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Conserved domains on  [gi|1960451003|ref|WP_202017106|]
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MULTISPECIES: HAD-IIB family hydrolase [Clostridia]

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 ...
 25-287 3.15e-46

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 cd07517:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 213  Bit Score: 154.69  E-value: 3.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  25 KAVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTGMISACGCTIEKDGKRLFNKEMT 104
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSYVSYNGQYVFFEGEVIYKNPLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 105 TEEAWHSVEVLRKYGMIPVMEGADWMYYDKDEYNTDINWYADLitkaLGGKWRPVkgyehdlhinkisskivpgsdpeka 184
Cdd:cd07517    81 QELVERLTEFAKEQGHPVSFYGQLLLFEDEEEEQKYEELRPEL----RFVRWHPL------------------------- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 185 caeledyyefighvgeglagdTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIK 264
Cdd:cd07517   132 ---------------------STDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELK 190

                         250       260
                  ....*....|....*....|...
gi 1960451003 265 KLADYVTTDIFHYGIKNGLEHLG 287
Cdd:cd07517   191 EIADYVTKDVDEDGILKALKHFG 213
 
Name Accession Description Interval E-value
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 25-287 3.15e-46

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 154.69  E-value: 3.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  25 KAVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTGMISACGCTIEKDGKRLFNKEMT 104
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSYVSYNGQYVFFEGEVIYKNPLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 105 TEEAWHSVEVLRKYGMIPVMEGADWMYYDKDEYNTDINWYADLitkaLGGKWRPVkgyehdlhinkisskivpgsdpeka 184
Cdd:cd07517    81 QELVERLTEFAKEQGHPVSFYGQLLLFEDEEEEQKYEELRPEL----RFVRWHPL------------------------- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 185 caeledyyefighvgeglagdTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIK 264
Cdd:cd07517   132 ---------------------STDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELK 190

                         250       260
                  ....*....|....*....|...
gi 1960451003 265 KLADYVTTDIFHYGIKNGLEHLG 287
Cdd:cd07517   191 EIADYVTKDVDEDGILKALKHFG 213
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 27-273 4.57e-43

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 147.77  E-value: 4.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  27 VFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTGMISAC-GCTI-EKDGKRLFNKEMT 104
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYnGALIyDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 105 TEEAWHSVEVLRKYGMIPVMEGADWMYYDKDEYNTDINWYADLITKAlggkwRPVKGYEHDLHINKISsKIVPGSDPEKA 184
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSF-----VPEIDDFELLEDEDIN-KILILLDEEDL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 185 CAELEDYYEFIGHVGEGL--AGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPG 262
Cdd:pfam08282 155 DELEKELKELFGSLITITssGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPE 234

                         250
                  ....*....|.
gi 1960451003 263 IKKLADYVTTD 273
Cdd:pfam08282 235 VKAAADYVTDS 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 24-286 4.92e-41

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: 140.66  E-value: 4.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  24 KKAVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTG-MISACGCTI-EKDGKRLFNK 101
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDpLITSNGALIyDPDGEVLYER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 102 EMTTEEAWHSVEVLRKYGMipvmegadwmyydkdeyntdinwyadlitkalggkwrpvkgyehdlhinkisskivpgsdp 181
Cdd:COG0561    82 PLDPEDVREILELLREHGL------------------------------------------------------------- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 182 ekacaeledYYEFIGHVGEGLagdtIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAP 261
Cdd:COG0561   101 ---------HLQVVVRSGPGF----LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPP 167

                         250       260
                  ....*....|....*....|....*
gi 1960451003 262 GIKKLADYVTTDIFHYGIKNGLEHL 286
Cdd:COG0561   168 EVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 26-283 2.01e-38

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: 135.86  E-value: 2.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  26 AVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQI-PFTGMISACGCTIEKD-GKRLFNKEM 103
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELgLDTPFITANGAAVIDDqGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 104 TTEEAWHSVEVLRKYGMIPVMEGADWMYYDKDEyntdiNWYADLITKALGGKWRPVKGYEHDLH-INKISsKIVPGSDPE 182
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYASKND-----PEYFTIFKKFLGEPKLEVVDIQYLPDdILKIL-LLFLDPEDL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 183 KACAELEDYYEFIGHVGEGL-AGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAP 261
Cdd:TIGR00099 155 DLLIEALNKLELEENVSVVSsGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADE 234

                         250       260
                  ....*....|....*....|..
gi 1960451003 262 GIKKLADYVTTDIFHYGIKNGL 283
Cdd:TIGR00099 235 ELKALADYVTDSNNEDGVALAL 256
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 25-288 3.28e-19

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 84.25  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  25 KAVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTG-MISACG--CTIEKDGKRLFNK 101
Cdd:PRK01158    4 KAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGpVIAENGgvISVGFDGKRIFLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 102 EMttEEAWHSVEVLRKYgmIPVMEGADWMYyDKDEYNTDINWYADLitkalggkwrpvkgyehdlhinkisskivpgsDP 181
Cdd:PRK01158   84 DI--EECEKAYSELKKR--FPEASTSLTKL-DPDYRKTEVALRRTV--------------------------------PV 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 182 EKACAELEDYYEFIGHVGEGLAgdtIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAP 261
Cdd:PRK01158  127 EEVRELLEELGLDLEIVDSGFA---IHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADE 203

                         250       260
                  ....*....|....*....|....*..
gi 1960451003 262 GIKKLADYVTTDIFHYGIKNGLEHLGL 288
Cdd:PRK01158  204 ELKEAADYVTEKSYGEGVAEAIEHLLL 230
 
Name Accession Description Interval E-value
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 25-287 3.15e-46

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 154.69  E-value: 3.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  25 KAVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTGMISACGCTIEKDGKRLFNKEMT 104
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSYVSYNGQYVFFEGEVIYKNPLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 105 TEEAWHSVEVLRKYGMIPVMEGADWMYYDKDEYNTDINWYADLitkaLGGKWRPVkgyehdlhinkisskivpgsdpeka 184
Cdd:cd07517    81 QELVERLTEFAKEQGHPVSFYGQLLLFEDEEEEQKYEELRPEL----RFVRWHPL------------------------- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 185 caeledyyefighvgeglagdTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIK 264
Cdd:cd07517   132 ---------------------STDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELK 190

                         250       260
                  ....*....|....*....|...
gi 1960451003 265 KLADYVTTDIFHYGIKNGLEHLG 287
Cdd:cd07517   191 EIADYVTKDVDEDGILKALKHFG 213
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 27-273 4.57e-43

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 147.77  E-value: 4.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  27 VFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTGMISAC-GCTI-EKDGKRLFNKEMT 104
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYnGALIyDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 105 TEEAWHSVEVLRKYGMIPVMEGADWMYYDKDEYNTDINWYADLITKAlggkwRPVKGYEHDLHINKISsKIVPGSDPEKA 184
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSF-----VPEIDDFELLEDEDIN-KILILLDEEDL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 185 CAELEDYYEFIGHVGEGL--AGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPG 262
Cdd:pfam08282 155 DELEKELKELFGSLITITssGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPE 234

                         250
                  ....*....|.
gi 1960451003 263 IKKLADYVTTD 273
Cdd:pfam08282 235 VKAAADYVTDS 245
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 24-286 4.92e-41

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: 140.66  E-value: 4.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  24 KKAVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTG-MISACGCTI-EKDGKRLFNK 101
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDpLITSNGALIyDPDGEVLYER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 102 EMTTEEAWHSVEVLRKYGMipvmegadwmyydkdeyntdinwyadlitkalggkwrpvkgyehdlhinkisskivpgsdp 181
Cdd:COG0561    82 PLDPEDVREILELLREHGL------------------------------------------------------------- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 182 ekacaeledYYEFIGHVGEGLagdtIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAP 261
Cdd:COG0561   101 ---------HLQVVVRSGPGF----LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPP 167

                         250       260
                  ....*....|....*....|....*
gi 1960451003 262 GIKKLADYVTTDIFHYGIKNGLEHL 286
Cdd:COG0561   168 EVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 26-283 2.01e-38

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: 135.86  E-value: 2.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  26 AVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQI-PFTGMISACGCTIEKD-GKRLFNKEM 103
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELgLDTPFITANGAAVIDDqGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 104 TTEEAWHSVEVLRKYGMIPVMEGADWMYYDKDEyntdiNWYADLITKALGGKWRPVKGYEHDLH-INKISsKIVPGSDPE 182
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYASKND-----PEYFTIFKKFLGEPKLEVVDIQYLPDdILKIL-LLFLDPEDL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 183 KACAELEDYYEFIGHVGEGL-AGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAP 261
Cdd:TIGR00099 155 DLLIEALNKLELEENVSVVSsGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADE 234

                         250       260
                  ....*....|....*....|..
gi 1960451003 262 GIKKLADYVTTDIFHYGIKNGL 283
Cdd:TIGR00099 235 ELKALADYVTDSNNEDGVALAL 256
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 27-273 2.71e-36

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: 130.02  E-value: 2.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  27 VFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTG-MISACGCTI-EKDGKRLFNKEMT 104
Cdd:cd07516     2 IALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSpLITFNGALVyDPTGKEILERLIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 105 TEEAWHSVEVLRKYGMipvmegADWMYydkDEYNTDINWYADLITKALGGKWRPVKGYE--HDLHINKIsskIVPGSDPE 182
Cdd:cd07516    82 KEDVKELEEFLRKLGI------GINIY---TNDDWADTIYEENEDDEIIKPAEILDDLLlpPDEDITKI---LFVGEDEE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 183 KACAELEDYYEFIGHVGEGLAGDT-IEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAP 261
Cdd:cd07516   150 LDELIAKLPEEFFDDLSVVRSAPFyLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                         250
                  ....*....|..
gi 1960451003 262 GIKKLADYVTTD 273
Cdd:cd07516   230 EVKEAADYVTLT 241
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 205-271 1.35e-19

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. 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: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 84.17  E-value: 1.35e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1960451003 205 DTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIKKLADYVT 271
Cdd:cd07518   105 GSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVA 171
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 25-288 3.28e-19

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 84.25  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  25 KAVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTG-MISACG--CTIEKDGKRLFNK 101
Cdd:PRK01158    4 KAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGpVIAENGgvISVGFDGKRIFLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 102 EMttEEAWHSVEVLRKYgmIPVMEGADWMYyDKDEYNTDINWYADLitkalggkwrpvkgyehdlhinkisskivpgsDP 181
Cdd:PRK01158   84 DI--EECEKAYSELKKR--FPEASTSLTKL-DPDYRKTEVALRRTV--------------------------------PV 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 182 EKACAELEDYYEFIGHVGEGLAgdtIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAP 261
Cdd:PRK01158  127 EEVRELLEELGLDLEIVDSGFA---IHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADE 203

                         250       260
                  ....*....|....*....|....*..
gi 1960451003 262 GIKKLADYVTTDIFHYGIKNGLEHLGL 288
Cdd:PRK01158  204 ELKEAADYVTEKSYGEGVAEAIEHLLL 230
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 213-286 5.67e-15

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 70.31  E-value: 5.67e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1960451003 213 GFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIKKLADYVTTDIFHYGIKNGLEHL 286
Cdd:cd07514    65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKL 138
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 30-289 6.58e-15

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 72.11  E-value: 6.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  30 DADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTG-MISACGCTI--EKDGKRLFNKEMttE 106
Cdd:TIGR01482   4 DIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDpVIAENGGEIsyNEGLDDIFLAYL--E 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 107 EAWHSVEVLRKYGMIPVMegadwmyydKDEYNTDINWYadlitkalggkwrpvkgyehdlhinkissKIVPGSDPEkACA 186
Cdd:TIGR01482  82 EEWFLDIVIAKTFPFSRL---------KVQYPRRASLV-----------------------------KMRYGIDVD-TVR 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 187 ELEDYyefighVGEGL----AGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPG 262
Cdd:TIGR01482 123 EIIKE------LGLNLvavdSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPE 196

                         250       260
                  ....*....|....*....|....*..
gi 1960451003 263 IKKLADYVTTDIFHYGiknGLEHLGLI 289
Cdd:TIGR01482 197 LKEWADYVTESPYGEG---GAEAIGEI 220
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 26-256 1.22e-13

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: 68.18  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  26 AVFFDADGTICDIEKGT-PASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQI-PFTGMISACGCTIEKDGKRLFNKEM 103
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHElSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLnLPLPLIAENGALIFYPGEILYIEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 104 TTEEAWHSvevlRKYGMIPvmegaDWMYYDKDEY-NTDINWYADLITKALGGkwrPVKGYEHDLHINKISSKIvpgsdpe 182
Cdd:TIGR01484  81 DVFEEILG----IKFEEIG-----AELKSLSEHYvGTFIEDKAIAVAIHYVG---AELGQELDSKMRERLEKI------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1960451003 183 KAC-AELEDYYEFIGhvgeglagdTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAM 256
Cdd:TIGR01484 142 GRNdLELEAIYSGKT---------DLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 25-271 1.44e-13

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 68.23  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  25 KAVFFDADGTICDIEKGTPASAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQIPFTG-MISACGCTIEKDGKRLFNKEM 103
Cdd:TIGR01487   2 KLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGpVVAENGGVIFYNKEDIFLANM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 104 ttEEAWHSVEVLRKYGMIPvmegadwmyydkdeyNTDINWY-ADLITKALGGKWRPVKGYEHDLHINKISSkivpgsdpe 182
Cdd:TIGR01487  82 --EEEWFLDEEKKKRFPRD---------------RLSNEYPrASLVIMREGKDVDEVREIIKERGLNLVAS--------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 183 kacaeledyyefighvgeglaGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPG 262
Cdd:TIGR01487 136 ---------------------GFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQ 194


                  ....*....
gi 1960451003 263 IKKLADYVT 271
Cdd:TIGR01487 195 LKEIADYVT 203
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 207-272 4.69e-11

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 62.02  E-value: 4.69e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1960451003 207 IEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIKKLADYVTT 272
Cdd:PRK10513  188 LEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTK 253
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 201-286 4.80e-11

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 61.60  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 201 GLAGDtIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIKKLADYVTTDIF----H 276
Cdd:cd02605   156 GLAYD-LDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLakgpY 234

                          90
                  ....*....|.
gi 1960451003 277 Y-GIKNGLEHL 286
Cdd:cd02605   235 AgGILEGLAHF 245
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 229-273 1.01e-09

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 58.11  E-value: 1.01e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1960451003 229 IAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIKKLADYVTTD 273
Cdd:PRK10530  213 WSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGD 257
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 202-268 3.30e-08

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 52.92  E-value: 3.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1960451003 202 LAGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMgNAAPGIKKLAD 268
Cdd:COG0560   142 LTGEVVGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
PRK15126 PRK15126
HMP-PP phosphatase;
203-264 5.45e-06

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 46.61  E-value: 5.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1960451003 203 AGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIK 264
Cdd:PRK15126  176 ATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNAMPQLR 237
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 210-288 5.88e-06

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 46.49  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003 210 IPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPgiKKLADYVTT-----DIFH------YG 278
Cdd:pfam05116 159 LPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQP--ELLQWYLENardnpRIYFasgrcaGG 236

                          90
                  ....*....|
gi 1960451003 279 IKNGLEHLGL 288
Cdd:pfam05116 237 ILEGIRHFGL 246
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 202-268 8.83e-06

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 45.81  E-value: 8.83e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1960451003 202 LAGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMgNAAPGIKKLAD 268
Cdd:TIGR00338 139 LTGLVEGPIVDASYKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKAD 204
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 26-94 1.18e-05

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: 43.54  E-value: 1.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1960451003  26 AVFFDADGTICdiekgtpasAVEAITKLVKNGHQAWLCTGRSRAFVPDYLEQI----PFTGMISACGCTIEKD 94
Cdd:cd01427     1 AVLFDLDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLglgdLFDGIIGSDGGGTPKP 64
PLN02887 PLN02887
hydrolase family protein
 205-270 5.99e-05

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 44.09  E-value: 5.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1960451003 205 DTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNAAPGIKKLADYV 270
Cdd:PLN02887  497 DMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVI 562
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 26-116 4.82e-04

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. 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: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 40.74  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  26 AVFFDADGTICDIEKgTPASAV------EAITKLVKN-GHQAWLCTGRSRAFVPDYLEQIPFTgmISAC-GCTIEKDGKR 97
Cdd:cd01627     1 LLFLDYDGTLAPIVP-DPDAAVpspellEALKKLAADpKNAVAIVSGRDLDDLDKWLGLPGIG--LAGEhGAEIRLPGGG 77

                          90
                  ....*....|....*....
gi 1960451003  98 LFNKEMTTEEAWHSVEVLR 116
Cdd:cd01627    78 EWVTLAPKADLEWKEEVEA 96
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
 24-96 7.14e-04

trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species, including E. coli, Saccharomyces cerevisiae, and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids, specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM, cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme, trehalose-phosphatase, removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified, roughly half of these are of the fungal type, with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273219 [Multi-domain]  Cd Length: 244  Bit Score: 40.20  E-value: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1960451003  24 KKAVFFDADGTICDIEKgTPASAV------EAITKLVKNGH-QAWLCTGRSRAFVpDYLEQIPFTGMISACGCTIEKDGK 96
Cdd:TIGR00685   3 KRAFFFDYDGTLSEIVP-DPDAAVvsdrllTILQKLAARPHnAIWIISGRKFLEK-WLGVKLPGLGLAGEHGCEMKDNGS 80
PRK10976 PRK10976
putative hydrolase; Provisional
 207-259 4.36e-03

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 38.11  E-value: 4.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1960451003 207 IEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVAMGNA 259
Cdd:PRK10976  182 LEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNA 234
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 202-255 4.92e-03

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 37.14  E-value: 4.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1960451003 202 LAGDTIEMIPKGFSKAVGIAAVCRIFDIAHEDTIVFGDSNNDLSMFEYAKTKVA 255
Cdd:cd07500   124 LTGKVLGPIVDAQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
 
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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