NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|398364625|ref|NP_012891|]
View 

putative hydrolase [Saccharomyces cerevisiae S288C]

Protein Classification

HAD family hydrolase( domain architecture ID 11576397)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 7-202 2.32e-93

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: 271.91  E-value: 2.32e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKGPlTWDVKIKLQGLPGPEAGKRVIEHYKLPITL-DEYDERNVALQSLK 85
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTY-TWDVKAKMMGRPASEAARIIVDELKLPMSLeEEFDEQQEALAELF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  86 WGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFDTIVTGDDPRIaKGRGKPFPDIWQLGLKELN 165
Cdd:cd07529   80 MGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEV-KGRGKPAPDIFLVAAKRFN 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398364625 166 EKFHtdiKPDECIVFEDGIPGVKSAKAFGAHVIWVPH 202
Cdd:cd07529  159 EPPK---DPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 7-202 2.32e-93

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: 271.91  E-value: 2.32e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKGPlTWDVKIKLQGLPGPEAGKRVIEHYKLPITL-DEYDERNVALQSLK 85
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTY-TWDVKAKMMGRPASEAARIIVDELKLPMSLeEEFDEQQEALAELF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  86 WGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFDTIVTGDDPRIaKGRGKPFPDIWQLGLKELN 165
Cdd:cd07529   80 MGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEV-KGRGKPAPDIFLVAAKRFN 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398364625 166 EKFHtdiKPDECIVFEDGIPGVKSAKAFGAHVIWVPH 202
Cdd:cd07529  159 EPPK---DPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-215 2.28e-43

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 145.35  E-value: 2.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKgPLTWDVKIKLQGLPGPEAGKRVIEHYKLPITLDEYDER--NVALQSL 84
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGI-DLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARkeELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  85 KWGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEgFDLFDTIVTGDDPriakGRGKPFPDIWQLGLKEL 164
Cdd:COG0637   81 AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGL-LDYFDVIVTGDDV----ARGKPDPDIYLLAAERL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398364625 165 NekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHP--------EAHAVLGDTEAL 215
Cdd:COG0637  156 G------VDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGgtaeeelaGADLVVDDLAEL 208
PLN02811 PLN02811
hydrolase
 14-236 2.45e-38

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 132.57  E-value: 2.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  14 MDGLLINTEDIYTETLNETLAEFGKgPLTWDVKIKLQGLPGPEAGKRVIEHYKLP--ITLDEY-DERNVALQSLkWGTCE 90
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGK-TFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFlVEREAMLQDL-FPTSD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  91 FLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFDTIVTGDDPRIAkgRGKPFPDIWqlgLKELNEKFHT 170
Cdd:PLN02811  79 LMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVK--QGKPAPDIF---LAAARRFEDG 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364625 171 DIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHPeahavlGDTEALLAGKGELLSSLEKLEMSKYGL 236
Cdd:PLN02811 154 PVDPGKVLVFEDAPSGVEAAKNAGMSVVMVPDP------RLDKSYCKGADQVLSSLLDFKPEEWGL 213
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
10-200 4.91e-26

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 99.58  E-value: 4.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   10 CLFDMDGLLINTEDIYTETLNETLAEFGKGPLTWDVKIKLQGLPGPEAGKRVIEHYKLPITLDEYDERnVALQSLKWGTC 89
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRK-YNEELHDKLVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   90 EFlPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLeeGF-DLFDTIVTGDDpriaKGRGKPFPDIWQLGLKELNekf 168
Cdd:pfam13419  80 PY-PGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQL--GLeDYFDVIVGGDD----VEGKKPDPDPILKALEQLG--- 149

                         170       180       190
                  ....*....|....*....|....*....|..
gi 398364625  169 htdIKPDECIVFEDGIPGVKSAKAFGAHVIWV 200
Cdd:pfam13419 150 ---LKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 9-200 2.61e-24

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: 95.18  E-value: 2.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625    9 ACLFDMDGLLINTEDIYTETLNEtlaeFGKGPLTWDVKIKLQGLPGpEAGKRVIEHY---KLPITLDEYDERNVALQSLK 85
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINR----EELGLVPDELGVSAVGRLE-LALRRFKAQYgrtISPEDAQLLYKQLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   86 WGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRgKTSHLEEgFDLFDTIVTGDDPriakGRGKPFPDIWQLGLKELN 165
Cdd:TIGR01509  76 EAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKL-VLALLGL-RDLFDVVIDSSDV----GLGKPDPDIYLQALKALG 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 398364625  166 ekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVIWV 200
Cdd:TIGR01509 150 ------LEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 7-202 2.32e-93

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: 271.91  E-value: 2.32e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKGPlTWDVKIKLQGLPGPEAGKRVIEHYKLPITL-DEYDERNVALQSLK 85
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTY-TWDVKAKMMGRPASEAARIIVDELKLPMSLeEEFDEQQEALAELF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  86 WGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFDTIVTGDDPRIaKGRGKPFPDIWQLGLKELN 165
Cdd:cd07529   80 MGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEV-KGRGKPAPDIFLVAAKRFN 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398364625 166 EKFHtdiKPDECIVFEDGIPGVKSAKAFGAHVIWVPH 202
Cdd:cd07529  159 EPPK---DPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-215 2.28e-43

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 145.35  E-value: 2.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKgPLTWDVKIKLQGLPGPEAGKRVIEHYKLPITLDEYDER--NVALQSL 84
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGI-DLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARkeELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  85 KWGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEgFDLFDTIVTGDDPriakGRGKPFPDIWQLGLKEL 164
Cdd:COG0637   81 AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGL-LDYFDVIVTGDDV----ARGKPDPDIYLLAAERL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398364625 165 NekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHP--------EAHAVLGDTEAL 215
Cdd:COG0637  156 G------VDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGgtaeeelaGADLVVDDLAEL 208
PLN02811 PLN02811
hydrolase
 14-236 2.45e-38

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 132.57  E-value: 2.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  14 MDGLLINTEDIYTETLNETLAEFGKgPLTWDVKIKLQGLPGPEAGKRVIEHYKLP--ITLDEY-DERNVALQSLkWGTCE 90
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGK-TFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFlVEREAMLQDL-FPTSD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  91 FLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFDTIVTGDDPRIAkgRGKPFPDIWqlgLKELNEKFHT 170
Cdd:PLN02811  79 LMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVK--QGKPAPDIF---LAAARRFEDG 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364625 171 DIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHPeahavlGDTEALLAGKGELLSSLEKLEMSKYGL 236
Cdd:PLN02811 154 PVDPGKVLVFEDAPSGVEAAKNAGMSVVMVPDP------RLDKSYCKGADQVLSSLLDFKPEEWGL 213
PLN02940 PLN02940
riboflavin kinase
 6-236 9.02e-31

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 116.86  E-value: 9.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   6 AVKACLFDMDGLLINTEDIYTETLNETLAEFGKgplTWDVK--IKLQGLPGPEAGKRVIEHYKLPITLDEYDERNVALQS 83
Cdd:PLN02940  10 LVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGK---QWDGReaQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  84 LKWGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFDTIVTGDDPRiakgRGKPFPDIWQLGLKE 163
Cdd:PLN02940  87 EQWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGDEVE----KGKPSPDIFLEAAKR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398364625 164 LNekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHpeahavLGDTEALLAGKGELLSSLEKLEMSKYGL 236
Cdd:PLN02940 163 LN------VEPSNCLVIEDSLPGVMAGKAAGMEVIAVPS------IPKQTHLYSSADEVINSLLDLQPEKWGL 223
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
10-200 4.91e-26

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 99.58  E-value: 4.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   10 CLFDMDGLLINTEDIYTETLNETLAEFGKGPLTWDVKIKLQGLPGPEAGKRVIEHYKLPITLDEYDERnVALQSLKWGTC 89
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRK-YNEELHDKLVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   90 EFlPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLeeGF-DLFDTIVTGDDpriaKGRGKPFPDIWQLGLKELNekf 168
Cdd:pfam13419  80 PY-PGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQL--GLeDYFDVIVGGDD----VEGKKPDPDPILKALEQLG--- 149

                         170       180       190
                  ....*....|....*....|....*....|..
gi 398364625  169 htdIKPDECIVFEDGIPGVKSAKAFGAHVIWV 200
Cdd:pfam13419 150 ---LKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 9-200 2.61e-24

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: 95.18  E-value: 2.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625    9 ACLFDMDGLLINTEDIYTETLNEtlaeFGKGPLTWDVKIKLQGLPGpEAGKRVIEHY---KLPITLDEYDERNVALQSLK 85
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINR----EELGLVPDELGVSAVGRLE-LALRRFKAQYgrtISPEDAQLLYKQLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   86 WGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRgKTSHLEEgFDLFDTIVTGDDPriakGRGKPFPDIWQLGLKELN 165
Cdd:TIGR01509  76 EAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKL-VLALLGL-RDLFDVVIDSSDV----GLGKPDPDIYLQALKALG 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 398364625  166 ekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVIWV 200
Cdd:TIGR01509 150 ------LEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-200 1.11e-22

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: 90.86  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625    7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKgPLTWDVKIKLQGLPGPEAGKRVIEHYKLPITLDEYDE----RNVALQ 82
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGI-SFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQlaerKNELYR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   83 SL-KWGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEegfDLFDTIVTGDDPRiakgRGKPFPDIWQLGL 161
Cdd:TIGR02009  80 ELlRLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLR---DYFDAIVDASEVK----NGKPHPETFLLAA 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 398364625  162 KELNekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVIWV 200
Cdd:TIGR02009 153 ELLG------VPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 9-202 2.42e-22

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: 88.83  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   9 ACLFDMDGLLINTEDIYTETLNEtlaefgkgpltwdvkiklqglpgpeagkrvIEHYKlpitlDEYDERnvalqsLKWGT 88
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQL------------------------------LERKN-----ALLLEL------IASEG 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  89 CEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFDTIVTGDDPRiakgRGKPFPDIWQLGLKELNekf 168
Cdd:cd07505   40 LKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVE----RGKPAPDIYLLAAERLG--- 112

                        170       180       190
                 ....*....|....*....|....*....|....
gi 398364625 169 htdIKPDECIVFEDGIPGVKSAKAFGAHVIWVPH 202
Cdd:cd07505  113 ---VDPERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 9-203 3.72e-19

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: 81.15  E-value: 3.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   9 ACLFDMDGLLINTEDIYTETLNETLAEfgkgpLTWDVKIKL-QGLPGPEAGKRVIEHyklpitLDEYDERNvalqslkwg 87
Cdd:cd16423    1 AVIFDFDGVIVDTEPLWYEAWQELLNE-----RRNELIKRQfSEKTDLPPIEGVKEL------LEFLKEKG--------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  88 tceflpgalnllkylklknIPIALCTSSNKTKFrgkTSHLEE-G-FDLFDTIVTGDDPRiakgRGKPFPDIWQLGLKELn 165
Cdd:cd16423   61 -------------------IKLAVASSSPRRWI---EPHLERlGlLDYFEVIVTGDDVE----KSKPDPDLYLEAAERL- 113

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 398364625 166 ekfhtDIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHP 203
Cdd:cd16423  114 -----GVNPEECVVIEDSRNGVLAAKAAGMKCVGVPNP 146
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 6-198 3.32e-18

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 81.29  E-value: 3.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   6 AVKACLFDMDGLLINTE-DIYTETLNETLAEFGKGPLTWDVKI--KLQGLPGpeaGKRVIEHY------------KLPIT 70
Cdd:PLN02779  39 LPEALLFDCDGVLVETErDGHRVAFNDAFKEFGLRPVEWDVELydELLNIGG---GKERMTWYfnengwptstieKAPKD 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  71 LDEYDERNVALQSLKW---------GTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHL--EEGFDLFDtIVT 139
Cdd:PLN02779 116 EEERKELVDSLHDRKTelfkeliesGALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVNTLlgPERAQGLD-VFA 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398364625 140 GDDPRiakgRGKPFPDIWQLGLKELNekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVI 198
Cdd:PLN02779 195 GDDVP----KKKPDPDIYNLAAETLG------VDPSRCVVVEDSVIGLQAAKAAGMRCI 243
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-217 3.46e-17

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 76.89  E-value: 3.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKGPLTWDVKIKLQGLPGPEAGKRVIEHY---KLPITLDEYDERnvaLQS 83
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDpdeELEELLARFREL---YEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  84 LKWGTCEFLPGALNLLKYLKLKNIPIALCTSsnktKFRGKTSHLEEGFDL---FDTIVTGDDPriakGRGKPFPDIWQLG 160
Cdd:COG0546   78 ELLDETRLFPGVRELLEALKARGIKLAVVTN----KPREFAERLLEALGLddyFDAIVGGDDV----PPAKPKPEPLLEA 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364625 161 LKELNekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVIWV---PHPE-------AHAVLGDTEALLA 217
Cdd:COG0546  150 LERLG------LDPEEVLMVGDSPHDIEAARAAGVPFIGVtwgYGSAeeleaagADYVIDSLAELLA 210
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 9-198 7.12e-17

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: 75.88  E-value: 7.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   9 ACLFDMDGLLINTEDIYTETLNETLAEFGKGPLTWDVK--IKLQGLPGpeaGKRVIEHY--------KLPITLDEY---- 74
Cdd:cd07528    1 ALIFDVDGTLAETEELHRRAFNNAFFAERGLDWYWDRElyGELLRVGG---GKERIAAYfekvgwpeSAPKDLKELiadl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  75 ----DERNVALqsLKWGTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHL--EEGFDLFDTIVTGDDPRIAkg 148
Cdd:cd07528   78 hkakTERYAEL--IAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALlgPERRAIFDAIAAGDDVAEK-- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 398364625 149 rgKPFPDIWQLGLKELnekfhtDIKPDECIVFEDGIPGVKSAKAFGAHVI 198
Cdd:cd07528  154 --KPDPDIYLLALERL------GVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-194 4.69e-14

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: 68.00  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625    7 VKACLFDMDGLLINTEDIYTETLNETLAEFgkgPLTWDVKIKLQGLPGPEA--------GKRV----IEHYKLPITLDEY 74
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEH---PLAKAIVAAAEDLPIPVEdftarlllGKRDwleeLDILRGLVETLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   75 DERNVALQSLKW-----GTCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEgFDLFDTIVTGDDpriaKGR 149
Cdd:pfam00702  78 EGLTVVLVELLGvialaDELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGL-DDYFDVVISGDD----VGV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 398364625  150 GKPFPDIWQLGLKELNekfhtdIKPDECIVFEDGIPGVKSAKAFG 194
Cdd:pfam00702 153 GKPKPEIYLAALERLG------VKPEEVLMVGDGVNDIPAAKAAG 191
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 9-235 9.25e-13

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: 64.67  E-value: 9.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   9 ACLFDMDGLLINTEDIYTETLNETLAEFGKGPLTwdVKIKLQGLPGPEagkrVIEHYkLPITLD-EYDERNVALQSLKWG 87
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEE--VLKVSHGRRAID----VIRKL-APDDADiELVLALETEEPESYP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  88 -TCEFLPGALNLLKYLKLKNIPIALCTSSNktkfRGKTSHLEEGFDLF--DTIVTGDDPRiakgRGKPFPDIWQLGLKEL 164
Cdd:cd07527   74 eGVIAIPGAVDLLASLPAAGDRWAIVTSGT----RALAEARLEAAGLPhpEVLVTADDVK----NGKPDPEPYLLGAKLL 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364625 165 nekfhtDIKPDECIVFEDGIPGVKSAKAFGAHVIWV-PHPEAHAVLGDTEALlagkgeLLSSLEKLEMSKYG 235
Cdd:cd07527  146 ------GLDPSDCVVFEDAPAGIKAGKAAGARVVAVnTSHDLEQLEAAGADL------VVEDLSDISVDGDE 205
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 7-200 2.20e-11

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 62.95  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625    7 VKACLFDMDGLLINTE--------DIYTET-LNETLAEF----GKGPLTWDVKI-KLQGLPG--PEAGK-RVIEHYklpi 69
Cdd:PLN02919   75 VSAVLFDMDGVLCNSEepsrraavDVFAEMgVEVTVEDFvpfmGTGEANFLGGVaSVKGVKGfdPDAAKkRFFEIY---- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   70 tLDEYDERNVALQslkwgtcefLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFDTIVTGDdpriAKGR 149
Cdd:PLN02919  151 -LEKYAKPNSGIG---------FPGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSAD----AFEN 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 398364625  150 GKPFPDIWQLGLKELnekfhtDIKPDECIVFEDGIPGVKSAKAFGAHVIWV 200
Cdd:PLN02919  217 LKPAPDIFLAAAKIL------GVPTSECVVIEDALAGVQAARAAGMRCIAV 261
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
11-200 2.95e-11

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 60.47  E-value: 2.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  11 LFDMDGLLINTEDIYTETLNETLAEFGkgpLTWDVK--IKLQGLPGPEAGKRVIEHYKlpITLDEY---DERNVALQSLK 85
Cdd:PRK10725   9 IFDMDGTILDTEPTHRKAWREVLGRYG---LQFDEQamVALNGSPTWRIAQAIIELNQ--ADLDPHalaREKTEAVKSML 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  86 WGTCEFLPGALNLLKYLKLKniPIALCTSSNKTKFRGKTSHLeeG-FDLFDTIVTGDDPRiakgRGKPFPDIWqLGLKEL 164
Cdd:PRK10725  84 LDSVEPLPLIEVVKAWHGRR--PMAVGTGSESAIAEALLAHL--GlRRYFDAVVAADDVQ----HHKPAPDTF-LRCAQL 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 398364625 165 nekfhTDIKPDECIVFEDGIPGVKSAKAFGAHVIWV 200
Cdd:PRK10725 155 -----MGVQPTQCVVFEDADFGIQAARAAGMDAVDV 185
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-217 1.79e-10

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: 58.89  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKGPLTWDV-----KIKLQGLPGPEAGK--------RVIEHYKLPITLDE 73
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELaeayrAIEYALWRRYERGEitfaellrRLLEELGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  74 YDERNVALQSLkwgtCEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLeeGF-DLFDTIVTGDDpriaKGRGKP 152
Cdd:COG1011   81 AEAFLAALPEL----VEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRL--GLdDLFDAVVSSEE----VGVRKP 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364625 153 FPDIWQLGLKELNekfhtdIKPDECIVFEDGIPG-VKSAKAFGAHVIWV--------PHPEAHAVLGDTEALLA 217
Cdd:COG1011  151 DPEIFELALERLG------VPPEEALFVGDSPETdVAGARAAGMRTVWVnrsgepapAEPRPDYVISDLAELLE 218
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 7-224 9.50e-10

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: 56.52  E-value: 9.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKGPLTWDVKIKLQGLPGPEAGKRVIEHyKLPITLDEYDERNVALQSlkw 86
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGPPLRETFEKIDPD-KLEDMVEEFRKYYREHND--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  87 GTCEFLPGALNLLKYLKLKNIPIALCTssNKTKFRGKTS-HLEEGFDLFDTIVTGDDpriaKGRGKPFPDIWQLGLKELN 165
Cdd:cd02616   77 DLTKEYPGVYETLARLKSQGIKLGVVT--TKLRETALKGlKLLGLDKYFDVIVGGDD----VTHHKPDPEPVLKALELLG 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364625 166 EkfhtdiKPDECIVFEDGIPGVKSAKAFG---AHVIWVPHPEAHAVLGDTEALLAGKGELLS 224
Cdd:cd02616  151 A------EPEEALMVGDSPHDILAGKNAGvktVGVTWGYKGREYLKAFNPDFIIDKMSDLLT 206
PRK11587 PRK11587
putative phosphatase; Provisional
 92-233 7.83e-09

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 54.23  E-value: 7.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  92 LPGALNLLKYLKLKNIPIALCTSSNK--TKFRGKTSHLEEGfdlfDTIVTGDdpRIAkgRGKPFPDIWQLGLKELnekfh 169
Cdd:PRK11587  85 LPGAIALLNHLNKLGIPWAIVTSGSVpvASARHKAAGLPAP----EVFVTAE--RVK--RGKPEPDAYLLGAQLL----- 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364625 170 tDIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHPEAHAVLGDTEAllagkgeLLSSLEKLEMSK 233
Cdd:PRK11587 152 -GLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAPADTPRLDEVDL-------VLHSLEQLTVTK 207
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 8-198 1.97e-08

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: 51.55  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   8 KACLFDMDGLLINTEDIYTETLNETLAEFGkGPLTWDVKIKLQGLPGPEAgkrviehyklpiTLDEydernvalqslkwg 87
Cdd:cd07526    1 DLVIFDCDGVLVDSEVIAARVLVEVLAELG-ARVLAAFEAELQPIPGAAA------------ALSA-------------- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  88 tceflpgalnllkylklknIPIALCTSSNKTkfRGKTSH------LEEGFDlfDTIVTGDDpriaKGRGKPFPDIWQLGL 161
Cdd:cd07526   54 -------------------LTLPFCVASNSS--RERLTHslglagLLAYFE--GRIFSASD----VGRGKPAPDLFLHAA 106

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398364625 162 KELNekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVI 198
Cdd:cd07526  107 AQMG------VAPERCLVIEDSPTGVRAALAAGMTVF 137
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 92-216 4.59e-08

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: 51.14  E-value: 4.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  92 LPGALNLLKYLKLKNIPIALCTSS-------NKTKFRgktshleegfDLFDTIVtgdDPRIAKgRGKPFPDIWQLGLKEL 164
Cdd:cd02598   51 LPGIASLLVDLKAKGIKIALASASknapkilEKLGLA----------EYFDAIV---DGAVLA-KGKPDPDIFLAAAEGL 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 398364625 165 NekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHPE----AHAVLGDTEALL 216
Cdd:cd02598  117 G------LNPKDCIGVEDAQAGIRAIKAAGFLVVGVGREEdllgADIVVPDTTADL 166
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 107-200 5.51e-06

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: 43.92  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625 107 IPIALCTSSNKTKFRGKTSHLEEGfDLFDTIVTGDDPRIAKGRGKPFPDIWQlglkelnekfHTDIKPDECIVFEDGIPG 186
Cdd:cd01427   24 IKLAIVTNRSREALRALLEKLGLG-DLFDGIIGSDGGGTPKPKPKPLLLLLL----------KLGVDPEEVLFVGDSEND 92

                         90
                 ....*....|....
gi 398364625 187 VKSAKAFGAHVIWV 200
Cdd:cd01427   93 IEAARAAGGRTVAV 106
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-229 1.41e-05

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 44.55  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   1 MTHPvAVKACLFDMDGLLINTEDIYTETLNETLAEFGkgpltwdVKIKLQGLPGPEAGKR---VIEHY--KLPitLDEYD 75
Cdd:PRK10826   2 STPR-QILAAIFDMDGLLIDSEPLWDRAELDVMASLG-------VDISRREELPDTLGLRidqVVDLWyaRQP--WNGPS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  76 ERNVALQ------SLKWGTCEFLPGALNLLKYLKLKNIPIALCTSSnktkfrgkTSHLEEG----FDL---FDTIVTGDD 142
Cdd:PRK10826  72 RQEVVQRiiarviSLIEETRPLLPGVREALALCKAQGLKIGLASAS--------PLHMLEAvltmFDLrdyFDALASAEK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625 143 PRiakgRGKPFPDIWqlglkeLNEKFHTDIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHPEaHAvlGDTEALLAGKGel 222
Cdd:PRK10826 144 LP----YSKPHPEVY------LNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPE-QQ--NDPRWALADVK-- 208


                 ....*..
gi 398364625 223 LSSLEKL 229
Cdd:PRK10826 209 LESLTEL 215
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 7-204 5.69e-05

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: 42.72  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLIN--TEDIYTETLNETLAEFGKGPLT-WDVKIKLQGLPG----PEAGKRVIEHYKLPITLDEYDErnv 79
Cdd:cd02603    1 IRAVLFDFGGVLIDpdPAAAVARFEALTGEPSEFVLDTeGLAGAFLELERGriteEEFWEELREELGRPLSAELFEE--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  80 alQSLKWGtcEFLPGALNLLKYLKLKNIPIALCTSSNKTKFRGKTSHLEEGFDLFD-TIVTGDdpriaKGRGKPFPDIWQ 158
Cdd:cd02603   78 --LVLAAV--DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDgVVESCR-----LGVRKPDPEIYQ 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 398364625 159 LGLKELnekfhtDIKPDECIVFEDGIPGVKSAKAFGAHVIWVPHPE 204
Cdd:cd02603  149 LALERL------GVKPEEVLFIDDREENVEAARALGIHAILVTDAE 188
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
2-210 7.25e-05

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 42.49  E-value: 7.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   2 THPVAVKACLFDMDGLLINT-EDIyTETLNETLAEFGKGPL------TW-----DVKIK-----LQGLPGPEAGKRVIEH 64
Cdd:PRK13222   1 MKFMDIRAVAFDLDGTLVDSaPDL-AAAVNAALAALGLPPAgeervrTWvgngaDVLVEraltwAGREPDEELLEKLREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  65 YklpitlDEYDERNVALQSlkwgtcEFLPGALNLLKYLKLKNIPIALCTssNK-TKFrgkTSHLEEGF---DLFDTIVTG 140
Cdd:PRK13222  80 F------DRHYAENVAGGS------RLYPGVKETLAALKAAGYPLAVVT--NKpTPF---VAPLLEALgiaDYFSVVIGG 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398364625 141 DD-PRIakgrgKPFPDiwqlGLKELNEKFhtDIKPDECIVFEDGIPGVKSAKAFGAHVIWVP----HPEAHAVLG 210
Cdd:PRK13222 143 DSlPNK-----KPDPA----PLLLACEKL--GLDPEEMLFVGDSRNDIQAARAAGCPSVGVTygynYGEPIALSE 206
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 7-206 2.07e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 38.09  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   7 VKACLFDMDGLLINTEDIYTETLNETLAEFGKGPLTWDVKIKLQGLP--------GPEAGKRVIEHYKlPITLDEYDErn 78
Cdd:PRK13288   3 INTVLFDLDGTLINTNELIISSFLHTLKTYYPNQYKREDVLPFIGPSlhdtfskiDESKVEEMITTYR-EFNHEHHDE-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625  79 valqslkwgTCEFLPGALNLLKYLKLKNIPIALCTSS-NKTKFRG-KTSHLEEgfdLFDTIVTGDDPRiakgRGKPFPDI 156
Cdd:PRK13288  80 ---------LVTEYETVYETLKTLKKQGYKLGIVTTKmRDTVEMGlKLTGLDE---FFDVVITLDDVE----HAKPDPEP 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 398364625 157 WQLGLKELnekfhtDIKPDECIVFEDG---IPGVKSAKAFGAHVIWVPHPEAH 206
Cdd:PRK13288 144 VLKALELL------GAKPEEALMVGDNhhdILAGKNAGTKTAGVAWTIKGREY 190
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 9-142 3.54e-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: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364625   9 ACLFDMDGLLINTEDIYTETLNETLAEFGKGPLTWD-----------VKIKL------QGLPGPEAG---KRVIEHYklp 68
Cdd:cd07512    1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAevrsfvghgapALIRRafaaagEDLDGPLHDallARFLDHY--- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364625  69 itldeydERNVALQSLKWgtceflPGALNLLKYLKLKNIPIALCTssNKTKfrGKTSHLEEGF---DLFDTIVTGDD 142
Cdd:cd07512   78 -------EADPPGLTRPY------PGVIEALERLRAAGWRLAICT--NKPE--APARALLSALglaDLFAAVVGGDT 137
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 132-198 8.67e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 36.36  E-value: 8.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364625 132 DLFDTIVTGDDPRiakgRGKPFPDIWQLGLKELNekfhtdIKPDECIVFEDGIPGVKSAKAFGAHVI 198
Cdd:PLN02770 149 DFFQAVIIGSECE----HAKPHPDPYLKALEVLK------VSKDHTFVFEDSVSGIKAGVAAGMPVV 205
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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