NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1655162436|ref|WP_137645751|]
View 

HAD family hydrolase [Lactiplantibacillus plajomi]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-98 1.34e-08

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: 50.13  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655162436   2 SIDLLVVDIDRTNLKSKNEI----------FQVKGfiygkTRLAICTASTYHDTKIRLEKLELsrceNTYMICSNGSMTF 71
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEIsprtkealrrLREKG-----IKVVIATGRPLRSALPLLEELGL----DDPLITSNGALIY 71

                          90       100
                  ....*....|....*....|....*..
gi 1655162436  72 TTDGRLIDARPLTDNTSKKyAVQVLHE 98
Cdd:COG0561    72 DPDGEVLYERPLDPEDVRE-ILELLRE 97
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-98 1.34e-08

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: 50.13  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655162436   2 SIDLLVVDIDRTNLKSKNEI----------FQVKGfiygkTRLAICTASTYHDTKIRLEKLELsrceNTYMICSNGSMTF 71
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEIsprtkealrrLREKG-----IKVVIATGRPLRSALPLLEELGL----DDPLITSNGALIY 71

                          90       100
                  ....*....|....*....|....*..
gi 1655162436  72 TTDGRLIDARPLTDNTSKKyAVQVLHE 98
Cdd:COG0561    72 DPDGEVLYERPLDPEDVRE-ILELLRE 97
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-78 1.16e-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: 39.50  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655162436   5 LLVVDIDRTNLKSKNEI----------FQVKGFiygktRLAICTASTYHDTKIRLEKLELsrceNTYMICSNGSMTFTTD 74
Cdd:cd07516     1 LIALDLDGTLLNSDKEIsprtkeaikkAKEKGI-----KVVIATGRPLRGAQPYLEELGL----DSPLITFNGALVYDPT 71


                  ....
gi 1655162436  75 GRLI 78
Cdd:cd07516    72 GKEI 75
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-84 7.31e-03

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 34.52  E-value: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655162436   6 LVVDIDRTNLKSKNEI----------FQVKGFIygktrLAICTASTYHDTKIRLEKLELsrceNTYMICSNGSMTFTTDG 75
Cdd:pfam08282   1 IASDLDGTLLNSDKKIsektkeaikkLKEKGIK-----FVIATGRPYRAILPVIKELGL----DDPVICYNGALIYDENG 71


                  ....*....
gi 1655162436  76 RLIDARPLT 84
Cdd:pfam08282  72 KILYSNPIS 80
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-98 1.34e-08

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: 50.13  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655162436   2 SIDLLVVDIDRTNLKSKNEI----------FQVKGfiygkTRLAICTASTYHDTKIRLEKLELsrceNTYMICSNGSMTF 71
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEIsprtkealrrLREKG-----IKVVIATGRPLRSALPLLEELGL----DDPLITSNGALIY 71

                          90       100
                  ....*....|....*....|....*..
gi 1655162436  72 TTDGRLIDARPLTDNTSKKyAVQVLHE 98
Cdd:COG0561    72 DPDGEVLYERPLDPEDVRE-ILELLRE 97
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-78 1.16e-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: 39.50  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655162436   5 LLVVDIDRTNLKSKNEI----------FQVKGFiygktRLAICTASTYHDTKIRLEKLELsrceNTYMICSNGSMTFTTD 74
Cdd:cd07516     1 LIALDLDGTLLNSDKEIsprtkeaikkAKEKGI-----KVVIATGRPLRGAQPYLEELGL----DSPLITFNGALVYDPT 71


                  ....
gi 1655162436  75 GRLI 78
Cdd:cd07516    72 GKEI 75
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-84 7.31e-03

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 34.52  E-value: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655162436   6 LVVDIDRTNLKSKNEI----------FQVKGFIygktrLAICTASTYHDTKIRLEKLELsrceNTYMICSNGSMTFTTDG 75
Cdd:pfam08282   1 IASDLDGTLLNSDKKIsektkeaikkLKEKGIK-----FVIATGRPYRAILPVIKELGL----DDPVICYNGALIYDENG 71


                  ....*....
gi 1655162436  76 RLIDARPLT 84
Cdd:pfam08282  72 KILYSNPIS 80
 
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