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Conserved domains on  [gi|544687646|ref|WP_021119285|]
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Cof-type HAD-IIB family hydrolase [Glaesserella parasuis]

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 ...
9-267 3.89e-73

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: 222.87  E-value: 3.89e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   9 KIVFFDIDETLYyKKETRIPLSISEqVLPRLRAKGIIPAIATGRTygafPKAIKPLMNEKGFDLFVTTNGQYNLYRDQVI 88
Cdd:cd07517    1 KIVFFDIDGTLL-DEDTTIPESTKE-AIAALKEKGILVVIATGRA----PFEIQPIVKALGIDSYVSYNGQYVFFEGEVI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  89 SEYPLTTERIERILAKLQALQIEYAFVTaeqiavskntaeveeslrpikedyivdpnfyldhsviQLLVFFPQERTEEVI 168
Cdd:cd07517   75 YKNPLPQELVERLTEFAKEQGHPVSFYG-------------------------------------QLLLFEDEEEEQKYE 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 169 RsgiLEDDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVAD 248
Cdd:cd07517  118 E---LRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIAD 194
                        250
                 ....*....|....*....
gi 544687646 249 YVTLPIEQDGILVALEKLG 267
Cdd:cd07517  195 YVTKDVDEDGILKALKHFG 213
 
Name Accession Description Interval E-value
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
9-267 3.89e-73

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: 222.87  E-value: 3.89e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   9 KIVFFDIDETLYyKKETRIPLSISEqVLPRLRAKGIIPAIATGRTygafPKAIKPLMNEKGFDLFVTTNGQYNLYRDQVI 88
Cdd:cd07517    1 KIVFFDIDGTLL-DEDTTIPESTKE-AIAALKEKGILVVIATGRA----PFEIQPIVKALGIDSYVSYNGQYVFFEGEVI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  89 SEYPLTTERIERILAKLQALQIEYAFVTaeqiavskntaeveeslrpikedyivdpnfyldhsviQLLVFFPQERTEEVI 168
Cdd:cd07517   75 YKNPLPQELVERLTEFAKEQGHPVSFYG-------------------------------------QLLLFEDEEEEQKYE 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 169 RsgiLEDDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVAD 248
Cdd:cd07517  118 E---LRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIAD 194
                        250
                 ....*....|....*....
gi 544687646 249 YVTLPIEQDGILVALEKLG 267
Cdd:cd07517  195 YVTKDVDEDGILKALKHFG 213
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
7-266 2.05e-54

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: 174.17  E-value: 2.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   7 PIKIVFFDIDETLYYKKETriplsISEQVLP---RLRAKGIIPAIATGRTYgafpKAIKPLMNEKGF-DLFVTTNGQYNL 82
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGE-----ISPRTKEalrRLREKGIKVVIATGRPL----RSALPLLEELGLdDPLITSNGALIY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  83 YR-DQVISEYPLTTERIERILAKLQALQIEYAFVTaeqiavskntaeveeslrpikedyivdpnfyldhsviqllvffpq 161
Cdd:COG0561   72 DPdGEVLYERPLDPEDVREILELLREHGLHLQVVV--------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 162 erteevirsgileddlkevRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAED 241
Cdd:COG0561  107 -------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPP 167
                        250       260
                 ....*....|....*....|....*
gi 544687646 242 ELKAVADYVTLPIEQDGILVALEKL 266
Cdd:COG0561  168 EVKAAADYVTGSNDEDGVAEALEKL 192
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
11-263 1.69e-52

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 171.27  E-value: 1.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   11 VFFDIDETL--YYKKetriplsISEQ---VLPRLRAKGIIPAIATGRTYgafpKAIKPLMNEKGFDLFV-TTNGQY-NLY 83
Cdd:pfam08282   1 IASDLDGTLlnSDKK-------ISEKtkeAIKKLKEKGIKFVIATGRPY----RAILPVIKELGLDDPViCYNGALiYDE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   84 RDQVISEYPLTTERIERILAKLQALQIEYAFVTAEQIAVSKNTAEVEESLR----PIKEDYIVDPNFYLDHSVIQLLVFF 159
Cdd:pfam08282  70 NGKILYSNPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKElnytKSFVPEIDDFELLEDEDINKILILL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  160 PQERTEEVIRsgILEDDLKE----VRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVA 235
Cdd:pfam08282 150 DEEDLDELEK--ELKELFGSlitiTSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVA 227
                         250       260
                  ....*....|....*....|....*...
gi 544687646  236 MGNAEDELKAVADYVTLPIEQDGILVAL 263
Cdd:pfam08282 228 MGNASPEVKAAADYVTDSNNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
10-263 1.18e-46

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: 156.27  E-value: 1.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   10 IVFFDIDETLYYKKETRIPLSIseQVLPRLRAKGIIPAIATGRTYgafpKAIKPLMNEKGFDL-FVTTNGQYNLYRD-QV 87
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTK--EALAKLREKGIKVVLATGRPY----KEVKNILKELGLDTpFITANGAAVIDDQgEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   88 ISEYPLTTERIERILAKLQALQIEYAFVTAEQIAVSKNTAEVEESLRP--IKEDYIVDPNFYLDHSVI-QLLVFFPQERT 164
Cdd:TIGR00099  75 LYKKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKflGEPKLEVVDIQYLPDDILkILLLFLDPEDL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  165 ---EEVIRSGILEDDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAED 241
Cdd:TIGR00099 155 dllIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADE 234
                         250       260
                  ....*....|....*....|..
gi 544687646  242 ELKAVADYVTLPIEQDGILVAL 263
Cdd:TIGR00099 235 ELKALADYVTDSNNEDGVALAL 256
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
9-259 3.96e-25

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 100.48  E-value: 3.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   9 KIVFFDIDETLYYKKETRIPLSISeqVLPRLRAKGIIPAIATGRTYgafpKAIKPLMNEKGFDL-FVTTNGQYnLYRDQ- 86
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLE--ALARAREAGYKVIIVTGRHH----VAIHPFYQALALDTpAICCNGTY-LYDYQa 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  87 --VISEYPLTTERIERILAKLQALQIE----------YAFVTAEQIAVSKNTAEVEESLRPI------KEDYIVDPN--- 145
Cdd:PRK10530  77 kkVLEADPLPVQQALQVIEMLDEHQIHglmyvddamlYEHPTGHVIRTLNWAQTLPPEQRPTftqvdsLAQAARQVNaiw 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 146 -FYLDHSVIQLLvffpQERTEEVirsgilEDDLK---EVRWHKySVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGL 221
Cdd:PRK10530 157 kFALTHEDLPQL----QHFAKHV------EHELGlecEWSWHD-QVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNF 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 544687646 222 NDLEMIAAVGFGVAMGNAEDELKAVADYVTLPIEQDGI 259
Cdd:PRK10530 226 NDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSI 263
 
Name Accession Description Interval E-value
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
9-267 3.89e-73

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: 222.87  E-value: 3.89e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   9 KIVFFDIDETLYyKKETRIPLSISEqVLPRLRAKGIIPAIATGRTygafPKAIKPLMNEKGFDLFVTTNGQYNLYRDQVI 88
Cdd:cd07517    1 KIVFFDIDGTLL-DEDTTIPESTKE-AIAALKEKGILVVIATGRA----PFEIQPIVKALGIDSYVSYNGQYVFFEGEVI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  89 SEYPLTTERIERILAKLQALQIEYAFVTaeqiavskntaeveeslrpikedyivdpnfyldhsviQLLVFFPQERTEEVI 168
Cdd:cd07517   75 YKNPLPQELVERLTEFAKEQGHPVSFYG-------------------------------------QLLLFEDEEEEQKYE 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 169 RsgiLEDDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVAD 248
Cdd:cd07517  118 E---LRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIAD 194
                        250
                 ....*....|....*....
gi 544687646 249 YVTLPIEQDGILVALEKLG 267
Cdd:cd07517  195 YVTKDVDEDGILKALKHFG 213
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
7-266 2.05e-54

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: 174.17  E-value: 2.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   7 PIKIVFFDIDETLYYKKETriplsISEQVLP---RLRAKGIIPAIATGRTYgafpKAIKPLMNEKGF-DLFVTTNGQYNL 82
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGE-----ISPRTKEalrRLREKGIKVVIATGRPL----RSALPLLEELGLdDPLITSNGALIY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  83 YR-DQVISEYPLTTERIERILAKLQALQIEYAFVTaeqiavskntaeveeslrpikedyivdpnfyldhsviqllvffpq 161
Cdd:COG0561   72 DPdGEVLYERPLDPEDVREILELLREHGLHLQVVV--------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 162 erteevirsgileddlkevRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAED 241
Cdd:COG0561  107 -------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPP 167
                        250       260
                 ....*....|....*....|....*
gi 544687646 242 ELKAVADYVTLPIEQDGILVALEKL 266
Cdd:COG0561  168 EVKAAADYVTGSNDEDGVAEALEKL 192
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
11-263 1.69e-52

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 171.27  E-value: 1.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   11 VFFDIDETL--YYKKetriplsISEQ---VLPRLRAKGIIPAIATGRTYgafpKAIKPLMNEKGFDLFV-TTNGQY-NLY 83
Cdd:pfam08282   1 IASDLDGTLlnSDKK-------ISEKtkeAIKKLKEKGIKFVIATGRPY----RAILPVIKELGLDDPViCYNGALiYDE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   84 RDQVISEYPLTTERIERILAKLQALQIEYAFVTAEQIAVSKNTAEVEESLR----PIKEDYIVDPNFYLDHSVIQLLVFF 159
Cdd:pfam08282  70 NGKILYSNPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKElnytKSFVPEIDDFELLEDEDINKILILL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  160 PQERTEEVIRsgILEDDLKE----VRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVA 235
Cdd:pfam08282 150 DEEDLDELEK--ELKELFGSlitiTSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVA 227
                         250       260
                  ....*....|....*....|....*...
gi 544687646  236 MGNAEDELKAVADYVTLPIEQDGILVAL 263
Cdd:pfam08282 228 MGNASPEVKAAADYVTDSNNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
10-263 1.18e-46

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: 156.27  E-value: 1.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   10 IVFFDIDETLYYKKETRIPLSIseQVLPRLRAKGIIPAIATGRTYgafpKAIKPLMNEKGFDL-FVTTNGQYNLYRD-QV 87
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTK--EALAKLREKGIKVVLATGRPY----KEVKNILKELGLDTpFITANGAAVIDDQgEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   88 ISEYPLTTERIERILAKLQALQIEYAFVTAEQIAVSKNTAEVEESLRP--IKEDYIVDPNFYLDHSVI-QLLVFFPQERT 164
Cdd:TIGR00099  75 LYKKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKflGEPKLEVVDIQYLPDDILkILLLFLDPEDL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  165 ---EEVIRSGILEDDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAED 241
Cdd:TIGR00099 155 dllIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADE 234
                         250       260
                  ....*....|....*....|..
gi 544687646  242 ELKAVADYVTLPIEQDGILVAL 263
Cdd:TIGR00099 235 ELKALADYVTDSNNEDGVALAL 256
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
10-265 6.54e-43

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: 146.59  E-value: 6.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  10 IVFFDIDETLYYKKETriplsISE---QVLPRLRAKGIIPAIATGRTYgafpKAIKPLMNEKGFDLFVTT-NGQ--YNLY 83
Cdd:cd07516    1 LIALDLDGTLLNSDKE-----ISPrtkEAIKKAKEKGIKVVIATGRPL----RGAQPYLEELGLDSPLITfNGAlvYDPT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  84 RDQVISEYPlTTERIERILAKLQALQIEYAFVTAEQIAVSKNTaEVEESLRPIKEDYIVDPNFYLDHSVIQLLVFFPQER 163
Cdd:cd07516   72 GKEILERLI-SKEDVKELEEFLRKLGIGINIYTNDDWADTIYE-ENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 164 TEEVIRSGILE--DDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAED 241
Cdd:cd07516  150 LDELIAKLPEEffDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229
                        250       260
                 ....*....|....*....|....
gi 544687646 242 ELKAVADYVTLPIEQDGILVALEK 265
Cdd:cd07516  230 EVKEAADYVTLTNNEDGVAKAIEK 253
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
9-259 3.96e-25

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 100.48  E-value: 3.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   9 KIVFFDIDETLYYKKETRIPLSISeqVLPRLRAKGIIPAIATGRTYgafpKAIKPLMNEKGFDL-FVTTNGQYnLYRDQ- 86
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLE--ALARAREAGYKVIIVTGRHH----VAIHPFYQALALDTpAICCNGTY-LYDYQa 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  87 --VISEYPLTTERIERILAKLQALQIE----------YAFVTAEQIAVSKNTAEVEESLRPI------KEDYIVDPN--- 145
Cdd:PRK10530  77 kkVLEADPLPVQQALQVIEMLDEHQIHglmyvddamlYEHPTGHVIRTLNWAQTLPPEQRPTftqvdsLAQAARQVNaiw 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 146 -FYLDHSVIQLLvffpQERTEEVirsgilEDDLK---EVRWHKySVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGL 221
Cdd:PRK10530 157 kFALTHEDLPQL----QHFAKHV------EHELGlecEWSWHD-QVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNF 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 544687646 222 NDLEMIAAVGFGVAMGNAEDELKAVADYVTLPIEQDGI 259
Cdd:PRK10530 226 NDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSI 263
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
96-264 3.09e-23

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: 93.42  E-value: 3.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  96 ERIERILAKLQALQIEYAFVTAEQIAVSKNT-AEVEESLrpikeDYIVDPNFYLdhsVIQLLVFFPQERTEEVIrsGILE 174
Cdd:cd07518   21 ERFFAILDQLLKKGIKFVVASGRQYYQLISFfPEIKDEM-----SFVAENGAVV---YFKFTLNVPDEAAPDII--DELN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 175 DDL-KEVRWH---KYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVADYV 250
Cdd:cd07518   91 QKFgGILRAVtsgFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYV 170
                        170
                 ....*....|....
gi 544687646 251 TLPIEQDGILVALE 264
Cdd:cd07518  171 APSNNENGVLQVIE 184
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
7-265 6.93e-22

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 91.68  E-value: 6.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   7 PIKIVFFDIDETLYYKKETRIPLSisEQVLPRLRAKGIIPAIATGRTYGAFPKAIKPLMNEKGFDLFVTTNG---QYNLY 83
Cdd:PRK10513   2 AIKLIAIDMDGTLLLPDHTISPAV--KQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGalvQKAAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  84 RDqVISEYPLT------TERIERIL-AKLQALQIEYAFvTAEQiAVSKNTA-------------EVEE---SLRPIKEdY 140
Cdd:PRK10513  80 GE-TVAQTALSyddylyLEKLSREVgVHFHALDRNTLY-TANR-DISYYTVhesfltgiplvfrEVEKmdpNLQFPKV-M 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 141 IVDPNFYLDHSVIQLlvffPQERTEeviRSGILeddlkevRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDG 220
Cdd:PRK10513 156 MIDEPEILDAAIARI----PAEVKE---RYTVL-------KSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQ 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 544687646 221 LNDLEMIAAVGFGVAMGNAEDELKAVADYVTLPIEQDGILVALEK 265
Cdd:PRK10513 222 ENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
166-267 1.27e-17

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 79.25  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 166 EVIRSGILEDDLK-EVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELK 244
Cdd:PRK01158 127 EEVRELLEELGLDlEIVDSGFAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELK 206
                         90       100
                 ....*....|....*....|...
gi 544687646 245 AVADYVTLPIEQDGILVALEKLG 267
Cdd:PRK01158 207 EAADYVTEKSYGEGVAEAIEHLL 229
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
10-236 4.24e-16

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: 74.72  E-value: 4.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   10 IVFFDIDETLYYKKETRIPLSISEQvLPRLRAKGIIPAIATGRTygafPKAIKPLMNEKGFDLFVTTNGQYnlyrdqvis 89
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEA-LERLREAGVKVVIVTGRS----LAEIKELLKQLNLPLPLIAENGA--------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   90 eypltterieriLAKLQALQIEYAFVTAEQIAVSKNTAEVEESLRPIKEDYIV----DPNFYLDHSVIQLLVF--FPQER 163
Cdd:TIGR01484  67 ------------LIFYPGEILYIEPSDVFEEILGIKFEEIGAELKSLSEHYVGtfieDKAIAVAIHYVGAELGqeLDSKM 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544687646  164 TEEVIRSGILEDDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAM 236
Cdd:TIGR01484 135 RERLEKIGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
195-266 4.20e-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: 4.20e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544687646 195 SKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVADYVTLPIEQDGILVALEKL 266
Cdd:cd07514   67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKL 138
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
14-251 1.40e-14

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: 70.95  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   14 DIDETLYYKKETripLSISEQVLPRLR-AKGIIPAIATGRTYgAFPKAIKPLMNEKgfDLFVTTNG---QYNLYRDQVIS 89
Cdd:TIGR01482   4 DIDGTLTDPNRA---INESALEAIRKAeSKGIPVVLVTGNSV-QFARALAKLIGTP--DPVIAENGgeiSYNEGLDDIFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   90 EYpLTTERIERILAKLqalqieyafvtAEQIAVSKNTAEVEESlrPIKEDYIVDPNFyldhsviqllvffpqerTEEVIR 169
Cdd:TIGR01482  78 AY-LEEEWFLDIVIAK-----------TFPFSRLKVQYPRRAS--LVKMRYGIDVDT-----------------VREIIK 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  170 SGILEddLKEVRwHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVADY 249
Cdd:TIGR01482 127 ELGLN--LVAVD-SGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADY 203

                  ..
gi 544687646  250 VT 251
Cdd:TIGR01482 204 VT 205
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
10-266 6.25e-14

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: 69.30  E-value: 6.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  10 IVFFDIDETLYYKKETRIPLSISEQVLPRLRAK-GIIPAIATGRTygafPKAIKPLMnekgfdlfvttnGQYNLYRDQVI 88
Cdd:cd02605    1 LLVSDLDETLVGHDTNLQALERLQDLLEQLTADnDVILVYATGRS----PESVLELI------------KEVMLPKPDFI 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  89 -----SE-YPLTTERIERILAKLQALQIEYAFVTAEQIAVSKNT--AEVEESLRPIKEdyivdpNFYLDHSVIQLLVffp 160
Cdd:cd02605   65 isdvgTEiYYGESGYLEPDTYWNEVLSEGWERFLFEAIADLFKQlkPQSELEQNPHKI------SFYLDPQNDAAVI--- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 161 qERTEEVIRSgiLEDDLKEVRW--HKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGN 238
Cdd:cd02605  136 -EQLEEMLLK--AGLTVRIIYSsgLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGN 212
                        250       260       270
                 ....*....|....*....|....*....|...
gi 544687646 239 AEDELKAVADYVTLPI-----EQDGILVALEKL 266
Cdd:cd02605  213 AQPELLKWADRVTRSRlakgpYAGGILEGLAHF 245
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
8-251 1.27e-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: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646    8 IKIVFFDIDETLYYKKeTRIPLSISEQVlPRLRAKGIIPAIATGRTYgAFPKAIKPLMNEKGfdLFVTTNGQYNLYRDqv 87
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPN-RMISERAIEAI-RKAEKKGIPVSLVTGNTV-PFARALAVLIGTSG--PVVAENGGVIFYNK-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   88 iseypltterierilaklqalqIEYAFVTAEqiavsKNTAEVEEslrpIKEDYIVDpNFYLDHSVIQLLVFFPQERTEEV 167
Cdd:TIGR01487  74 ----------------------EDIFLANME-----EEWFLDEE----KKKRFPRD-RLSNEYPRASLVIMREGKDVDEV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  168 IRsgILEDDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVA 247
Cdd:TIGR01487 122 RE--IIKERGLNLVASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIA 199

                  ....
gi 544687646  248 DYVT 251
Cdd:TIGR01487 200 DYVT 203
PLN02887 PLN02887
hydrolase family protein
195-263 2.86e-11

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 63.35  E-value: 2.86e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544687646 195 SKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVADYVTLPIEQDGILVAL 263
Cdd:PLN02887 507 SKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
6-248 1.26e-09

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: 56.77  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   6 APIKIVFFDIDETLyykketrIPLSISEQVLPRLRAKGIIPAIATGRTYGAFPKA---------------IKPLmneKGF 70
Cdd:COG0560    1 RKMRLAVFDLDGTL-------IAGESIDELARFLGRRGLVDRREVLEEVAAITERamageldfeeslrfrVALL---AGL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  71 DLfvttnGQYNLYRDQVISEYPLTTERIERILAKLQALQIEYAFVTA--EQIAvskntaeveeslRPIKEDYIVDpnfyl 148
Cdd:COG0560   71 PE-----EELEELAERLFEEVPRLYPGARELIAEHRAAGHKVAIVSGgfTFFV------------EPIAERLGID----- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646 149 dHSV-IQLlvffpqerteeVIRSGILEDDLKEVRWHKysvdllnknNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMI 227
Cdd:COG0560  129 -HVIaNEL-----------EVEDGRLTGEVVGPIVDG---------EGKAEALRELAAELGIDLEQSYAYGDSANDLPML 187
                        250       260
                 ....*....|....*....|.
gi 544687646 228 AAVGFGVAMgNAEDELKAVAD 248
Cdd:COG0560  188 EAAGLPVAV-NPDPALREAAD 207
PRK15126 PRK15126
HMP-PP phosphatase;
205-245 2.22e-09

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 56.63  E-value: 2.22e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 544687646 205 NHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKA 245
Cdd:PRK15126 198 QHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNAMPQLRA 238
PRK10976 PRK10976
putative hydrolase; Provisional
195-244 1.31e-08

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 54.28  E-value: 1.31e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 544687646 195 SKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELK 244
Cdd:PRK10976 190 SKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNAHQRLK 239
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
196-251 2.02e-08

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 52.36  E-value: 2.02e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544687646 196 KARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVADYVT 251
Cdd:COG1778   84 KLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVT 139
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
194-248 2.00e-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: 47.35  E-value: 2.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 544687646  194 NSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMgNAEDELKAVAD 248
Cdd:TIGR00338 151 SYKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKAD 204
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
200-251 1.81e-05

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 43.66  E-value: 1.81e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 544687646 200 IEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVADYVT 251
Cdd:cd01630   81 LEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT 132
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
7-262 2.45e-05

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: 44.56  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646    7 PIKIVFFDIDETLyykketripLSISEQVLPRLRA------KGIIPAIATGRTygafPKAIKPLMNEKGF---DLFVTTN 77
Cdd:pfam05116   1 PPLLLVSDLDNTL---------VDGDNEALARLNQlleayrPDVGLVFATGRS----LDSAKELLKEKPLptpDYLITSV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   78 GQYNLYRDQVISEYPLT--------TERIERILAKLQALqieyafvtaeqiavsknTAEVEESLRPIKEDYIVDPnfylD 149
Cdd:pfam05116  68 GTEIYYGPSLVPDQSWQehldyhwdRQAVVEALAKFPGL-----------------TLQPEEEQRPHKVSYFLDP----E 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646  150 HSVIQLlvffpQERTEEVIRSGIledDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAA 229
Cdd:pfam05116 127 AAAAVL-----AELEQLLRKRGL---DVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIG 198
                         250       260       270
                  ....*....|....*....|....*....|...
gi 544687646  230 VGFGVAMGNAEDELkaVADYVTLPIEQDGILVA 262
Cdd:pfam05116 199 GTRGVVVGNAQPEL--LQWYLENARDNPRIYFA 229
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
194-235 3.42e-05

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: 43.31  E-value: 3.42e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 544687646 194 NSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVA 235
Cdd:cd07500  136 QRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
201-251 5.31e-05

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130731 [Multi-domain]  Cd Length: 154  Bit Score: 42.51  E-value: 5.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 544687646  201 EDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVADYVT 251
Cdd:TIGR01670  82 SDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVT 132
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
11-78 4.40e-04

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: 38.92  E-value: 4.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544687646  11 VFFDIDETLyykketriplsISEQVLPRLRAKGIIPAIATGRTYGAFPKAIKPLMNEKGFDLFVTTNG 78
Cdd:cd01427    2 VLFDLDGTL-----------LAVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDG 58
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
8-231 8.01e-04

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: 39.49  E-value: 8.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646    8 IKIVFFDIDETLYyKKETRIPLSISEQVLPRLRAKGIIPAiatgrtygafpkAIKPLMNEKGFDLFVTTnGQYNLYRDQV 87
Cdd:pfam00702   1 IKAVVFDLDGTLT-DGEPVVTEAIAELASEHPLAKAIVAA------------AEDLPIPVEDFTARLLL-GKRDWLEELD 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544687646   88 ISEYPLTTERIERILAKLQalQIEYAFVTAEQIAVSKNTAEVEESLRPIKedyivdpnfyldhsvIQLLVFFPQERteEV 167
Cdd:pfam00702  67 ILRGLVETLEAEGLTVVLV--ELLGVIALADELKLYPGAAEALKALKERG---------------IKVAILTGDNP--EA 127
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544687646  168 IRSGILEDDLKEVRWHKYSVDLLNKNNSKARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVG 231
Cdd:pfam00702 128 AEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
201-251 1.05e-03

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 39.14  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544687646 201 EDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVAMGNAEDELKAVADYVT 251
Cdd:PRK09484 102 SDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVT 152
serB PRK11133
phosphoserine phosphatase; Provisional
196-235 2.97e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 38.39  E-value: 2.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 544687646 196 KARGIEDVLNHFGFGIENAMAFGDGLNDLEMIAAVGFGVA 235
Cdd:PRK11133 249 KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
 
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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