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Conserved domains on  [gi|2304517984|ref|WP_260473814|]
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HAD family hydrolase [Amycolatopsis balhimycina]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 1-125 2.91e-23

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd02588:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 216  Bit Score: 89.63  E-value: 2.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   1 MDPWPDAVDALTRLK-AEYVVCSLSNGNVALLT----HAGLP--WDCILSAETFRRYKPEPEAYHGAASVFDVLEADVML 73
Cdd:cd02588    90 LPPFPDVVAGLRRLReAGYRLAILSNGSPDLIEdvvaNAGLRdlFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILH 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2304517984  74 VAAHHDDLAAARSCGLHTAYVERPHEFGRDALKDVspslgnTLHARDLGELA 125
Cdd:cd02588   170 VASHAWDLAGARALGLRTAWINRPGEVPDPLGPAP------DFVVPDLGELA 215
 
Name Accession Description Interval E-value
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 1-125 2.91e-23

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 89.63  E-value: 2.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   1 MDPWPDAVDALTRLK-AEYVVCSLSNGNVALLT----HAGLP--WDCILSAETFRRYKPEPEAYHGAASVFDVLEADVML 73
Cdd:cd02588    90 LPPFPDVVAGLRRLReAGYRLAILSNGSPDLIEdvvaNAGLRdlFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILH 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2304517984  74 VAAHHDDLAAARSCGLHTAYVERPHEFGRDALKDVspslgnTLHARDLGELA 125
Cdd:cd02588   170 VASHAWDLAGARALGLRTAWINRPGEVPDPLGPAP------DFVVPDLGELA 215
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 1-99 5.76e-21

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 83.54  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   1 MDPWPDAVDALTRLK-AEYVVCSLSNGN----VALLTHAGL--PWDCILSAETFRRYKPEPEAYHGAASVFDVLEADVML 73
Cdd:TIGR01428  91 LPPHPDVPAGLRALKeRGYRLAILSNGSpamlKSLVKHAGLddPFDAVLSADAVRAYKPAPQVYQLALEALGVPPDEVLF 170

                          90       100
                  ....*....|....*....|....*.
gi 2304517984  74 VAAHHDDLAAARSCGLHTAYVERPHE 99
Cdd:TIGR01428 171 VASNPWDLGGAKKFGFKTAWINRPGE 196
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 2-128 1.51e-12

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: 61.58  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   2 DPWPDAVDALTRLKAE-YVVCSLSNGNV----ALLTHAGL--PWDCILSAETFRRYKPEPEAYHGAASVFDV-------- 66
Cdd:COG1011    93 EPYPDALELLEALKARgYRLALLTNGSAelqeAKLRRLGLddLFDAVVSSEEVGVRKPDPEIFELALERLGVppeealfv 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2304517984  67 ---LEADVMlvaahhddlaAARSCGLHTAYVERPHEFGRDALKDvspslgnTLHARDLGELATLL 128
Cdd:COG1011   173 gdsPETDVA----------GARAAGMRTVWVNRSGEPAPAEPRP-------DYVISDLAELLELL 220
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-74 7.75e-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: 40.26  E-value: 7.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2304517984   3 PWPDAVDALTRLKAE-YVVCSLSNGNV----ALLTHAGLP--WDCILSAETFRRYKPEPEAYHGAASVFDVLEADVMLV 74
Cdd:pfam00702  99 LYPGAAEALKALKERgIKVAILTGDNPeaaeALLRLLGLDdyFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMV 177
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 29-112 1.54e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 37.14  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   29 ALLTHAGLP---WDCILSAETFRRYKPEPEAYHGAASVFDVLEADVMLVAAHHDDLAAARSCGLHTAYVERphEFGRDAL 105
Cdd:PLN02919   193 ANLAAAGLPlsmFDAIVSADAFENLKPAPDIFLAAAKILGVPTSECVVIEDALAGVQAARAAGMRCIAVTT--TLSEEIL 270


                   ....*..
gi 2304517984  106 KDVSPSL 112
Cdd:PLN02919   271 KDAGPSL 277
 
Name Accession Description Interval E-value
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 1-125 2.91e-23

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 89.63  E-value: 2.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   1 MDPWPDAVDALTRLK-AEYVVCSLSNGNVALLT----HAGLP--WDCILSAETFRRYKPEPEAYHGAASVFDVLEADVML 73
Cdd:cd02588    90 LPPFPDVVAGLRRLReAGYRLAILSNGSPDLIEdvvaNAGLRdlFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILH 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2304517984  74 VAAHHDDLAAARSCGLHTAYVERPHEFGRDALKDVspslgnTLHARDLGELA 125
Cdd:cd02588   170 VASHAWDLAGARALGLRTAWINRPGEVPDPLGPAP------DFVVPDLGELA 215
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 1-99 5.76e-21

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 83.54  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   1 MDPWPDAVDALTRLK-AEYVVCSLSNGN----VALLTHAGL--PWDCILSAETFRRYKPEPEAYHGAASVFDVLEADVML 73
Cdd:TIGR01428  91 LPPHPDVPAGLRALKeRGYRLAILSNGSpamlKSLVKHAGLddPFDAVLSADAVRAYKPAPQVYQLALEALGVPPDEVLF 170

                          90       100
                  ....*....|....*....|....*.
gi 2304517984  74 VAAHHDDLAAARSCGLHTAYVERPHE 99
Cdd:TIGR01428 171 VASNPWDLGGAKKFGFKTAWINRPGE 196
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 2-128 1.51e-12

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: 61.58  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   2 DPWPDAVDALTRLKAE-YVVCSLSNGNV----ALLTHAGL--PWDCILSAETFRRYKPEPEAYHGAASVFDV-------- 66
Cdd:COG1011    93 EPYPDALELLEALKARgYRLALLTNGSAelqeAKLRRLGLddLFDAVVSSEEVGVRKPDPEIFELALERLGVppeealfv 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2304517984  67 ---LEADVMlvaahhddlaAARSCGLHTAYVERPHEFGRDALKDvspslgnTLHARDLGELATLL 128
Cdd:COG1011   173 gdsPETDVA----------GARAAGMRTVWVNRSGEPAPAEPRP-------DYVISDLAELLELL 220
HAD-SF-IA-v2 TIGR01493
Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid ...
 1-74 1.58e-07

Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called 'capping domain', or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model.


Pssm-ID: 130557 [Multi-domain]  Cd Length: 175  Bit Score: 47.52  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   1 MDPWPDAVDALTRLKAeyvvcsLSNGNVALL----THAGLPW--DCILSAETFRRYKPEPEAYHGAASVFDVLEADVMLV 74
Cdd:TIGR01493  89 LPPWPDSAAALARVAI------LSNASHWAFdqfaQQAGLPWyfDRAFSVDTVRAYKPDPVVYELVFDTVGLPPDRVLMV 162
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-74 7.75e-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: 40.26  E-value: 7.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2304517984   3 PWPDAVDALTRLKAE-YVVCSLSNGNV----ALLTHAGLP--WDCILSAETFRRYKPEPEAYHGAASVFDVLEADVMLV 74
Cdd:pfam00702  99 LYPGAAEALKALKERgIKVAILTGDNPeaaeALLRLLGLDdyFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMV 177
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 2-91 4.81e-04

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: 37.78  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   2 DPWPDAVDALTRLKAE-YVVCSLSNGN---VALLTHAGLpWDC---ILSAETFRRYKPEPEAYHGAASVFDVLEADVMLV 74
Cdd:TIGR01509  80 KPLPGVRALLEALRARgKKLALLTNSPrahKLVLALLGL-RDLfdvVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFV 158

                          90
                  ....*....|....*..
gi 2304517984  75 AAHHDDLAAARSCGLHT 91
Cdd:TIGR01509 159 DDSPAGIEAAKAAGMHT 175
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-72 8.63e-04

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: 37.32  E-value: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   1 MDPWPDAVDALTRLKAE-YVVCSLSNGNVALLTHAGLPWDC--------ILSAETfRRYKPEPEAYHGAASVFDVLEADV 71
Cdd:cd02603    83 VDPNPEMLDLLEALRAKgYKVYLLSNTWPDHFKFQLELLPRrgdlfdgvVESCRL-GVRKPDPEIYQLALERLGVKPEEV 161


                  .
gi 2304517984  72 M 72
Cdd:cd02603   162 L 162
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 29-112 1.54e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 37.14  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   29 ALLTHAGLP---WDCILSAETFRRYKPEPEAYHGAASVFDVLEADVMLVAAHHDDLAAARSCGLHTAYVERphEFGRDAL 105
Cdd:PLN02919   193 ANLAAAGLPlsmFDAIVSADAFENLKPAPDIFLAAAKILGVPTSECVVIEDALAGVQAARAAGMRCIAVTT--TLSEEIL 270


                   ....*..
gi 2304517984  106 KDVSPSL 112
Cdd:PLN02919   271 KDAGPSL 277
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 1-70 4.48e-03

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: 35.43  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304517984   1 MDPWPDAVDALTRLKAEYV---VCSLSN-GNVALL------THAGLPWDCILSAETFRRYKPEPEAYHGAASVFDVLEAD 70
Cdd:cd07528    94 LPLRPGVARLIDEAKAAGVrlaIATTTSpANVDALlsallgPERRAIFDAIAAGDDVAEKKPDPDIYLLALERLGVSPSD 173
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
5-66 5.07e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 35.18  E-value: 5.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2304517984   5 PDAVDALTRLKAE---YVVCSLSNGNVA--LLTHAGL-PW-DCILSAETFRRYKPEPEAYHGAASVFDV 66
Cdd:COG0637    89 PGVVELLEALKEAgikIAVATSSPRENAeaVLEAAGLlDYfDVIVTGDDVARGKPDPDIYLLAAERLGV 157
 
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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