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Conserved domains on  [gi|446137853|ref|WP_000215708|]
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MULTISPECIES: HAD family hydrolase [Leptospira]

Protein Classification

HAD family hydrolase( domain architecture ID 11425524)

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

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|7966317

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
9-224 8.04e-41

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


:

Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 138.52  E-value: 8.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   9 LQALAFDVDGTLFSSEGIILEVYRDSILNFsktsgiQIELPSRDRIMAEIGKPVKTIFFNLLPQLNEEQRDSISDSVLRF 88
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAEL------GLPPLDLEELRALIGLGLRELLRRLLGEDPDEELEELLARFREL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  89 LCDRIKKgEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDN-KRIRTKAEILEEYIKLY 167
Cdd:COG0546   75 YEEELLD-ETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDvPPAKPKPEPLLEALERL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446137853 168 HLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEIPDF--DLKLKNISDLNEVL 224
Cdd:COG0546  154 GLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAgaDYVIDSLAELLALL 212
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
9-224 8.04e-41

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 138.52  E-value: 8.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   9 LQALAFDVDGTLFSSEGIILEVYRDSILNFsktsgiQIELPSRDRIMAEIGKPVKTIFFNLLPQLNEEQRDSISDSVLRF 88
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAEL------GLPPLDLEELRALIGLGLRELLRRLLGEDPDEELEELLARFREL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  89 LCDRIKKgEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDN-KRIRTKAEILEEYIKLY 167
Cdd:COG0546   75 YEEELLD-ETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDvPPAKPKPEPLLEALERL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446137853 168 HLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEIPDF--DLKLKNISDLNEVL 224
Cdd:COG0546  154 GLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAgaDYVIDSLAELLALL 212
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 14-207 4.74e-22

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: 89.57  E-value: 4.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  14 FDVDGTLF-SSEGIIlevyrDSI---LNFsktsgIQIELPSRDRIMAEIGKPVKTIFFNLLPqlneEQRDSISDSVLRFL 89
Cdd:cd04302    4 FDLDGTLTdSAEGIT-----ASVqyaLEE-----LGIPVPDESELRRFIGPPLEDSFRELLP----FDEEEAQRAVDAYR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  90 CDRIKKG--EGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPIL--VLDNKRiRTKAEILEEYIK 165
Cdd:cd04302   70 EYYKEKGlfENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAgaSLDGSR-VHKADVIRYALD 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446137853 166 LYHLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEI 207
Cdd:cd04302  149 TLGIAPEQAVMIGDRKHDIIGARANGIDSIGVLYGYGSEDEL 190
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 7-224 7.97e-21

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 90.07  E-value: 7.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   7 ESLQALAFDVDGTLFSSEGIiLEVYRDSILNFSKTSGIQIELPSRDRIMAEIGKPVKTIFFNLLPQLNEEQRDSISDSVL 86
Cdd:PRK06698 239 EMLQALIFDMDGTLFQTDKI-LELSLDDTFDHLRSLQLWDTVTPIDKYREIMGVPLPKVWEALLPDHSLEIREQTDAYFL 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  87 RFLCDRIKKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRIRTKAEILEEYIKL 166
Cdd:PRK06698 318 ERLIENIKSGKGALYPNVKEIFTYIKENNCSIYIASNGLTEYLRAIVSYYDLDQWVTETFSIEQINSLNKSDLVKSILNK 397

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446137853 167 YHLKpnQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEIPDFDLKLKNISDLNEVL 224
Cdd:PRK06698 398 YDIK--EAAVVGDRLSDINAAKDNGLIAIGCNFDFAQEDELAQADIVIDDLLELKGIL 453
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 9-191 1.36e-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: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853    9 LQALAFDVDGTLFSSEGIILEVYRDSILNFSKTSGIQIELPSRDRIMAEIGKPVK----------TIFFNLLPQLNEEQR 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLlgkrdwleelDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   79 DSISDSVLRFLcdrIKKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRIR-TKA 157
Cdd:pfam00702  81 TVVLVELLGVI---ALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGkPKP 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 446137853  158 EILEEYIKLYHLKPNQILMIGDRLSDHEAARQNG 191
Cdd:pfam00702 158 EIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 11-188 1.47e-08

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: 52.40  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   11 ALAFDVDGTLFSSEGIILEVYRDsILNFSKTSGIQIELPSRDRIMAEigkpvktiffnllpQLNEEQRDSISDSVLRFLC 90
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQ-TFEEFGLDPASFKALKQAGGLAE--------------EEWYRIATSALEELQGRFW 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   91 DRIKKGEgEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDnkRIRTKAEILEEYIKLYHLK 170
Cdd:TIGR01549  66 SEYDAEE-AYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSD--EPGSKPEPEIFLAALESLG 142

                         170
                  ....*....|....*....
gi 446137853  171 -PNQILMIGDRLSDHEAAR 188
Cdd:TIGR01549 143 vPPEVLHVGDNLNDIEGAR 161
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
9-224 8.04e-41

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 138.52  E-value: 8.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   9 LQALAFDVDGTLFSSEGIILEVYRDSILNFsktsgiQIELPSRDRIMAEIGKPVKTIFFNLLPQLNEEQRDSISDSVLRF 88
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAEL------GLPPLDLEELRALIGLGLRELLRRLLGEDPDEELEELLARFREL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  89 LCDRIKKgEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDN-KRIRTKAEILEEYIKLY 167
Cdd:COG0546   75 YEEELLD-ETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDvPPAKPKPEPLLEALERL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446137853 168 HLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEIPDF--DLKLKNISDLNEVL 224
Cdd:COG0546  154 GLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAgaDYVIDSLAELLALL 212
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 14-207 4.74e-22

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: 89.57  E-value: 4.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  14 FDVDGTLF-SSEGIIlevyrDSI---LNFsktsgIQIELPSRDRIMAEIGKPVKTIFFNLLPqlneEQRDSISDSVLRFL 89
Cdd:cd04302    4 FDLDGTLTdSAEGIT-----ASVqyaLEE-----LGIPVPDESELRRFIGPPLEDSFRELLP----FDEEEAQRAVDAYR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  90 CDRIKKG--EGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPIL--VLDNKRiRTKAEILEEYIK 165
Cdd:cd04302   70 EYYKEKGlfENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAgaSLDGSR-VHKADVIRYALD 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446137853 166 LYHLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEI 207
Cdd:cd04302  149 TLGIAPEQAVMIGDRKHDIIGARANGIDSIGVLYGYGSEDEL 190
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 7-224 7.97e-21

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 90.07  E-value: 7.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   7 ESLQALAFDVDGTLFSSEGIiLEVYRDSILNFSKTSGIQIELPSRDRIMAEIGKPVKTIFFNLLPQLNEEQRDSISDSVL 86
Cdd:PRK06698 239 EMLQALIFDMDGTLFQTDKI-LELSLDDTFDHLRSLQLWDTVTPIDKYREIMGVPLPKVWEALLPDHSLEIREQTDAYFL 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  87 RFLCDRIKKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRIRTKAEILEEYIKL 166
Cdd:PRK06698 318 ERLIENIKSGKGALYPNVKEIFTYIKENNCSIYIASNGLTEYLRAIVSYYDLDQWVTETFSIEQINSLNKSDLVKSILNK 397

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446137853 167 YHLKpnQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEIPDFDLKLKNISDLNEVL 224
Cdd:PRK06698 398 YDIK--EAAVVGDRLSDINAAKDNGLIAIGCNFDFAQEDELAQADIVIDDLLELKGIL 453
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 10-224 4.07e-19

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: 82.00  E-value: 4.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  10 QALAFDVDGTLFSSEGIILEVYRdsilnfsKTSGIQIELPSRDRIMAEI--------------GKPVKTIFFNLLPQLNE 75
Cdd:COG1011    2 KAVLFDLDGTLLDFDPVIAEALR-------ALAERLGLLDEAEELAEAYraieyalwrryergEITFAELLRRLLEELGL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  76 EQRDSISDSVLRFLCDRIkkgegEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRIRt 155
Cdd:COG1011   75 DLAEELAEAFLAALPELV-----EPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVR- 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446137853 156 K--AEILEEYIKLYHLKPNQILMIGDRL-SDHEAARQNGCPFAFCSYGHAPEGEIPDFDLKLKNISDLNEVL 224
Cdd:COG1011  149 KpdPEIFELALERLGVPPEEALFVGDSPeTDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 9-191 1.36e-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: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853    9 LQALAFDVDGTLFSSEGIILEVYRDSILNFSKTSGIQIELPSRDRIMAEIGKPVK----------TIFFNLLPQLNEEQR 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLlgkrdwleelDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   79 DSISDSVLRFLcdrIKKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRIR-TKA 157
Cdd:pfam00702  81 TVVLVELLGVI---ALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGkPKP 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 446137853  158 EILEEYIKLYHLKPNQILMIGDRLSDHEAARQNG 191
Cdd:pfam00702 158 EIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 14-210 2.68e-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: 76.93  E-value: 2.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  14 FDVDGTLF-SSEGIIlevyrDSILNFSKTSGIqiELPSRDRIMAEIGKPVKTIFFNLLPQLNEEQRDSISDSVLRFLCDR 92
Cdd:cd02616    6 FDLDGTLIdTNELII-----KSFNHTLKEYGL--EGYTREEVLPFIGPPLRETFEKIDPDKLEDMVEEFRKYYREHNDDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  93 IKkgegeFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDnkrIRTKA----EILEEYIKLYH 168
Cdd:cd02616   79 TK-----EYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGD---DVTHHkpdpEPVLKALELLG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446137853 169 LKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEI----PDF 210
Cdd:cd02616  151 AEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLkafnPDF 196
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
14-195 3.89e-16

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 73.00  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   14 FDVDGTLFSSEGIILEVYRDSILNFsktsgiQIELPSRDRIMAEIGKPVKTIFFNLLPQLNEEQrdsISDSVLRFLCDRI 93
Cdd:pfam13419   3 FDFDGTLLDTEELIIKSFNYLLEEF------GYGELSEEEILKFIGLPLREIFRYLGVSEDEEE---KIEFYLRKYNEEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   94 KKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDN-KRIRTKAEILEEYIKLYHLKPN 172
Cdd:pfam13419  74 HDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDvEGKKPDPDPILKALEQLGLKPE 153

                         170       180
                  ....*....|....*....|...
gi 446137853  173 QILMIGDRLSDHEAARQNGCPFA 195
Cdd:pfam13419 154 EVIYVGDSPRDIEAAKNAGIKVI 176
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
9-220 3.89e-15

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 71.01  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   9 LQALAFDVDGTLFSSEGIILEVYRDsilnFSKTSGIQIELPSRDRIMaeiGKPVKTIFFNLLPQLN-EEQRDSISDSVLR 87
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWRE----AFAELGIDLTEEEYRRLM---GRSREDILRYLLEEYGlDLPEEELAARKEE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  88 FLCDRIKKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEpilvldnkRIRTkAEILEE----- 162
Cdd:COG0637   75 LYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFD--------VIVT-GDDVARgkpdp 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446137853 163 --YIK---LYHLKPNQILMIGDRLSDHEAARQNGCP-FAFCSyGHAPEGEIPDFDLKLKNISDL 220
Cdd:COG0637  146 diYLLaaeRLGVDPEECVVFEDSPAGIRAAKAAGMRvVGVPD-GGTAEEELAGADLVVDDLAEL 208
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
8-224 1.02e-14

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 70.22  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   8 SLQALAFDVDGTLF-SSEGIILEVyrDSILnfsktsgIQIELP--SRDRIMAEIGKP----VKTIFFNLLPQLNEEQRDs 80
Cdd:PRK13222   5 DIRAVAFDLDGTLVdSAPDLAAAV--NAAL-------AALGLPpaGEERVRTWVGNGadvlVERALTWAGREPDEELLE- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  81 isDSVLRFLcDRIKK---GEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDN-KRIRTK 156
Cdd:PRK13222  75 --KLRELFD-RHYAEnvaGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSlPNKKPD 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853 157 AEILEEYIKLYHLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEIPDF--DLKLKNISDLNEVL 224
Cdd:PRK13222 152 PAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYNYGEPIALSepDVVIDHFAELLPLL 221
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 104-195 2.65e-11

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: 58.56  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853 104 VLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRIRT-KAEILEEYIKLYHLKPNQILMIGDRLS 182
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKpKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                         90
                 ....*....|...
gi 446137853 183 DHEAARQNGCPFA 195
Cdd:cd01427   92 DIEAARAAGGRTV 104
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 14-204 4.24e-11

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: 60.10  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  14 FDVDGTLFSSEGIILEVYRDSILNFSKtsgiqiELPSRDRIMAEIGKPVKTIFFNLLPQLNEEQRDSISDSVLRFLCDRI 93
Cdd:cd07533    4 FDWDGTLADSQHNIVAAMTAAFADLGL------PVPSAAEVRSIIGLSLDEAIARLLPMATPALVAVAERYKEAFDILRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  94 KKGEGE-FYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRIRTKAEILEEYIKLYHLKPN 172
Cdd:cd07533   78 LPEHAEpLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPSKPHPEMLREILAELGVDPS 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446137853 173 QILMIGDRLSDHEAARQNGCPFAFCSYG-HAPE 204
Cdd:cd07533  158 RAVMVGDTAYDMQMAANAGAHAVGVAWGyHSLE 190
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 11-202 3.31e-10

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


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 57.63  E-value: 3.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  11 ALAFDVDGTLFSSEGIILEvyrdsilnfsktsgiqielpSRDRIMAEIGkpvktiffnlLPQLNEEQ-RDSISDSVLRfL 89
Cdd:cd16417    1 LVAFDLDGTLVDSAPDLAE--------------------AANAMLAALG----------LPPLPEETvRTWIGNGADV-L 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  90 CDR--------------IKKGEGEF--------------YPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPK 141
Cdd:cd16417   50 VERaltgareaepdeelFKEARALFdrhyaetlsvhshlYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDY 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446137853 142 FEPILVLDnkrirTKAEILEEYIKLYH------LKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHA 202
Cdd:cd16417  130 FSLVLGGD-----SLPEKKPDPAPLLHaceklgIAPAQMLMVGDSRNDILAARAAGCPSVGLTYGYN 191
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 8-224 2.78e-09

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 55.04  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   8 SLQALAFDVDGTLFSSEGIILEVYRDSILNFSKTSgiqielPSRDRIMAEIGKPVKTIFFNLLP-----------QLNEE 76
Cdd:PRK13288   2 KINTVLFDLDGTLINTNELIISSFLHTLKTYYPNQ------YKREDVLPFIGPSLHDTFSKIDEskveemittyrEFNHE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  77 QRDSisdsvlrfLCdrikkgegEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDN-KRIRT 155
Cdd:PRK13288  76 HHDE--------LV--------TEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDvEHAKP 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446137853 156 KAEILEEYIKLYHLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAPEGEI----PDFdlKLKNISDLNEVL 224
Cdd:PRK13288 140 DPEPVLKALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVAWTIKGREYLeqykPDF--MLDKMSDLLAIV 210
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 11-188 1.47e-08

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: 52.40  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   11 ALAFDVDGTLFSSEGIILEVYRDsILNFSKTSGIQIELPSRDRIMAEigkpvktiffnllpQLNEEQRDSISDSVLRFLC 90
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQ-TFEEFGLDPASFKALKQAGGLAE--------------EEWYRIATSALEELQGRFW 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   91 DRIKKGEgEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDnkRIRTKAEILEEYIKLYHLK 170
Cdd:TIGR01549  66 SEYDAEE-AYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSD--EPGSKPEPEIFLAALESLG 142

                         170
                  ....*....|....*....
gi 446137853  171 -PNQILMIGDRLSDHEAAR 188
Cdd:TIGR01549 143 vPPEVLHVGDNLNDIEGAR 161
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 11-211 2.79e-08

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: 52.32  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  11 ALAFDVDGTLF-SSEGIIlevyrdSILNFS-KTSGIQIELPSRDRIMAEIGKP--VKTIFFNLLPQLNEEQRDSISDSVL 86
Cdd:cd07512    1 AVIFDLDGTLIdSAPDLH------AALNAVlAAEGLAPLSLAEVRSFVGHGAPalIRRAFAAAGEDLDGPLHDALLARFL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  87 -RFLCDriKKGEGEFYPNVLETIEILAQKGYRILAASNgrKPYIQT--ILEVSGILPKFEPILVLDNKRIRT-KAEILEE 162
Cdd:cd07512   75 dHYEAD--PPGLTRPYPGVIEALERLRAAGWRLAICTN--KPEAPAraLLSALGLADLFAAVVGGDTLPQRKpDPAPLRA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446137853 163 YIKLYHLKPNQILMIGDRLSDHEAARQNGCPFAFCSYG--HAPEGEIP------DFD 211
Cdd:cd07512  151 AIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGyrHAPVAELPhdavfsDFD 207
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 11-222 6.64e-08

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: 51.11  E-value: 6.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  11 ALAFDVDGTLFSSEGIILEVYRDSILNFSKTS----GIQIELPSRDRIM------AEIGKPVKTIFFNLLPQ-LNEEQRD 79
Cdd:cd02588    2 ALVFDVYGTLIDWHSGLAAAERAFPGRGEELSrlwrQKQLEYTWLVTLMgpyvdfDELTRDALRATAAELGLeLDESDLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  80 SISDSVLRFlcdrikkgegEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPIL-VLDNKRIRTKAE 158
Cdd:cd02588   82 ELGDAYLRL----------PPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLsAEDVRAYKPAPA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446137853 159 ILEEYIKLYHLKPNQILMIGDRLSDHEAARQNGCPFAFCS-YGHAPEGEIPDFDLKLKNISDLNE 222
Cdd:cd02588  152 VYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAWINrPGEVPDPLGPAPDFVVPDLGELAD 216
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 11-202 1.00e-07

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: 50.43  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  11 ALAFDVDGTLFSSEGIILEVYRD--SILNFSKTSGIQIE----LPSRDrIMAEIGKPVKTiffnlLPqlneeqrdSISDS 84
Cdd:cd04303    1 LIIFDFDGTLADSFPWFLSILNQlaARHGFKTVDEEEIEqlrqLSSRE-ILKQLGVPLWK-----LP--------LIAKD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  85 VLRFLCDRIKkgEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEpilVLDNKRIRTKAEILEEYI 164
Cdd:cd04303   67 FRRLMAEAAP--ELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFA---VIEGSSLFGKAKKIRRVL 141

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446137853 165 KLYHLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHA 202
Cdd:cd04303  142 RRTKITAAQVIYVGDETRDIEAARKVGLAFAAVSWGYA 179
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 11-192 1.10e-07

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: 50.11  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   11 ALAFDVDGTLFSSEGIILEVYRDSILNFS-----KTSGIQIELPSRdRIMAEIGKPVKTIFFNLLPQLneeqrdsisdsv 85
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREELGLVpdelgVSAVGRLELALR-RFKAQYGRTISPEDAQLLYKQ------------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   86 lRFLCDRIKKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVsGILPKFEPILVLDN-KRIRTKAEILEEYI 164
Cdd:TIGR01509  68 -LFYEQIEEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLALL-GLRDLFDVVIDSSDvGLGKPDPDIYLQAL 145

                         170       180
                  ....*....|....*....|....*...
gi 446137853  165 KLYHLKPNQILMIGDRLSDHEAARQNGC 192
Cdd:TIGR01509 146 KALGLEPSECVFVDDSPAGIEAAKAAGM 173
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 15-191 7.33e-06

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: 44.68  E-value: 7.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  15 DVDGTLFSSEGIILEVYRDSILNFsktsGIQIELPSRDRIMAEIGKPVKTIFFNLLPQLNEEqrdsisdsvlrflcdrIK 94
Cdd:cd07523    5 DLDGTLLDSYPAMTKALSETLADF----GIPQDLETVYKIIKESSVQFAIQYYAEVPDLEEE----------------YK 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  95 KGEGEF------YPNVLETIEILAQKGYRILAASNgRKPYIQTILEVSGILPKFEPILVLDNKRIRTKA-EILEEYIKLY 167
Cdd:cd07523   65 ELEAEYlakpilFPGAKAVLRWIKEQGGKNFLMTH-RDHSALTILKKDGIASYFTEIVTSDNGFPRKPNpEAINYLLNKY 143

                        170       180
                 ....*....|....*....|....
gi 446137853 168 HLKPNQILMIGDRLSDHEAARQNG 191
Cdd:cd07523  144 QLNPEETVMIGDRELDIEAGHNAG 167
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 11-203 1.31e-05

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: 44.25  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   11 ALAFDVDGTLFSSEGII---LEVYRDSILNFSKTSGIQIELPSRDRimaEIGKPVKTIffnllpqlneeqrDSISDSVLR 87
Cdd:TIGR01428   3 ALVFDVYGTLFDVHSVAeraAELYGGRGEALSQLWRQKQLEYSWLR---TLMGPYKDF-------------WDLTREALR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   88 FLCDRIKKGEGEF--------------YPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRI 153
Cdd:TIGR01428  67 YLLGRLGLEDDESaadrlaeaylrlppHPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRA 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446137853  154 -RTKAEILEEYIKLYHLKPNQILMIGDRLSDHEAARQNGCPFAFCSYGHAP 203
Cdd:TIGR01428 147 yKPAPQVYQLALEALGVPPDEVLFVASNPWDLGGAKKFGFKTAWINRPGEP 197
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 99-192 1.67e-05

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


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 43.93  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  99 EFYPNVLETIEILAQKGYRILAASN----GRKPY-----------IQTILEVSGIlpKFEPILV-----LDNKRIRtKAE 158
Cdd:COG0241   28 EFLPGVLEALARLNEAGYRLVVVTNqsgiGRGLFteedlnavhakMLELLAAEGG--RIDAIYYcphhpDDNCDCR-KPK 104

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446137853 159 I--LEEYIKLYHLKPNQILMIGDRLSDHEAARQNGC 192
Cdd:COG0241  105 PgmLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGC 140
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 11-197 3.41e-05

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 43.29  E-value: 3.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  11 ALAFDVDGTLFSSEGIIL---EVYRDSILNFSKTSGIQIELPsrDRIMA-EIG-KPVKTIFFNLLPQLNEEQrdsisdsv 85
Cdd:COG0560    5 LAVFDLDGTLIAGESIDElarFLGRRGLVDRREVLEEVAAIT--ERAMAgELDfEESLRFRVALLAGLPEEE-------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  86 LRFLCDRIKKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQ-------------TILEVS-GIL-PKFEPILVLDN 150
Cdd:COG0560   75 LEELAERLFEEVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEpiaerlgidhviaNELEVEdGRLtGEVVGPIVDGE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446137853 151 krirTKAEILEEYIKLYHLKPNQILMIGDRLSD---HEAArqnGCPFAFC 197
Cdd:COG0560  155 ----GKAEALRELAAELGIDLEQSYAYGDSANDlpmLEAA---GLPVAVN 197
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 99-197 4.13e-05

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: 42.13  E-value: 4.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  99 EFYPNVLETIEILAQKGYRILAASN----GRKPY-----------IQTILEVSGIlpKFEPILV---LDNKRIRT---KA 157
Cdd:cd07503   25 EFLPGVIEALKKLKDAGYLVVVVTNqsgiARGYFseadfealhdkMRELLASQGV--EIDDIYYcphHPDDGCPCrkpKP 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446137853 158 EILEEYIKLYHLKPNQILMIGDRLSDHEAARQNGCPFAFC 197
Cdd:cd07503  103 GMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 101-181 4.72e-04

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: 38.29  E-value: 4.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853 101 YPNVLETIEILaQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLD-------NKRIRTKAEileeyiKLYHLKPNQ 173
Cdd:cd04305   11 LPGAKELLEEL-KKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEevgvqkpNPEIFDYAL------NQLGVKPEE 83


                 ....*...
gi 446137853 174 ILMIGDRL 181
Cdd:cd04305   84 TLMVGDSL 91
HAD pfam12710
haloacid dehalogenase-like hydrolase;
14-188 4.97e-04

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 39.82  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   14 FDVDGTLF---SSEGIILEVYRDSILNFSKTSGIQIELPSRDRIMAEIGKPVKTIFFNLLPQLNEEqrdsISDSVLRFLC 90
Cdd:pfam12710   3 FDLDGTLLdgdSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEE----DAAELERFVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   91 DRIKKGegeFYPNVLETIEILAQKGYRILAASNGRKPYIQTILE------------------VSGILPKFEPILVLDNKR 152
Cdd:pfam12710  79 EVALPR---LHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAelgfdevlatelevddgrFTGELRLIGPPCAGEGKV 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446137853  153 IRTKAEILEEYiklYHLKPNQILMIGDRLSDHEAAR 188
Cdd:pfam12710 156 RRLRAWLAARG---LGLDLADSVAYGDSPSDLPMLR 188
Hydrolase_like pfam13242
HAD-hyrolase-like;
157-220 7.84e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 37.21  E-value: 7.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446137853  157 AEILEEYIKLYHLKPNQILMIGDRL-SDHEAARQNGCPFAFCSYGHAPEGEIPDFDLK----LKNISDL 220
Cdd:pfam13242   7 PGMLERALARLGLDPERTVMIGDRLdTDILGAREAGARTILVLTGVTRPADLEKAPIRpdyvVDDLAEA 75
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 94-193 1.86e-03

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 37.62  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  94 KKGEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDN-KRIRTKAEILEEYIKLYHLKPN 172
Cdd:cd16423   39 EKTDLPPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDvEKSKPDPDLYLEAAERLGVNPE 118

                         90       100
                 ....*....|....*....|.
gi 446137853 173 QILMIGDRLSDHEAARQNGCP 193
Cdd:cd16423  119 ECVVIEDSRNGVLAAKAAGMK 139
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 96-197 1.93e-03

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


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 37.38  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853   96 GEGEFYPNVLETIEILAQKGYRILAASN----GR-------KPYIQTILEVSGiLPKFEPILVLDNKRIRTKA--EILEE 162
Cdd:TIGR01662  22 DERILYPEVPDALAELKEAGYKVVIVTNqsgiGRgyfsrsfSGRVARRLEELG-VPIDILYACPGCRKPKPGMflEALKR 100

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446137853  163 YIklyHLKPNQILMIGDR-LSDHEAARQNGCPFAFC 197
Cdd:TIGR01662 101 FN---EIDPEESVYVGDQdLTDLQAAKRVGLATILV 133
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 81-179 2.49e-03

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 37.53  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  81 ISDSVLRFLCDRIkkgegEFYPNVLETIEILAQKGYRILAASNGRKPYIQTILEVSGILPKFEPILVLDNKRI------- 153
Cdd:cd07500   57 LPESVLDEVYERL-----TLTPGAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLtgkvlgp 131

                         90       100       110
                 ....*....|....*....|....*....|
gi 446137853 154 ----RTKAEILEEYIKLYHLKPNQILMIGD 179
Cdd:cd07500  132 ivdaQRKAETLQELAARLGIPLEQTVAVGD 161
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
157-220 2.79e-03

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 37.78  E-value: 2.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853 157 AEILEEYIKLYHLKPNQILMIGDRL-SDHEAARQNGCPFAFCSYG-HAPEgEIPDFDLK----LKNISDL 220
Cdd:COG0647  189 PPIYELALERLGVDPERVLMVGDRLdTDILGANAAGLDTLLVLTGvTTAE-DLEAAPIRpdyvLDSLAEL 257
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
96-181 4.90e-03

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 36.26  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  96 GEGEFYPNVLETIEILAQKGYRILAASNGRKPYIQTI---LEVSGILPKFEPilvldnkriRTKAeiLEEYIKLYHLKPN 172
Cdd:COG2179   41 DEPEATPEVIEWLEELKEAGFKVCIVSNNSEKRVKRFaekLGIPYIARAKKP---------LPRG--FRKALKLMGLPPE 109


                 ....*....
gi 446137853 173 QILMIGDRL 181
Cdd:COG2179  110 ETAVVGDQL 118
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 96-181 7.68e-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: 34.94  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446137853  96 GEGEFYPNVLETIEILAQKGYRILAASNG----RKPYIQTiLEVSGILPKFEPilvldNKRIRTKAeileeyIKLYHLKP 171
Cdd:cd16416   14 DNPDLTPEVKAWLADLKEAGIKVVLVSNNnerrVAKVIEK-LDLPFVARAGKP-----RPRAFRRA------LKEMDLPP 81

                         90
                 ....*....|
gi 446137853 172 NQILMIGDRL 181
Cdd:cd16416   82 EQVAMVGDQL 91
 
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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