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Conserved domains on  [gi|1750497364|gb|QES91567|]
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HAD family phosphatase [Empedobacter brevis]

Protein Classification

HAD family hydrolase( domain architecture ID 11428160)

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

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-184 6.85e-44

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


:

Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 145.74  E-value: 6.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   4 KINAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDticLVEND-----GMNFTtnEAIQLMLENQQRftNHLYEEIIDWTE 78
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGID---LTEEEyrrlmGRSRE--DILRYLLEEYGL--DLPEEELAARKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  79 KFYIENF-HPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALS 157
Cdd:COG0637    74 ELYRELLaEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAE 153

                         170       180
                  ....*....|....*....|....*..
gi 1750497364 158 LSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:COG0637   154 RLGVDPEECVVFEDSPAGIRAAKAAGM 180
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-184 6.85e-44

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 145.74  E-value: 6.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   4 KINAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDticLVEND-----GMNFTtnEAIQLMLENQQRftNHLYEEIIDWTE 78
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGID---LTEEEyrrlmGRSRE--DILRYLLEEYGL--DLPEEELAARKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  79 KFYIENF-HPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALS 157
Cdd:COG0637    74 ELYRELLaEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAE 153

                         170       180
                  ....*....|....*....|....*..
gi 1750497364 158 LSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:COG0637   154 RLGVDPEECVVFEDSPAGIRAAKAAGM 180
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 7-205 2.09e-34

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: 120.05  E-value: 2.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQLWELMFDEVVKIYRldticlvendgmnfttneaiqlmlenqqrftNHLYEEIIDwtEKFYIEnfh 86
Cdd:cd16423     1 AVIFDFDGVIVDTEPLWYEAWQELLNERR-------------------------------NELIKRQFS--EKTDLP--- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  87 pfvqLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEV 166
Cdd:cd16423    45 ----PIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1750497364 167 LVIEDSLTGINAAKDAGLNYKIYNNSDFCHQPNYIADFR 205
Cdd:cd16423   121 VVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKADLV 159
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 7-186 5.80e-27

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: 101.34  E-value: 5.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDS-----QQLWELMFDEVVKIYRLDticLVENDGMNFTTNEAIQLMLENQQRFTNHLYEEIIDWtekFY 81
Cdd:TIGR01509   1 AILFDLDGVLVDTefaiaKLINREELGLVPDELGVS---AVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQ---IE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  82 IENFhpfVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKyAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEK 161
Cdd:TIGR01509  75 EEAK---LKPLPGVRALLEALRARGKKLALLTNSPRAHKL-VLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGL 150

                         170       180
                  ....*....|....*....|....*
gi 1750497364 162 QKEEVLVIEDSLTGINAAKDAGLNY 186
Cdd:TIGR01509 151 EPSECVFVDDSPAGIEAAKAAGMHT 175
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-186 5.95e-27

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 101.12  E-value: 5.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   8 IFFDFDGVIVDSQQLWELMFDEVVKIYRLDTICLVE-NDGMNFTTNEAIQLMLENQQrftnhlYEEII-DWTEKFYIENF 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEiLKFIGLPLREIFRYLGVSED------EEEKIeFYLRKYNEELH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  86 HPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEE 165
Cdd:pfam13419  75 DKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEE 154

                         170       180
                  ....*....|....*....|.
gi 1750497364 166 VLVIEDSLTGINAAKDAGLNY 186
Cdd:pfam13419 155 VIYVGDSPRDIEAAKNAGIKV 175
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 3-203 8.18e-15

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 70.06  E-value: 8.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   3 KKINAIFFDFDGVIVDSQQLWELMFDEVVKIYrldticlveNDGmNFTTNEAIQL----MLENQQRFTNHLYEEIIDWTE 78
Cdd:PRK13288    1 MKINTVLFDLDGTLINTNELIISSFLHTLKTY---------YPN-QYKREDVLPFigpsLHDTFSKIDESKVEEMITTYR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  79 KFYIENFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSL 158
Cdd:PRK13288   71 EFNHEHHDELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALEL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1750497364 159 SEKQKEEVLVIEDS----LTGINA-AKDAGLNYKIYNNSD-FCHQPNYIAD 203
Cdd:PRK13288  151 LGAKPEEALMVGDNhhdiLAGKNAgTKTAGVAWTIKGREYlEQYKPDFMLD 201
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-184 6.85e-44

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 145.74  E-value: 6.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   4 KINAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDticLVEND-----GMNFTtnEAIQLMLENQQRftNHLYEEIIDWTE 78
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGID---LTEEEyrrlmGRSRE--DILRYLLEEYGL--DLPEEELAARKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  79 KFYIENF-HPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALS 157
Cdd:COG0637    74 ELYRELLaEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAE 153

                         170       180
                  ....*....|....*....|....*..
gi 1750497364 158 LSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:COG0637   154 RLGVDPEECVVFEDSPAGIRAAKAAGM 180
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 7-205 2.09e-34

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: 120.05  E-value: 2.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQLWELMFDEVVKIYRldticlvendgmnfttneaiqlmlenqqrftNHLYEEIIDwtEKFYIEnfh 86
Cdd:cd16423     1 AVIFDFDGVIVDTEPLWYEAWQELLNERR-------------------------------NELIKRQFS--EKTDLP--- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  87 pfvqLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEV 166
Cdd:cd16423    45 ----PIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1750497364 167 LVIEDSLTGINAAKDAGLNYKIYNNSDFCHQPNYIADFR 205
Cdd:cd16423   121 VVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKADLV 159
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
5-211 4.57e-34

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 120.80  E-value: 4.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDTICLVE-NDGMNFTTNEAIQLMLENQqrfTNHLYEEIIDWTEKFYIE 83
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEElRALIGLGLRELLRRLLGED---PDEELEELLARFRELYEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  84 NFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQK 163
Cdd:COG0546    78 ELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1750497364 164 EEVLVIEDSLTGINAAKDAGL-----NYKIYNNSDF-CHQPNYIAD-FRELIKEI 211
Cdd:COG0546   158 EEVLMVGDSPHDIEAARAAGVpfigvTWGYGSAEELeAAGADYVIDsLAELLALL 212
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 7-184 1.00e-29

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


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 107.32  E-value: 1.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQLWELMFdevvkiyrldticlvendgmnfttneaiqlmleNQQRFTNHLYEEIIDWTEKFYIEnfh 86
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAW---------------------------------QLLERKNALLLELIASEGLKLKP--- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  87 pfvqlngHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLH-SYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEE 165
Cdd:cd07505    45 -------GVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLrGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPER 117

                         170
                  ....*....|....*....
gi 1750497364 166 VLVIEDSLTGINAAKDAGL 184
Cdd:cd07505   118 CLVFEDSLAGIEAAKAAGM 136
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-209 8.06e-28

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: 104.73  E-value: 8.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWELMFDEVVKIYR--------LDTICLVENDGMN------FTTNEAIQLMLEnqqrftnHLY 70
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGlldeaeelAEAYRAIEYALWRryergeITFAELLRRLLE-------ELG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  71 EEIIDWTEKFYIENFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAE 150
Cdd:COG1011    74 LDLAEELAEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1750497364 151 PYLKALSLSEKQKEEVLVIEDSLTG-INAAKDAGLNYKIYNNS----DFCHQPNY-IADFRELIK 209
Cdd:COG1011   154 IFELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVWVNRSgepaPAEPRPDYvISDLAELLE 218
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 7-186 5.80e-27

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: 101.34  E-value: 5.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDS-----QQLWELMFDEVVKIYRLDticLVENDGMNFTTNEAIQLMLENQQRFTNHLYEEIIDWtekFY 81
Cdd:TIGR01509   1 AILFDLDGVLVDTefaiaKLINREELGLVPDELGVS---AVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQ---IE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  82 IENFhpfVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKyAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEK 161
Cdd:TIGR01509  75 EEAK---LKPLPGVRALLEALRARGKKLALLTNSPRAHKL-VLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGL 150

                         170       180
                  ....*....|....*....|....*
gi 1750497364 162 QKEEVLVIEDSLTGINAAKDAGLNY 186
Cdd:TIGR01509 151 EPSECVFVDDSPAGIEAAKAAGMHT 175
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-186 5.95e-27

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 101.12  E-value: 5.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   8 IFFDFDGVIVDSQQLWELMFDEVVKIYRLDTICLVE-NDGMNFTTNEAIQLMLENQQrftnhlYEEII-DWTEKFYIENF 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEiLKFIGLPLREIFRYLGVSED------EEEKIeFYLRKYNEELH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  86 HPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEE 165
Cdd:pfam13419  75 DKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEE 154

                         170       180
                  ....*....|....*....|.
gi 1750497364 166 VLVIEDSLTGINAAKDAGLNY 186
Cdd:pfam13419 155 VIYVGDSPRDIEAAKNAGIKV 175
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 5-183 5.55e-26

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: 99.20  E-value: 5.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDTICLVENDGMNFTTNEAIQLMLENQQRFTNHL------------YEE 72
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELdilrglvetleaEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  73 IIDWTEKFYIENFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPY 152
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1750497364 153 LKALSLSEKQKEEVLVIEDSLTGINAAKDAG 183
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 5-183 3.75e-22

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: 89.65  E-value: 3.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDTIclvendgmnftTNEAIQLML-----ENQQRFTNHLYEEIIDWTEK 79
Cdd:cd02616     1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGY-----------TREEVLPFIgpplrETFEKIDPDKLEDMVEEFRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  80 FYIENFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLS 159
Cdd:cd02616    70 YYREHNDDLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELL 149

                         170       180
                  ....*....|....*....|....
gi 1750497364 160 EKQKEEVLVIEDSLTGINAAKDAG 183
Cdd:cd02616   150 GAEPEEALMVGDSPHDILAGKNAG 173
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 5-183 1.39e-20

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 84.70  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQL----WELMFDEVvkIYRLDTICLVENDGMN-FTTNEAIqlmleNQQRFTNHLYEEIIDWTEk 79
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLhaqaWKHIAAKY--GISFDKQYNESLKGLSrEDILRAI-----LKLRGDGLSLEEIHQLAE- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  80 FYIENFHPFVQLNGHVAE-----ILEHLKANQIQIVLVSnsSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLK 154
Cdd:TIGR02009  73 RKNELYRELLRLTGVAVLpgirnLLKRLKAKGIAVGLGS--SSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLL 150

                         170       180
                  ....*....|....*....|....*....
gi 1750497364 155 ALSLSEKQKEEVLVIEDSLTGINAAKDAG 183
Cdd:TIGR02009 151 AAELLGVPPNECIVFEDALAGVQAARAAG 179
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 5-185 4.73e-19

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 80.85  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWELMFDEVVKIYrldticlvendGMNFTTNEAIQLM----LENQQRFTNHL------YEEII 74
Cdd:cd07529     1 VTHCIFDMDGLLLDTERIYTETTQEILARY-----------GKTYTWDVKAKMMgrpaSEAARIIVDELklpmslEEEFD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  75 DWTEKFyIENFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLH-SYFDHTISADD---VSKGKPNAE 150
Cdd:cd07529    70 EQQEAL-AELFMGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELfSLFHHVVTGDDpevKGRGKPAPD 148

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1750497364 151 PYLKALSL---SEKQKEEVLVIEDSLTGINAAKDAGLN 185
Cdd:cd07529   149 IFLVAAKRfnePPKDPSKCLVFEDSPNGVKAAKAAGMQ 186
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 7-184 3.62e-17

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 75.81  E-value: 3.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQL----WELM-------FDEVVK-----IYRLDTICLV-ENDGMNFTTNEAIQLMlenQQRftNHL 69
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYhylaWKHLadelgipFDEEFNeslkgVSREESLERIlDLGGKKYSEEEKEELA---ERK--NDY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  70 YEEIIdwtekfyiENFHPFVQLNGhVAEILEHLKANQIQIVLVSNSsrRQIKYAFQQLKLHSYFDHTISADDVSKGKPNA 149
Cdd:TIGR01990  76 YVELL--------KELTPADVLPG-IKSLLADLKKNNIKIALASAS--KNAPTILEKLELIDYFDAIVDPAELKKGKPDP 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1750497364 150 EPYLKALSLSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:TIGR01990 145 EIFLAAAEGLGVSPSECIGIEDAQAGIEAIKAAGM 179
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 95-183 2.13e-16

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: 71.66  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  95 VAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSLT 174
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91


                  ....*....
gi 1750497364 175 GINAAKDAG 183
Cdd:cd01427    92 DIEAARAAG 100
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 7-183 3.52e-16

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: 72.81  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQLWELMFDEVVKIYRLDTIclvendgmNFTTNEAIQLM-LENQQRFTNHLYEEIIDWTEKFYiENF 85
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPA--------SFKALKQAGGLaEEEWYRIATSALEELQGRFWSEY-DAE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  86 HPFVQlngHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSkGKPNAEPYLKALsLSEKQKEE 165
Cdd:TIGR01549  72 EAYIR---GAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPG-SKPEPEIFLAAL-ESLGVPPE 146

                         170
                  ....*....|....*...
gi 1750497364 166 VLVIEDSLTGINAAKDAG 183
Cdd:TIGR01549 147 VLHVGDNLNDIEGARNAG 164
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 7-183 6.57e-16

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 72.76  E-value: 6.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQLWELMFDEVVKIYRLD-TICLVENDGMnfTTNEAIQLMlenqqrFTNHLYEEIIDWTEKFYIENF 85
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDpEEVLKVSHGR--RAIDVIRKL------APDDADIELVLALETEEPESY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  86 HPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKL-HSyfDHTISADDVSKGKPNAEPYLKALSLSEKQKE 164
Cdd:cd07527    73 PEGVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGLpHP--EVLVTADDVKNGKPDPEPYLLGAKLLGLDPS 150

                         170
                  ....*....|....*....
gi 1750497364 165 EVLVIEDSLTGINAAKDAG 183
Cdd:cd07527   151 DCVVFEDAPAGIKAGKAAG 169
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 3-203 8.18e-15

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 70.06  E-value: 8.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   3 KKINAIFFDFDGVIVDSQQLWELMFDEVVKIYrldticlveNDGmNFTTNEAIQL----MLENQQRFTNHLYEEIIDWTE 78
Cdd:PRK13288    1 MKINTVLFDLDGTLINTNELIISSFLHTLKTY---------YPN-QYKREDVLPFigpsLHDTFSKIDESKVEEMITTYR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  79 KFYIENFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSL 158
Cdd:PRK13288   71 EFNHEHHDELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALEL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1750497364 159 SEKQKEEVLVIEDS----LTGINA-AKDAGLNYKIYNNSD-FCHQPNYIAD 203
Cdd:PRK13288  151 LGAKPEEALMVGDNhhdiLAGKNAgTKTAGVAWTIKGREYlEQYKPDFMLD 201
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 79-208 1.61e-14

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: 69.19  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  79 KFYIENFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSL 158
Cdd:cd16417    76 RHYAETLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEK 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1750497364 159 SEKQKEEVLVIEDSLTGINAAKDAG-----LNYKiYN-NSDFCH-QPNYIAD-FRELI 208
Cdd:cd16417   156 LGIAPAQMLMVGDSRNDILAARAAGcpsvgLTYG-YNyGEDIAAsGPDAVIDsLAELL 212
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 7-184 2.22e-14

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 67.34  E-value: 2.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSqqlwelmfdEVVkiyrldticlvendgmnfttneAIQLMLENQQRFTNHLYEEiidwtekfyienFH 86
Cdd:cd07526     2 LVIFDCDGVLVDS---------EVI----------------------AARVLVEVLAELGARVLAA------------FE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  87 PFVQLNGHVAEILEHLkanQIQIVLVSNSSRRQIKYAFQQLKLHSYFD-HTISADDVSKGKPNAEPYLKALSLSEKQKEE 165
Cdd:cd07526    39 AELQPIPGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEgRIFSASDVGRGKPAPDLFLHAAAQMGVAPER 115

                         170
                  ....*....|....*....
gi 1750497364 166 VLVIEDSLTGINAAKDAGL 184
Cdd:cd07526   116 CLVIEDSPTGVRAALAAGM 134
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-184 3.62e-13

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 65.60  E-value: 3.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   1 MGKKINAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDTicLVENDGMNFTTNEA---IQLMLENQQR-FTNHLYEEIIDW 76
Cdd:PRK13222    2 KFMDIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLPP--AGEERVRTWVGNGAdvlVERALTWAGRePDEELLEKLREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  77 TEKFYIENFHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKAL 156
Cdd:PRK13222   80 FDRHYAENVAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLAC 159

                         170       180
                  ....*....|....*....|....*...
gi 1750497364 157 SLSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:PRK13222  160 EKLGLDPEEMLFVGDSRNDIQAARAAGC 187
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 5-193 1.18e-12

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 63.90  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQqlwelmFDEVVKIYRLDTICLVENDGMNFTTNEAIQLMLE---NQQRFTNHLYEEIIDWTEKFY 81
Cdd:cd02603     1 IRAVLFDFGGVLIDPD------PAAAVARFEALTGEPSEFVLDTEGLAGAFLELERgriTEEEFWEELREELGRPLSAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  82 IEN-FHPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQL-KLHSYFDHTISADDVSKGKPNAEPYLKALSLS 159
Cdd:cd02603    75 FEElVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLpRRGDLFDGVVESCRLGVRKPDPEIYQLALERL 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1750497364 160 EKQKEEVLVIEDSLTGINAAKDAGLNYKIYNNSD 193
Cdd:cd02603   155 GVKPEEVLFIDDREENVEAARALGIHAILVTDAE 188
PLN02940 PLN02940
riboflavin kinase
 3-184 1.57e-12

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 65.24  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   3 KKINAIFFDFDGVIVDSqqlwELMFDEVVKIYrldticLVEN----DG------MNFTTNEAIQLMLENQQRFTNHLyEE 72
Cdd:PLN02940    9 KLVSHVILDLDGTLLNT----DGIVSDVLKAF------LVKYgkqwDGreaqkiVGKTPLEAAATVVEDYGLPCSTD-EF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  73 IIDWTEKFYiENFHPFVQLNGHVaEILEHLKANQIQIVLVSNSSRRQI--KYAFQQlKLHSYFDHTISADDVSKGKPNAE 150
Cdd:PLN02940   78 NSEITPLLS-EQWCNIKALPGAN-RLIKHLKSHGVPMALASNSPRANIeaKISCHQ-GWKESFSVIVGGDEVEKGKPSPD 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1750497364 151 PYLKALSLSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:PLN02940  155 IFLEAAKRLNVEPSNCLVIEDSLPGVMAGKAAGM 188
PRK10826 PRK10826
hexitol phosphatase HxpB;
5-182 2.34e-12

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 63.43  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDticLVENDGMNFTTNEAIQLMLE-----------NQQRFTNHLYEEI 73
Cdd:PRK10826    7 ILAAIFDMDGLLIDSEPLWDRAELDVMASLGVD---ISRREELPDTLGLRIDQVVDlwyarqpwngpSRQEVVQRIIARV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  74 IDwtekfYIENFHPFvqLNGhVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYL 153
Cdd:PRK10826   84 IS-----LIEETRPL--LPG-VREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYL 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1750497364 154 ---KALSLSEKQkeeVLVIEDSLTGINAAKDA 182
Cdd:PRK10826  156 ncaAKLGVDPLT---CVALEDSFNGMIAAKAA 184
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 4-208 2.12e-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: 60.88  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   4 KINAIFFDFDGVIVDSQQLWELMFDEVVKIyrldticlVENDGMNFTTNEAIQLMLENQQRF-----------TNHLYEE 72
Cdd:TIGR02253   1 MIKAIFFDLDDTLIDTSGLAEKARRNAIEV--------LIEAGLNVDFEEAYEELLKLIKEYgsnypthfdylIRRLWEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  73 ----------IIDWTEKFYIENFHPfvqlngHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDV 142
Cdd:TIGR02253  73 ynpklvaafvYAYHKLKFAYLRVYP------GVRDTLMELRESGYRLGIITDGLPVKQWEKLERLGVRDFFDAVITSEEE 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1750497364 143 SKGKPNAEPYLKALSLSEKQKEEVLVIEDSL-TGINAAKDAGL-----NYKIYNN--SDFCHQPNY-IADFRELI 208
Cdd:TIGR02253 147 GVEKPHPKIFYAALKRLGVKPEEAVMVGDRLdKDIKGAKNAGMktvwiNQGKSSKmeDDVYPYPDYeISSLRELL 221
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 95-185 2.51e-11

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: 60.74  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  95 VAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSLT 174
Cdd:cd02588    96 VVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASHAW 175

                          90
                  ....*....|.
gi 1750497364 175 GINAAKDAGLN 185
Cdd:cd02588   176 DLAGARALGLR 186
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 7-183 3.91e-10

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


Pssm-ID: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 56.53  E-value: 3.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQ----QLWELMFDevvkiyrldticlvendgmnfttneaIQLMLENQQRFTNHLYEEIIDwtekfyi 82
Cdd:cd02598     1 GVIFDLDGVITDTAeyhyRAWKKLAD--------------------------KEELAARKNRIYVELIEELTP------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  83 enfhpfVQLNGHVAEILEHLKANQIQIVLVSnSSRRQIKYAfQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQ 162
Cdd:cd02598    48 ------VDVLPGIASLLVDLKAKGIKIALAS-ASKNAPKIL-EKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLN 119

                         170       180
                  ....*....|....*....|.
gi 1750497364 163 KEEVLVIEDSLTGINAAKDAG 183
Cdd:cd02598   120 PKDCIGVEDAQAGIRAIKAAG 140
PLN02811 PLN02811
hydrolase
 95-185 4.51e-10

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 57.08  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  95 VAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLK-LHSYFDHTISADD--VSKGKPNAEPYLKALSLSEKQK---EEVLV 168
Cdd:PLN02811   83 AERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGeLFSLMHHVVTGDDpeVKQGKPAPDIFLAAARRFEDGPvdpGKVLV 162

                          90
                  ....*....|....*..
gi 1750497364 169 IEDSLTGINAAKDAGLN 185
Cdd:PLN02811  163 FEDAPSGVEAAKNAGMS 179
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 5-184 5.45e-10

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 57.16  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWELMFDEVVKIYRLdticlveNDGMNFTT-----------NEAIQLML-----ENQQRFTNH 68
Cdd:PLN02770   22 LEAVLFDVDGTLCDSDPLHYYAFREMLQEINF-------NGGVPITEeffveniagkhNEDIALGLfpddlERGLKFTDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  69 lyEEIIdwTEKFYIENFHPfvqLNGhVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPN 148
Cdd:PLN02770   95 --KEAL--FRKLASEQLKP---LNG-LYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPH 166

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1750497364 149 AEPYLKALSLSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:PLN02770  167 PDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGM 202
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 94-184 1.43e-08

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: 51.00  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  94 HVAEILEHLKANqIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSL 173
Cdd:cd04305    13 GAKELLEELKKG-YKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDSL 91

                          90
                  ....*....|..
gi 1750497364 174 TG-INAAKDAGL 184
Cdd:cd04305    92 ESdILGAKNAGI 103
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 8-183 1.57e-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: 52.79  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   8 IFFDFDGVIVDSQQL--------WELMFDEVVKIYRLDTIclvendgMNFTTNEAIQLMLEnqqrftnHLYEEIIDWTEk 79
Cdd:cd07533     2 VIFDWDGTLADSQHNivaamtaaFADLGLPVPSAAEVRSI-------IGLSLDEAIARLLP-------MATPALVAVAE- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  80 FYIENFHPFVQLNGH-------VAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDvSKGKPNAEPY 152
Cdd:cd07533    67 RYKEAFDILRLLPEHaeplfpgVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADD-TPSKPHPEML 145

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1750497364 153 LKALSLSEKQKEEVLVIEDSLTGINAAKDAG 183
Cdd:cd07533   146 REILAELGVDPSRAVMVGDTAYDMQMAANAG 176
HAD pfam12710
haloacid dehalogenase-like hydrolase;
8-121 3.55e-08

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 51.38  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   8 IFFDFDGVIVDSQQLWELMfDEVVKIYRLDTICLVENDGMNFTTNEAIQLM----LENQQRFTNHLYEEIIDWTEKFYIE 83
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLI-RALLRRGGPDLWRALLVLLLLALLRLLGRLSragaRELLRALLAGLPEEDAAELERFVAE 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1750497364  84 NFHPfvQLNGHVAEILEHLKANQIQIVLVSNSSRRQIK 121
Cdd:pfam12710  80 VALP--RLHPGALELLAAHRAAGDRVVVVTGGLRPLVE 115
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 7-185 3.57e-08

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: 51.59  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQLWELMFDEVVKIYRLDTICLVENDGM-NFTTNEAIQLM---LENQQRFTNHLYEEIIDWTEKFYI 82
Cdd:cd04303     1 LIIFDFDGTLADSFPWFLSILNQLAARHGFKTVDEEEIEQLrQLSSREILKQLgvpLWKLPLIAKDFRRLMAEAAPELAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  83 enFHpfvqlngHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKpNAEPYLKALSLSEKQ 162
Cdd:cd04303    81 --FP-------GVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFAVIEGSSLFGKAK-KIRRVLRRTKITAAQ 150

                         170       180
                  ....*....|....*....|...
gi 1750497364 163 keeVLVIEDSLTGINAAKDAGLN 185
Cdd:cd04303   151 ---VIYVGDETRDIEAARKVGLA 170
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 7-184 3.91e-08

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 51.23  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQLW-ELMFDEVVKIYRLDticlvendgMNFTTNEAIQLM-----LENQQRFTNHLY-EEIIDWTEK 79
Cdd:cd07528     1 ALIFDVDGTLAETEELHrRAFNNAFFAERGLD---------WYWDRELYGELLrvgggKERIAAYFEKVGwPESAPKDLK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  80 FYIENFHP-----FVQLNGH--------VAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLH---SYFDHTISADDVS 143
Cdd:cd07528    72 ELIADLHKakterYAELIAAgllplrpgVARLIDEAKAAGVRLAIATTTSPANVDALLSALLGPerrAIFDAIAAGDDVA 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1750497364 144 KGKPNAEPYLKALSLSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:cd07528   152 EKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGL 192
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 97-211 4.31e-08

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 49.98  E-value: 4.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  97 EILEHLKANQIQIVLVSNSSRRqIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSL-TG 175
Cdd:cd16415    14 ETLKDLKEKGLKLAVVSNFDRR-LRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDDLkND 92

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1750497364 176 INAAKDAGLNYKIYNNSDFCHQPNYIADFRELIKEI 211
Cdd:cd16415    93 YLGARAVGWHALLVDREGALHELPSLANLLERLLEL 128
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 5-185 4.34e-08

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: 51.19  E-value: 4.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWE---------------LMFDEVVKIYRLDTIclvENDGMNF--TTNEAIQLMLENQQ---- 63
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAEraaelyggrgealsqLWRQKQLEYSWLRTL---MGPYKDFwdLTREALRYLLGRLGledd 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  64 -RFTNHLYEEIIDWTEkfyienfHPfvqlngHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDV 142
Cdd:TIGR01428  78 eSAADRLAEAYLRLPP-------HP------DVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAV 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1750497364 143 SKGKPNAEPYLKALSLSEKQKEEVLVIEDSLTGINAAKDAGLN 185
Cdd:TIGR01428 145 RAYKPAPQVYQLALEALGVPPDEVLFVASNPWDLGGAKKFGFK 187
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
125-186 3.26e-07

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 48.53  E-value: 3.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1750497364 125 QQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSLTGINAAKDAGLNY 186
Cdd:PRK10725  121 AHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGMDA 182
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 97-182 3.32e-07

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 49.26  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  97 EILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSLTGI 176
Cdd:PLN03243  116 EFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLGFIPERCIVFGNSNSSV 195


                  ....*.
gi 1750497364 177 NAAKDA 182
Cdd:PLN03243  196 EAAHDG 201
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 97-182 8.12e-07

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 48.71  E-value: 8.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  97 EILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSLTGI 176
Cdd:PLN02575  223 EFVNVLMNYKIPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTV 302


                  ....*.
gi 1750497364 177 NAAKDA 182
Cdd:PLN02575  303 EAAHDA 308
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 4-184 1.65e-06

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 47.92  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364    4 KINAIFFDFDGVIVDSQQLwelmfdevvkiYRLDTICLVENDGMNFTTNEAIQLMLENQQRF---TNHLYE----EIIDW 76
Cdd:PLN02919    74 KVSAVLFDMDGVLCNSEEP-----------SRRAAVDVFAEMGVEVTVEDFVPFMGTGEANFlggVASVKGvkgfDPDAA 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   77 TEKF---YIENFHPFVQLNGHVA--EILEHLKANQIQIVLVSNSSRRQIKYAFQQLKL-HSYFDHTISADDVSKGKPNAE 150
Cdd:PLN02919   143 KKRFfeiYLEKYAKPNSGIGFPGalELITQCKNKGLKVAVASSADRIKVDANLAAAGLpLSMFDAIVSADAFENLKPAPD 222

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1750497364  151 PYLKALSLSEKQKEEVLVIEDSLTGINAAKDAGL 184
Cdd:PLN02919   223 IFLAAAKILGVPTSECVVIEDALAGVQAARAAGM 256
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 94-184 1.98e-06

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: 44.95  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  94 HVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLhsyfdhtisaDDVSK-GKPNAEPYLKALSLSEKQKEEVLVIEDS 172
Cdd:cd16416    21 EVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDL----------PFVARaGKPRPRAFRRALKEMDLPPEQVAMVGDQ 90

                          90
                  ....*....|...
gi 1750497364 173 L-TGINAAKDAGL 184
Cdd:cd16416    91 LfTDILGGNRAGL 103
DREG-2 TIGR02252
REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes ...
 97-185 1.37e-05

REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes uncharacterized sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster which has been identified as a rhythmically (diurnally) regulated gene. This family is a member 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. This family is a member of subfamily 1A in which the cap domain consists of a predicted alpha helical bundle found in between the first and second catalytic motifs. A distinctive feature of this family is a conserved tandem pair of tryptophan residues in the cap domain. The most divergent sequences included within the scope of this model are from plants and have "FW" at this position instead. Most likely, these sequences, like the vast majority of HAD sequences, represent phosphatase enzymes.


Pssm-ID: 274056 [Multi-domain]  Cd Length: 203  Bit Score: 44.20  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  97 EILEHLKANQIQIVLVSNSSRRqIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSL-TG 175
Cdd:TIGR02252 112 KLLKDLRERGLILGVISNFDSR-LRGLLEALGLLEYFDFVVTSYEVGAEKPDPKIFQEALERAGISPEEALHIGDSLrND 190

                          90
                  ....*....|
gi 1750497364 176 INAAKDAGLN 185
Cdd:TIGR02252 191 YQGARAAGWR 200
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 5-190 3.32e-05

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 43.25  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWELMFDEVVKIYRLDticLVENDGMNF-TTNEAIQLMLENQQ---------RFTNHLYEEII 74
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIP---LTEDMFAQYkEINQGLWRAYEEGKitkdevvntRFSALLKEYNT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  75 DWTEKFYIENFHPFV----QLNGHVAEILEHLKaNQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAE 150
Cdd:TIGR02254  78 EADEALLNQKYLRFLeeghQLLPGAFELMENLQ-QKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1750497364 151 PYLKALSLSEK-QKEEVLVIEDSLTG-INAAKDAGLNYKIYN 190
Cdd:TIGR02254 157 IFNYALERMPKfSKEEVLMIGDSLTAdIKGGQNAGLDTCWMN 198
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 86-184 4.36e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 43.31  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  86 HPFVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEE 165
Cdd:PRK13223   97 HELTVVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMAGVPPSQ 176

                          90
                  ....*....|....*....
gi 1750497364 166 VLVIEDSLTGINAAKDAGL 184
Cdd:PRK13223  177 SLFVGDSRSDVLAAKAAGV 195
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 7-194 4.55e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 43.16  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQ-------------------LWELMF-DEVVKI----------YRLDTICLVENDGMNFTTNEAIQ 56
Cdd:PLN02779   42 ALLFDCDGVLVETERdghrvafndafkefglrpvEWDVELyDELLNIgggkermtwyFNENGWPTSTIEKAPKDEEERKE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  57 LMLENQQRFTNhLYEEIIDWTEkfyienfhpfVQLNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFD-- 134
Cdd:PLN02779  122 LVDSLHDRKTE-LFKELIESGA----------LPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVNTLLGPERAQgl 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1750497364 135 HTISADDVSKGKPNAEPYLKAlslSEK---QKEEVLVIEDSLTGINAAKDAGL----NYKIYN-NSDF 194
Cdd:PLN02779  191 DVFAGDDVPKKKPDPDIYNLA---AETlgvDPSRCVVVEDSVIGLQAAKAAGMrcivTKSSYTaDEDF 255
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 5-197 9.41e-05

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 42.69  E-value: 9.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   5 INAIFFDFDGVIVDSQQLWEL----MFDEVVKIYRLDTICLVEN--DGMNFTTNEAIQLMLENQQRftnhlyeEIIDWTE 78
Cdd:PRK06698  241 LQALIFDMDGTLFQTDKILELslddTFDHLRSLQLWDTVTPIDKyrEIMGVPLPKVWEALLPDHSL-------EIREQTD 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  79 KFYIENFHPFVQ-----LNGHVAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKgkPNAEPYL 153
Cdd:PRK06698  314 AYFLERLIENIKsgkgaLYPNVKEIFTYIKENNCSIYIASNGLTEYLRAIVSYYDLDQWVTETFSIEQINS--LNKSDLV 391

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1750497364 154 KALsLSEKQKEEVLVIEDSLTGINAAKDAGLnYKIYNNSDFCHQ 197
Cdd:PRK06698  392 KSI-LNKYDIKEAAVVGDRLSDINAAKDNGL-IAIGCNFDFAQE 433
PRK11587 PRK11587
putative phosphatase; Provisional
 71-183 1.46e-04

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 41.13  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  71 EEI---IDWTEKFYIENFHPFVQLNGHVAeILEHLKANQIQIVLVSN------SSRRQIKyafqQLKLHSYFdhtISADD 141
Cdd:PRK11587   62 AEIqaeFTRLEQIEATDTEGITALPGAIA-LLNHLNKLGIPWAIVTSgsvpvaSARHKAA----GLPAPEVF---VTAER 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1750497364 142 VSKGKPNAEPYLKALSLSEKQKEEVLVIEDSLTGINAAKDAG 183
Cdd:PRK11587  134 VKRGKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAG 175
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 7-184 1.75e-04

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: 40.82  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364   7 AIFFDFDGVIVDSQQLWELMFDEVVKIYrldticlvendGMNFTTNEAIQLMLENQQRFTNHLYEEIIDWTEKFYI---E 83
Cdd:cd07523     1 NFIWDLDGTLLDSYPAMTKALSETLADF-----------GIPQDLETVYKIIKESSVQFAIQYYAEVPDLEEEYKEleaE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  84 NFHPFVQLNGhVAEILEHLKANQIQIVLVSNSSRRQIKYaFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQK 163
Cdd:cd07523    70 YLAKPILFPG-AKAVLRWIKEQGGKNFLMTHRDHSALTI-LKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNP 147

                         170       180
                  ....*....|....*....|.
gi 1750497364 164 EEVLVIEDSLTGINAAKDAGL 184
Cdd:cd07523   148 EETVMIGDRELDIEAGHNAGI 168
HAD-SF-IA-v2 TIGR01493
Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid ...
 109-180 1.38e-03

Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase; 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 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). 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.


Pssm-ID: 130557 [Multi-domain]  Cd Length: 175  Bit Score: 38.27  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1750497364 109 IVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSLTGINAAK 180
Cdd:TIGR01493 102 VAILSNASHWAFDQFAQQAGLPWYFDRAFSVDTVRAYKPDPVVYELVFDTVGLPPDRVLMVAAHQWDLIGAR 173
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 95-184 3.43e-03

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: 37.30  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  95 VAEILEHLKANQIQIVLVSNSSRRQIKYAFQQLKLHSYFDHTISADDVSKGKPNAEPYLKALSLSEKQKEEVLVIEDSLT 174
Cdd:cd07512    91 VIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVSRALMVGDSET 170

                          90
                  ....*....|
gi 1750497364 175 GINAAKDAGL 184
Cdd:cd07512   171 DAATARAAGV 180
Hydrolase_like pfam13242
HAD-hyrolase-like;
145-207 5.40e-03

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 34.51  E-value: 5.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1750497364 145 GKPNAEPYLKALSLSEKQKEEVLVIEDSL-TGINAAKDAGL--------NYKIYNNSDFCHQPNYIA-DFREL 207
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDRLdTDILGAREAGArtilvltgVTRPADLEKAPIRPDYVVdDLAEA 75
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 94-184 7.46e-03

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


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 35.46  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750497364  94 HVAEILEHLKANQIQIVLVSNSS---RRQIKYAFQQ------LKLHSYFDHTISADDVSkgKPNAEPYLKALS-LSEKQK 163
Cdd:TIGR01662  29 EVPDALAELKEAGYKVVIVTNQSgigRGYFSRSFSGrvarrlEELGVPIDILYACPGCR--KPKPGMFLEALKrFNEIDP 106

                          90       100
                  ....*....|....*....|..
gi 1750497364 164 EEVLVIED-SLTGINAAKDAGL 184
Cdd:TIGR01662 107 EESVYVGDqDLTDLQAAKRVGL 128
 
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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