5-198 2.49e-08

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: 52.02  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   5 IWDFDGTLFDTYPAMVDGAQQALKDFG------------INMDKKEIYFKMKKYSTSYLINesnlDANEFNEWFHRYEKK 72
Cdd:cd07533    3 IFDWDGTLADSQHNIVAAMTAAFADLGlpvpsaaevrsiIGLSLDEAIARLLPMATPALVA----VAERYKEAFDILRLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  73 SKEASRPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDqDFPRKPNPASLNYLIDTFHLERT 152
Cdd:cd07533   79 PEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTAD-DTPSKPHPEMLREILAELGVDPS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488258061 153 DTMMIGDRRLDIEAGKNAGV----VTCLYDIDHFLGEIPADHVVGNLNEI 198
Cdd:cd07533  158 RAVMVGDTAYDMQMAANAGAhavgVAWGYHSLEDLRSAGADAVVDHFSEL 207
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 117-197 3.21e-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: 52.21  E-value: 3.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061 117 LAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIGDR-RLDIEAGKNAGV--------VTCLYDIDHFlgEIP 187
Cdd:cd07530  160 VVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRlDTDIAAGIAAGIdtllvltgVTTREDLAKP--PYR 237

                         90
                 ....*....|
gi 488258061 188 ADHVVGNLNE 197
Cdd:cd07530  238 PTYIVPSLRE 247
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 133-177 4.44e-08

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: 50.22  E-value: 4.44e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488258061 133 RKPNPASLNYLIDTFHLERTDTMMIGDRRLDIEAGKNAGVVTCLY 177
Cdd:cd07503   98 RKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 5-175 3.97e-07

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 48.49  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   5 IWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINEsnLDANEFNEWFHRY----EKKSKEASRPF 80
Cdd:PRK13288   7 LFDLDGTLINTNELIISSFLHTLKTYYPNQYKREDVLPFIGPSLHDTFSK--IDESKVEEMITTYrefnHEHHDELVTEY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  81 PETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIGDR 160
Cdd:PRK13288  85 ETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKPEEALMVGDN 164

                        170
                 ....*....|....*
gi 488258061 161 RLDIEAGKNAGVVTC 175
Cdd:PRK13288 165 HHDILAGKNAGTKTA 179
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 1-173 4.00e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 46.24  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   1 MKNYIWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINESNLDANEFNEWFHRYEKKSKE---AS 77
Cdd:PRK13225  62 LQAIIFDFDGTLVDSLPTVVAIANAHAPDFGYDPIDERDYAQLRQWSSRTIVRRAGLSPWQQARLLQRVQRQLGDclpAL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  78 RPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVvgiDQDFPRKPNPASLNYLIDTFHLERTDTMMI 157
Cdd:PRK13225 142 QLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQRQGLRSLFSVV---QAGTPILSKRRALSQLVAREGWQPAAVMYV 218

                        170
                 ....*....|....*.
gi 488258061 158 GDRRLDIEAGKNAGVV 173
Cdd:PRK13225 219 GDETRDVEAARQVGLI 234
PLN02645 PLN02645
phosphoglycolate phosphatase
 124-176 1.18e-05

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 44.70  E-value: 1.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488258061 124 VVGidqdfprKPNPASLNYLIDTFHLERTDTMMIGDR-RLDIEAGKNAGVVTCL 176
Cdd:PLN02645 227 VVG-------KPSTFMMDYLANKFGIEKSQICMVGDRlDTDILFGQNGGCKTLL 273
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 5-199 2.60e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 43.70  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   5 IWDFDGTLFDTYPAMVDGAQQALKDFGINMDKKEIYFKMKKYSTSYLINES---NLDANEFN--------EWFHRYEKKS 73
Cdd:PRK13223  17 MFDLDGTLVDSVPDLAAAVDRMLLELGRPPAGLEAVRHWVGNGAPVLVRRAlagSIDHDGVDdelaeqalALFMEAYADS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  74 KEASRPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTD 153
Cdd:PRK13223  97 HELTVVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMAGVPPSQ 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488258061 154 TMMIGDRRLDIEAGKNAGV--VTCLYDIDH---FLGEIPAdHVVGNLNEIL 199
Cdd:PRK13223 177 SLFVGDSRSDVLAAKAAGVqcVALSYGYNHgrpIAEESPA-LVIDDLRALL 226
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 78-198 2.61e-05

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 43.41  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  78 RPFPETKQVLESLKineGRHFILThRLTESTWELLKEYQ----LAHLIEEVVGIDQdfPR--KPNPASLNYLIDTFHLER 151
Cdd:cd02588   91 PPFPDVVAGLRRLR---EAGYRLA-ILSNGSPDLIEDVVanagLRDLFDAVLSAED--VRayKPAPAVYELAAERLGVPP 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488258061 152 TDTMMIGDRRLDIEAGKNAGVVTCLYDIDH----FLGEIPaDHVVGNLNEI 198
Cdd:cd02588  165 DEILHVASHAWDLAGARALGLRTAWINRPGevpdPLGPAP-DFVVPDLGEL 214
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 134-176 1.45e-04

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: 41.27  E-value: 1.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488258061 134 KPNPASLNYLIDTFHLERTDTMMIGDR-RLDIEAGKNAGVVTCL 176
Cdd:cd16422  177 KPNPIILDPVLEKFDYSKEETVMVGDRlYTDIVLGINAGVDSIL 220
PRK09449 PRK09449
dUMP phosphatase; Provisional
 75-201 3.91e-04

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 39.88  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  75 EASRPFPETKQVLESL--KINEGrhfILTHRLTESTWELLKEYQLAH-----LIEEVVGIdqdfpRKPNPASLNYLIDTF 147
Cdd:PRK09449  92 EICTPLPGAVELLNALrgKVKMG---IITNGFTELQQVRLERTGLRDyfdllVISEQVGV-----AKPDVAIFDYALEQM 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061 148 -HLERTDTMMIGDR-RLDIEAGKNAGVVTCLYDIDHflGEIPAD----HVVGNLNEILSL 201
Cdd:PRK09449 164 gNPDRSRVLMVGDNlHSDILGGINAGIDTCWLNAHG--REQPEGiaptYQVSSLSELEQL 221
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
133-176 4.16e-04

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 39.34  E-value: 4.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488258061 133 RKPNPASLNYLIDTFHLERTDTMMIGDRRL-DIEAGKNAGVVTCL 176
Cdd:COG2179   90 KKPLPRGFRKALKLMGLPPEETAVVGDQLFtDVLGGNRAGLYTIL 134
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
133-176 5.18e-04

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 39.42  E-value: 5.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488258061 133 RKPNPASLNYLIDTFHLERTDTMMIGDRRLDIEAGKNAGVVTCL 176
Cdd:PRK08942 102 RKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVL 145
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 133-173 6.11e-04

histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.


Pssm-ID: 273737  Cd Length: 147  Bit Score: 38.53  E-value: 6.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 488258061  133 RKPNPASLNYLIDTFHLERTDTMMIGDRRLDIEAGKNAGVV 173
Cdd:TIGR01656 100 RKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAA 140
PRK06769 PRK06769
HAD-IIIA family hydrolase;
80-197 9.77e-04

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 38.56  E-value: 9.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061  80 FPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLieEVVGIDQDF--P---------RKPNPASLNYLIDTFH 148
Cdd:PRK06769  30 FPFTKASLQKLKANHIKIFSFTNQPGIADGIATIADFVQEL--KGFGFDDIYlcPhkhgdgcecRKPSTGMLLQAAEKHG 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488258061 149 LERTDTMMIGDRRLDIEAGKNAGVVTCL------YDIDHF----LGEIPADHVVGNLNE 197
Cdd:PRK06769 108 LDLTQCAVIGDRWTDIVAAAKVNATTILvrtgagYDALHTyrdkWAHIEPNYIAENFED 166
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 133-176 1.04e-03

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: 37.25  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488258061 133 RKPNPASLNYLIDTFHLERTDTMMIGDRRL-DIEAGKNAGVVTCL 176
Cdd:cd16416   63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFtDILGGNRAGLYTIL 107
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 117-176 1.40e-03

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: 38.46  E-value: 1.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488258061  117 LAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTM-MIGDR-RLDIEAGKNAGVVTCL 176
Cdd:TIGR01460 171 IAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRDvMVGDNlRTDILGAKNAGFDTLL 232
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 134-176 2.53e-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: 37.67  E-value: 2.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488258061 134 KPNPASLNYLIDTFHLERTDTMMIGDR-RLDIEAGKNAGVVTCL 176
Cdd:cd07532  206 KPNPQILNFLMKSGVIKPERTLMIGDRlKTDILFANNCGFQSLL 249
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 134-176 2.67e-03

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: 37.75  E-value: 2.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488258061 134 KPNPASLNYLIDTFHLERTDTMMIGDR-RLDIEAGKNAGVVTCL 176
Cdd:cd07510  204 KPSRFMFDCISSKFSIDPARTCMVGDRlDTDILFGQNCGLKTLL 247
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 78-175 3.00e-03

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


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 37.32  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488258061   78 RPFPETKQVLESLKINEGRHFILTHRLTESTWELLKEYQLAHLIEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMI 157
Cdd:TIGR01428  92 PPHPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQLALEALGVPPDEVLFV 171

                          90
                  ....*....|....*...
gi 488258061  158 GDRRLDIEAGKNAGVVTC 175
Cdd:TIGR01428 172 ASNPWDLGGAKKFGFKTA 189
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 99-175 7.60e-03

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 34.74  E-value: 7.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488258061  99 ILTHRLTESTWELLKEYQLAHLiEEVVGIDQDFPRKPNPASLNYLIDTFHLERTDTMMIGDRRLDIEAGKNAGVVTC 175
Cdd:cd16421   28 VLSNKPNEAVQVLVEELFPGSF-DFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQTARNAGMDEI 103
 
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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