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MULTISPECIES: HAD family hydrolase [Bacillus]

Protein Classification

HAD family hydrolase( domain architecture ID 11426169)

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
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-225 6.51e-12

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


:

Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 62.85  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   2 IFASDLDQTLIYSRKSfrapiedesiqlietldgkeisfISHKTISLLKKLQLHSH-FIPVTTRTIEQFQRIalFQDEII 80
Cdd:COG0561    4 LIALDLDGTLLNDDGE-----------------------ISPRTKEALRRLREKGIkVVIATGRPLRSALPL--LEELGL 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524  81 PEYVITSNGGNILHNGKqdgtwnrtvkerlsvECIERNDIlkefgqiahkdwviSQKTADDLFHYCiiKRENIPYDEL-S 159
Cdd:COG0561   59 DDPLITSNGALIYDPDG---------------EVLYERPL--------------DPEDVREILELL--REHGLHLQVVvR 107

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446497524 160 SFTSWLDkqgwnhslqgrklyFVPKPINKWDAVQYIKEILQIDT--IITAGDSLLDLCMLEKANHAFA 225
Cdd:COG0561  108 SGPGFLE--------------ILPKGVSKGSALKKLAERLGIPPeeVIAFGDSGNDLEMLEAAGLGVA 161
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-225 6.51e-12

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 62.85  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   2 IFASDLDQTLIYSRKSfrapiedesiqlietldgkeisfISHKTISLLKKLQLHSH-FIPVTTRTIEQFQRIalFQDEII 80
Cdd:COG0561    4 LIALDLDGTLLNDDGE-----------------------ISPRTKEALRRLREKGIkVVIATGRPLRSALPL--LEELGL 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524  81 PEYVITSNGGNILHNGKqdgtwnrtvkerlsvECIERNDIlkefgqiahkdwviSQKTADDLFHYCiiKRENIPYDEL-S 159
Cdd:COG0561   59 DDPLITSNGALIYDPDG---------------EVLYERPL--------------DPEDVREILELL--REHGLHLQVVvR 107

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446497524 160 SFTSWLDkqgwnhslqgrklyFVPKPINKWDAVQYIKEILQIDT--IITAGDSLLDLCMLEKANHAFA 225
Cdd:COG0561  108 SGPGFLE--------------ILPKGVSKGSALKKLAERLGIPPeeVIAFGDSGNDLEMLEAAGLGVA 161
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 3-225 4.98e-08

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 52.63  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524    3 FASDLDQTLIYSRKSfrapiedesiqlietldgkeisfISHKTISLLKKLQLHSH-FIPVTTRTIEQFQRIalFQDEIIP 81
Cdd:pfam08282   1 IASDLDGTLLNSDKK-----------------------ISEKTKEAIKKLKEKGIkFVIATGRPYRAILPV--IKELGLD 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   82 EYVITSNGGNILHNGKQDgtwnrTVKERLSVECIErnDILKEFGQIaHKDWVISqkTADDLFHYcIIKRENIPYDELSSF 161
Cdd:pfam08282  56 DPVICYNGALIYDENGKI-----LYSNPISKEAVK--EIIEYLKEN-NLEILLY--TDDGVYIL-NDNELEKILKELNYT 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524  162 TSWLDKQGWNHSLQGRKLY-------------------------------------FVPKPINKWDAVQYIKEILQIDT- 203
Cdd:pfam08282 125 KSFVPEIDDFELLEDEDINkililldeedldelekelkelfgslititssgpgyleIMPKGVSKGTALKALAKHLNISLe 204

                         250       260
                  ....*....|....*....|...
gi 446497524  204 -IITAGDSLLDLCMLEKANHAFA 225
Cdd:pfam08282 205 eVIAFGDGENDIEMLEAAGLGVA 227
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 2-226 2.57e-06

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 46.99  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524    2 IFASDLDQTLiysrksfrapiedesiqlietLDGKEISfISHKTISLLKKLQLHSH-FIPVTTRTIEQFQRiaLFQDEII 80
Cdd:TIGR01484   1 LLFFDLDGTL---------------------LDPNAHE-LSPETIEALERLREAGVkVVIVTGRSLAEIKE--LLKQLNL 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   81 PEYVITSNGGNI-LHNGKQDGTWNRTVKERLSVECIERNDILKEFgqiahKDWVISQKTADDLFHYCIIKRENIPYDEL- 158
Cdd:TIGR01484  57 PLPLIAENGALIfYPGEILYIEPSDVFEEILGIKFEEIGAELKSL-----SEHYVGTFIEDKAIAVAIHYVGAELGQELd 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446497524  159 SSFTSWLDKQGWN------HSLQGRKLYFVPKPINKWDAVQYIKEILQI--DTIITAGDSLLDLCMLEKANHAFAP 226
Cdd:TIGR01484 132 SKMRERLEKIGRNdleleaIYSGKTDLEVLPAGVNKGSALQALLQELNGkkDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_like cd07520
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 5-102 6.02e-06

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


Pssm-ID: 319822  Cd Length: 144  Bit Score: 45.13  E-value: 6.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   5 SDLDQTLIYSRKSFRAPIEDESIQLieTLDGKEISFISHKTISLLKKLQLHSHFIPVTTRTIEQFQRIAL-FQdeiipEY 83
Cdd:cd07520    4 VDLDDTLFQTARKLPGHGRLAPATV--DKRGNALSYMTPAQTAFVDWLLAGAVLIPVTARSVEAMSRVTLpFR-----SW 76

                         90       100
                 ....*....|....*....|
gi 446497524  84 VITSNGGNILH-NGKQDGTW 102
Cdd:cd07520   77 AICSHGGVILTpDGEPDPEW 96
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-225 6.51e-12

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 62.85  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   2 IFASDLDQTLIYSRKSfrapiedesiqlietldgkeisfISHKTISLLKKLQLHSH-FIPVTTRTIEQFQRIalFQDEII 80
Cdd:COG0561    4 LIALDLDGTLLNDDGE-----------------------ISPRTKEALRRLREKGIkVVIATGRPLRSALPL--LEELGL 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524  81 PEYVITSNGGNILHNGKqdgtwnrtvkerlsvECIERNDIlkefgqiahkdwviSQKTADDLFHYCiiKRENIPYDEL-S 159
Cdd:COG0561   59 DDPLITSNGALIYDPDG---------------EVLYERPL--------------DPEDVREILELL--REHGLHLQVVvR 107

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446497524 160 SFTSWLDkqgwnhslqgrklyFVPKPINKWDAVQYIKEILQIDT--IITAGDSLLDLCMLEKANHAFA 225
Cdd:COG0561  108 SGPGFLE--------------ILPKGVSKGSALKKLAERLGIPPeeVIAFGDSGNDLEMLEAAGLGVA 161
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 3-225 4.98e-08

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 52.63  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524    3 FASDLDQTLIYSRKSfrapiedesiqlietldgkeisfISHKTISLLKKLQLHSH-FIPVTTRTIEQFQRIalFQDEIIP 81
Cdd:pfam08282   1 IASDLDGTLLNSDKK-----------------------ISEKTKEAIKKLKEKGIkFVIATGRPYRAILPV--IKELGLD 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   82 EYVITSNGGNILHNGKQDgtwnrTVKERLSVECIErnDILKEFGQIaHKDWVISqkTADDLFHYcIIKRENIPYDELSSF 161
Cdd:pfam08282  56 DPVICYNGALIYDENGKI-----LYSNPISKEAVK--EIIEYLKEN-NLEILLY--TDDGVYIL-NDNELEKILKELNYT 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524  162 TSWLDKQGWNHSLQGRKLY-------------------------------------FVPKPINKWDAVQYIKEILQIDT- 203
Cdd:pfam08282 125 KSFVPEIDDFELLEDEDINkililldeedldelekelkelfgslititssgpgyleIMPKGVSKGTALKALAKHLNISLe 204

                         250       260
                  ....*....|....*....|...
gi 446497524  204 -IITAGDSLLDLCMLEKANHAFA 225
Cdd:pfam08282 205 eVIAFGDGENDIEMLEAAGLGVA 227
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 2-226 2.57e-06

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 46.99  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524    2 IFASDLDQTLiysrksfrapiedesiqlietLDGKEISfISHKTISLLKKLQLHSH-FIPVTTRTIEQFQRiaLFQDEII 80
Cdd:TIGR01484   1 LLFFDLDGTL---------------------LDPNAHE-LSPETIEALERLREAGVkVVIVTGRSLAEIKE--LLKQLNL 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   81 PEYVITSNGGNI-LHNGKQDGTWNRTVKERLSVECIERNDILKEFgqiahKDWVISQKTADDLFHYCIIKRENIPYDEL- 158
Cdd:TIGR01484  57 PLPLIAENGALIfYPGEILYIEPSDVFEEILGIKFEEIGAELKSL-----SEHYVGTFIEDKAIAVAIHYVGAELGQELd 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446497524  159 SSFTSWLDKQGWN------HSLQGRKLYFVPKPINKWDAVQYIKEILQI--DTIITAGDSLLDLCMLEKANHAFAP 226
Cdd:TIGR01484 132 SKMRERLEKIGRNdleleaIYSGKTDLEVLPAGVNKGSALQALLQELNGkkDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_like cd07520
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 5-102 6.02e-06

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


Pssm-ID: 319822  Cd Length: 144  Bit Score: 45.13  E-value: 6.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   5 SDLDQTLIYSRKSFRAPIEDESIQLieTLDGKEISFISHKTISLLKKLQLHSHFIPVTTRTIEQFQRIAL-FQdeiipEY 83
Cdd:cd07520    4 VDLDDTLFQTARKLPGHGRLAPATV--DKRGNALSYMTPAQTAFVDWLLAGAVLIPVTARSVEAMSRVTLpFR-----SW 76

                         90       100
                 ....*....|....*....|
gi 446497524  84 VITSNGGNILH-NGKQDGTW 102
Cdd:cd07520   77 AICSHGGVILTpDGEPDPEW 96
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 2-225 8.71e-06

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 45.72  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524    2 IFASDLDQTLIysrksfrapiedesiqlietLDGKEISfisHKTISLLKKLQLHSH-FIPVTTRTIEQFQRIalFQDEII 80
Cdd:TIGR00099   1 LIFIDLDGTLL--------------------NDDHTIS---PSTKEALAKLREKGIkVVLATGRPYKEVKNI--LKELGL 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   81 PEYVITSNGGNILHNGKQDGTwnrtvKERLSVECIER-NDILKEFGQIAH--KDWVISQKTADD---------LFHYCII 148
Cdd:TIGR00099  56 DTPFITANGAAVIDDQGEILY-----KKPLDLDLVEEiLNFLKKHGLDVIlyGDDSIYASKNDPeyftifkkfLGEPKLE 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524  149 KREN--------------IPYDELSSFTSWLDKQGW--NHSLQGRKLYFV---PKPINKWDAVQYIKEILQI--DTIITA 207
Cdd:TIGR00099 131 VVDIqylpddilkilllfLDPEDLDLLIEALNKLELeeNVSVVSSGPYSIeitAKGVSKGSALQSLAEALGIslEDVIAF 210

                         250
                  ....*....|....*...
gi 446497524  208 GDSLLDLCMLEKANHAFA 225
Cdd:TIGR00099 211 GDGMNDIEMLEAAGYGVA 228
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 2-225 1.20e-04

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 42.58  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524   2 IFASDLDQTLIYSRKSfrapiedesiqlietldgkeisfISHKTISLLKKLQ-LHSHFIPVTTRTIEQFQRIAlfqDEI- 79
Cdd:cd07516    1 LIALDLDGTLLNSDKE-----------------------ISPRTKEAIKKAKeKGIKVVIATGRPLRGAQPYL---EELg 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524  80 IPEYVITSNGGNILHngkqdgtwnrTVKERLSVECIERNDI--LKEFGQIAHKDWVISQKTADDLFHY------------ 145
Cdd:cd07516   55 LDSPLITFNGALVYD----------PTGKEILERLISKEDVkeLEEFLRKLGIGINIYTNDDWADTIYeeneddeiikpa 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446497524 146 ------------------CIIKRENIPYDELSSFTSWLDK----QGWNHslqgrKLYFVPKPINKWDAVQYIKEILQIDT 203
Cdd:cd07516  125 eilddlllppdeditkilFVGEDEELDELIAKLPEEFFDDlsvvRSAPF-----YLEIMPKGVSKGNALKKLAEYLGISL 199

                        250       260
                 ....*....|....*....|....
gi 446497524 204 --IITAGDSLLDLCMLEKANHAFA 225
Cdd:cd07516  200 eeVIAFGDNENDLSMLEYAGLGVA 223
 
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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