MULTISPECIES: HAD family hydrolase [Bacillus]
Protein Classification
HAD-IIIC family phosphatase( domain architecture ID 11467521)
haloacid dehalogenase (HAD)-IIIC family phosphatase from the FkbH subfamily may be involved in methoxymalonyl-ACP biosynthesis; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| FkbH | COG3882 | Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism]; |
1-342 | 1.91e-153 | ||||||
Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism]; : Pssm-ID: 443090 [Multi-domain] Cd Length: 375 Bit Score: 436.23 E-value: 1.91e-153
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| Name | Accession | Description | Interval | E-value | ||||||
| FkbH | COG3882 | Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism]; |
1-342 | 1.91e-153 | ||||||
Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism]; Pssm-ID: 443090 [Multi-domain] Cd Length: 375 Bit Score: 436.23 E-value: 1.91e-153
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| FkbH | TIGR01686 | FkbH-like domain; This model describes a domain of a family of proteins of unknown overall ... |
5-310 | 1.52e-74 | ||||||
FkbH-like domain; This model describes a domain of a family of proteins of unknown overall function. One of these, however, is a modular polyketide synthase 4800 amino acids in length from Streptomyces avermilitis in which this domain is the C-terminal segment. By contrast, the FkbH protein from Streptomyces hygroscopicus aparently contains only this domain. The remaining members of the family all contain an additional N-terminal domain of between 200 and 275 amino acids which show less than 20% identity to one another. It seems likely then that these proteins are involved in disparate functions, probably the biosynthesis of different natural products. For instance, the FkbH gene is found in a gene cluster believed to be responsible for the biosynthesis of unususal "PKS extender units" in the ascomycin pathway. This domain is composed of two parts, the first of which is a member of subfamily IIIC (TIGR01681) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in this domain. The C-terminal portion of this domain is unique to this family (by BLAST). Pssm-ID: 273757 [Multi-domain] Cd Length: 320 Bit Score: 233.20 E-value: 1.52e-74
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| HAD_MDP-1_like | cd07501 | eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ... |
6-116 | 4.97e-35 | ||||||
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain] Cd Length: 129 Bit Score: 124.77 E-value: 4.97e-35
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| Acid_PPase | pfam12689 | Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ... |
6-112 | 3.76e-08 | ||||||
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase. Pssm-ID: 372256 Cd Length: 169 Bit Score: 52.23 E-value: 3.76e-08
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| Name | Accession | Description | Interval | E-value | ||||||
| FkbH | COG3882 | Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism]; |
1-342 | 1.91e-153 | ||||||
Predicted enzyme involved in methoxymalonyl-ACP biosynthesis [Lipid transport and metabolism]; Pssm-ID: 443090 [Multi-domain] Cd Length: 375 Bit Score: 436.23 E-value: 1.91e-153
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| FkbH | TIGR01686 | FkbH-like domain; This model describes a domain of a family of proteins of unknown overall ... |
5-310 | 1.52e-74 | ||||||
FkbH-like domain; This model describes a domain of a family of proteins of unknown overall function. One of these, however, is a modular polyketide synthase 4800 amino acids in length from Streptomyces avermilitis in which this domain is the C-terminal segment. By contrast, the FkbH protein from Streptomyces hygroscopicus aparently contains only this domain. The remaining members of the family all contain an additional N-terminal domain of between 200 and 275 amino acids which show less than 20% identity to one another. It seems likely then that these proteins are involved in disparate functions, probably the biosynthesis of different natural products. For instance, the FkbH gene is found in a gene cluster believed to be responsible for the biosynthesis of unususal "PKS extender units" in the ascomycin pathway. This domain is composed of two parts, the first of which is a member of subfamily IIIC (TIGR01681) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in this domain. The C-terminal portion of this domain is unique to this family (by BLAST). Pssm-ID: 273757 [Multi-domain] Cd Length: 320 Bit Score: 233.20 E-value: 1.52e-74
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| HAD_MDP-1_like | cd07501 | eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ... |
6-116 | 4.97e-35 | ||||||
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain] Cd Length: 129 Bit Score: 124.77 E-value: 4.97e-35
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| HAD-SF-IIIC | TIGR01681 | HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the ... |
6-114 | 3.90e-16 | ||||||
HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. Subfamily III (also including IIIA - TIGR01662 and IIIB - pfam03767) contains sequences which do not contain either of the insert domains (between the 1st and 2nd conserved catalytic motifs, subfamily I - TIGR01493, TIGR01509, TIGR01549, TIGR01488, TIGR01494, TIGR01658, TIGR01544 and TIGR01545, or between the 2nd and 3rd, subfamily II - TIGR01460 and TIGR01484). Subfamily IIIC contains five relatively distantly related clades: a family of viral proteins (TIGR01684), a family of eukaryotic proteins called MDP-1 and a family of archaeal proteins most closely related to MDP-1 (TIGR01685), a family of bacteria including the Streptomyces FkbH protein (TIGR01686), and a small clade including the Pasteurella BcbF and EcbF proteins. The overall lack of species overlap among these clades may indicate a conserved function, but the degree of divergence between the clades and the differences in archetecture outside of the domain in some clades warns against such a conclusion. No member of this subfamily is characterized with respect to function, however the MDP-1 protein is a characterized phosphatase. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC. Pssm-ID: 273752 [Multi-domain] Cd Length: 128 Bit Score: 74.00 E-value: 3.90e-16
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| COG4996 | COG4996 | Predicted phosphatase [General function prediction only]; |
6-131 | 6.29e-14 | ||||||
Predicted phosphatase [General function prediction only]; Pssm-ID: 444020 Cd Length: 165 Bit Score: 68.86 E-value: 6.29e-14
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| Acid_PPase | pfam12689 | Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ... |
6-112 | 3.76e-08 | ||||||
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase. Pssm-ID: 372256 Cd Length: 169 Bit Score: 52.23 E-value: 3.76e-08
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| HAD_2 | pfam13419 | Haloacid dehalogenase-like hydrolase; |
27-115 | 3.41e-07 | ||||||
Haloacid dehalogenase-like hydrolase; Pssm-ID: 404323 [Multi-domain] Cd Length: 178 Bit Score: 49.89 E-value: 3.41e-07
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| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
7-115 | 4.76e-07 | ||||||
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: 47.78 E-value: 4.76e-07
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| Gph | COG0546 | Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]; |
25-71 | 8.30e-07 | ||||||
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]; Pssm-ID: 440312 [Multi-domain] Cd Length: 214 Bit Score: 49.16 E-value: 8.30e-07
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| Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
18-104 | 2.73e-05 | ||||||
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: 44.50 E-value: 2.73e-05
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| HAD_BPGM-like | cd16423 | uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ... |
8-71 | 8.20e-05 | ||||||
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: 42.63 E-value: 8.20e-05
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| HAD_like | cd07506 | uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ... |
8-71 | 1.49e-04 | ||||||
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: 319809 Cd Length: 115 Bit Score: 40.82 E-value: 1.49e-04
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| HAD_BsYqeG-like | cd16416 | Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ... |
8-107 | 6.37e-04 | ||||||
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319853 [Multi-domain] Cd Length: 108 Bit Score: 38.79 E-value: 6.37e-04
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| YcjU | COG0637 | Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism]; |
21-71 | 1.11e-03 | ||||||
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 440402 [Multi-domain] Cd Length: 208 Bit Score: 39.81 E-value: 1.11e-03
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| HAD-SF-IIIA | TIGR01662 | HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ... |
6-73 | 1.56e-03 | ||||||
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273742 [Multi-domain] Cd Length: 135 Bit Score: 38.15 E-value: 1.56e-03
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| Blast search parameters | ||||
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