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Conserved domains on  [gi|505740944|ref|WP_015702577|]
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Cof-type HAD-IIB family hydrolase [Pasteurella multocida]

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 ...
 11-265 4.66e-72

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: 219.79  E-value: 4.66e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  11 KIVFFDIDETLLVKDeDYIPATVVPAIRKLKENGIVPAIATGRTLSNFPPKIKglieQTDMNLFVTMNGQYVSYQNEPIR 90
Cdd:cd07517    1 KIVFFDIDGTLLDED-TTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVK----ALGIDSYVSYNGQYVFFEGEVIY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  91 KHPLSKAKIQEFVDFCDQHQIVYAQVSptdtavsaitdqvrdaldplkghyhvdkdyfkhhdvfQILAFYDATQDQFVQD 170
Cdd:cd07517   76 KNPLPQELVERLTEFAKEQGHPVSFYG-------------------------------------QLLLFEDEEEEQKYEE 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 171 SgvLKGLQSVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHV 250
Cdd:cd07517  119 L--RPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYV 196

                        250
                 ....*....|....*
gi 505740944 251 TLPIKEHGIEYFLKQ 265
Cdd:cd07517  197 TKDVDEDGILKALKH 211
 
Name Accession Description Interval E-value
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 11-265 4.66e-72

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: 219.79  E-value: 4.66e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  11 KIVFFDIDETLLVKDeDYIPATVVPAIRKLKENGIVPAIATGRTLSNFPPKIKglieQTDMNLFVTMNGQYVSYQNEPIR 90
Cdd:cd07517    1 KIVFFDIDGTLLDED-TTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVK----ALGIDSYVSYNGQYVFFEGEVIY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  91 KHPLSKAKIQEFVDFCDQHQIVYAQVSptdtavsaitdqvrdaldplkghyhvdkdyfkhhdvfQILAFYDATQDQFVQD 170
Cdd:cd07517   76 KNPLPQELVERLTEFAKEQGHPVSFYG-------------------------------------QLLLFEDEEEEQKYEE 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 171 SgvLKGLQSVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHV 250
Cdd:cd07517  119 L--RPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYV 196

                        250
                 ....*....|....*
gi 505740944 251 TLPIKEHGIEYFLKQ 265
Cdd:cd07517  197 TKDVDEDGILKALKH 211
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 13-263 1.13e-55

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 179.74  E-value: 1.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   13 VFFDIDETLLVKDEDYIPATVVpAIRKLKENGIVPAIATGRTLSNFPPKIKGLIEQTdmnLFVTMNGQYVSYQN-EPIRK 91
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKE-AIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD---PVICYNGALIYDENgKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   92 HPLSKAKIQEFVDFCDQHQIVYAQVSpTDTAVSAITDQVRDALDPLKGHYH-----VDKDYFKHHDVFQILAFYDATQ-D 165
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYT-DDGVYILNDNELEKILKELNYTKSfvpeiDDFELLEDEDINKILILLDEEDlD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  166 QFVQD--SGVLKGLQSVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQL 243
Cdd:pfam08282 156 ELEKElkELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235

                         250       260
                  ....*....|....*....|
gi 505740944  244 KTVADHVTLPIKEHGIEYFL 263
Cdd:pfam08282 236 KAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 10-265 1.31e-52

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: 169.55  E-value: 1.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  10 IKIVFFDIDETLLvKDEDYIPATVVPAIRKLKENGIVPAIATGRTLSNfppkIKGLIEQTDMNL-FVTMNGQYVSY-QNE 87
Cdd:COG0561    2 IKLIALDLDGTLL-NDDGEISPRTKEALRRLREKGIKVVIATGRPLRS----ALPLLEELGLDDpLITSNGALIYDpDGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  88 PIRKHPLSKAKIQEFVDFCDQHQIVYAQVsptdtavsaitdqvrdaldplkghyhvdkdyfkhhdvfqilafydatqdqf 167
Cdd:COG0561   77 VLYERPLDPEDVREILELLREHGLHLQVV--------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 168 vqdsgvlkglqsVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVA 247
Cdd:COG0561  106 ------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAA 173

                        250
                 ....*....|....*...
gi 505740944 248 DHVTLPIKEHGIEYFLKQ 265
Cdd:COG0561  174 DYVTGSNDEDGVAEALEK 191
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 12-263 1.21e-47

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: 158.97  E-value: 1.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   12 IVFFDIDETLLVKDeDYIPATVVPAIRKLKENGIVPAIATGRTlsnfPPKIKGLIEQTDMNL-FVTMNGQYVSYQN-EPI 89
Cdd:TIGR00099   1 LIFIDLDGTLLNDD-HTISPSTKEALAKLREKGIKVVLATGRP----YKEVKNILKELGLDTpFITANGAAVIDDQgEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   90 RKHPLSKAKIQEFVDFCDQHQIVYAQVSPTDTAVSAITDQVRDALDPLKGHYH---VDKDYFKHHDVFQILAFYDATQDQ 166
Cdd:TIGR00099  76 YKKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKlevVDIQYLPDDILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  167 FVQDSGVLKGLQS----VRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQ 242
Cdd:TIGR00099 156 LLIEALNKLELEEnvsvVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 505740944  243 LKTVADHVTLPIKEHGIEYFL 263
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 11-265 7.48e-19

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 83.53  E-value: 7.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  11 KIVFFDIDETLLVKDEDYIPATVVpAIRKLKENGIVPAIATGRTLSNFPPKIKGLIEQTDMnlfVTMNGQYV-SYQNEP- 88
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLE-ALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPA---ICCNGTYLyDYQAKKv 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  89 IRKHPLSKAKIQEFVDFCDQHQI----------VYAQVSPTDTAVSAITDQVRDALDPLkgHYHVDKDYFKHHDVFQILA 158
Cdd:PRK10530  80 LEADPLPVQQALQVIEMLDEHQIhglmyvddamLYEHPTGHVIRTLNWAQTLPPEQRPT--FTQVDSLAQAARQVNAIWK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 159 FYDATQD-----QFVQDSGVLKGLQ-SVRWHKySVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGV 232
Cdd:PRK10530 158 FALTHEDlpqlqHFAKHVEHELGLEcEWSWHD-QVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGL 236

                        250       260       270
                 ....*....|....*....|....*....|...
gi 505740944 233 GVAMGNAHHQLKTVADHVTLPIKEHGIEYFLKQ 265
Cdd:PRK10530 237 GVAMGNADDAVKARADLVIGDNTTPSIAEFIYS 269
 
Name Accession Description Interval E-value
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 11-265 4.66e-72

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: 219.79  E-value: 4.66e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  11 KIVFFDIDETLLVKDeDYIPATVVPAIRKLKENGIVPAIATGRTLSNFPPKIKglieQTDMNLFVTMNGQYVSYQNEPIR 90
Cdd:cd07517    1 KIVFFDIDGTLLDED-TTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVK----ALGIDSYVSYNGQYVFFEGEVIY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  91 KHPLSKAKIQEFVDFCDQHQIVYAQVSptdtavsaitdqvrdaldplkghyhvdkdyfkhhdvfQILAFYDATQDQFVQD 170
Cdd:cd07517   76 KNPLPQELVERLTEFAKEQGHPVSFYG-------------------------------------QLLLFEDEEEEQKYEE 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 171 SgvLKGLQSVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHV 250
Cdd:cd07517  119 L--RPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYV 196

                        250
                 ....*....|....*
gi 505740944 251 TLPIKEHGIEYFLKQ 265
Cdd:cd07517  197 TKDVDEDGILKALKH 211
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 13-263 1.13e-55

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 179.74  E-value: 1.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   13 VFFDIDETLLVKDEDYIPATVVpAIRKLKENGIVPAIATGRTLSNFPPKIKGLIEQTdmnLFVTMNGQYVSYQN-EPIRK 91
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKE-AIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD---PVICYNGALIYDENgKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   92 HPLSKAKIQEFVDFCDQHQIVYAQVSpTDTAVSAITDQVRDALDPLKGHYH-----VDKDYFKHHDVFQILAFYDATQ-D 165
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYT-DDGVYILNDNELEKILKELNYTKSfvpeiDDFELLEDEDINKILILLDEEDlD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  166 QFVQD--SGVLKGLQSVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQL 243
Cdd:pfam08282 156 ELEKElkELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235

                         250       260
                  ....*....|....*....|
gi 505740944  244 KTVADHVTLPIKEHGIEYFL 263
Cdd:pfam08282 236 KAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 10-265 1.31e-52

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: 169.55  E-value: 1.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  10 IKIVFFDIDETLLvKDEDYIPATVVPAIRKLKENGIVPAIATGRTLSNfppkIKGLIEQTDMNL-FVTMNGQYVSY-QNE 87
Cdd:COG0561    2 IKLIALDLDGTLL-NDDGEISPRTKEALRRLREKGIKVVIATGRPLRS----ALPLLEELGLDDpLITSNGALIYDpDGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  88 PIRKHPLSKAKIQEFVDFCDQHQIVYAQVsptdtavsaitdqvrdaldplkghyhvdkdyfkhhdvfqilafydatqdqf 167
Cdd:COG0561   77 VLYERPLDPEDVREILELLREHGLHLQVV--------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 168 vqdsgvlkglqsVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVA 247
Cdd:COG0561  106 ------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAA 173

                        250
                 ....*....|....*...
gi 505740944 248 DHVTLPIKEHGIEYFLKQ 265
Cdd:COG0561  174 DYVTGSNDEDGVAEALEK 191
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 12-263 1.21e-47

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: 158.97  E-value: 1.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   12 IVFFDIDETLLVKDeDYIPATVVPAIRKLKENGIVPAIATGRTlsnfPPKIKGLIEQTDMNL-FVTMNGQYVSYQN-EPI 89
Cdd:TIGR00099   1 LIFIDLDGTLLNDD-HTISPSTKEALAKLREKGIKVVLATGRP----YKEVKNILKELGLDTpFITANGAAVIDDQgEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   90 RKHPLSKAKIQEFVDFCDQHQIVYAQVSPTDTAVSAITDQVRDALDPLKGHYH---VDKDYFKHHDVFQILAFYDATQDQ 166
Cdd:TIGR00099  76 YKKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKlevVDIQYLPDDILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  167 FVQDSGVLKGLQS----VRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQ 242
Cdd:TIGR00099 156 LLIEALNKLELEEnvsvVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 505740944  243 LKTVADHVTLPIKEHGIEYFL 263
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 12-265 2.15e-38

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: 135.03  E-value: 2.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  12 IVFFDIDETLLvKDEDYIPATVVPAIRKLKENGIVPAIATGRTLSNfppkIKGLIEQTDMNLF-VTMNGQYV-SYQNEPI 89
Cdd:cd07516    1 LIALDLDGTLL-NSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRG----AQPYLEELGLDSPlITFNGALVyDPTGKEI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  90 RKHPLSKAKIQEFVDFCDQHQIVYAQVSPTDTAVSAITDQvRDALDPLKGHYHVDKDYFKHHDVFQILAFYDAtqdqfvq 169
Cdd:cd07516   76 LERLISKEDVKELEEFLRKLGIGINIYTNDDWADTIYEEN-EDDEIIKPAEILDDLLLPPDEDITKILFVGED------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 170 DSGVLKGLQSVRWHKYSVDLF----------DEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNA 239
Cdd:cd07516  148 EELDELIAKLPEEFFDDLSVVrsapfyleimPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                        250       260
                 ....*....|....*....|....*.
gi 505740944 240 HHQLKTVADHVTLPIKEHGIEYFLKQ 265
Cdd:cd07516  228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 11-264 2.45e-21

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: 88.41  E-value: 2.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  11 KIVFFDIDETLLVKDEDYIPATVVPAIRKLKENGIVPAIATGR----TLSNFPPKIKGLIeqtdmnlFVTMNGQYVSYqn 86
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRqyyqLISFFPEIKDEMS-------FVAENGAVVYF-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  87 epirkhplskaKIQEFVDfcdqhqivyaqvsptDTAVSAITDQVRDALDPlkghyhvdkdyfKHHDVfqilafydatqdq 166
Cdd:cd07518   72 -----------KFTLNVP---------------DEAAPDIIDELNQKFGG------------ILRAV------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 167 fvqDSGvlkglqsvrwhKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTV 246
Cdd:cd07518  101 ---TSG-----------FGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAA 166

                        250
                 ....*....|....*...
gi 505740944 247 ADHVTLPIKEHGIEYFLK 264
Cdd:cd07518  167 AKYVAPSNNENGVLQVIE 184
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 11-265 7.48e-19

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 83.53  E-value: 7.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  11 KIVFFDIDETLLVKDEDYIPATVVpAIRKLKENGIVPAIATGRTLSNFPPKIKGLIEQTDMnlfVTMNGQYV-SYQNEP- 88
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLE-ALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPA---ICCNGTYLyDYQAKKv 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  89 IRKHPLSKAKIQEFVDFCDQHQI----------VYAQVSPTDTAVSAITDQVRDALDPLkgHYHVDKDYFKHHDVFQILA 158
Cdd:PRK10530  80 LEADPLPVQQALQVIEMLDEHQIhglmyvddamLYEHPTGHVIRTLNWAQTLPPEQRPT--FTQVDSLAQAARQVNAIWK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 159 FYDATQD-----QFVQDSGVLKGLQ-SVRWHKySVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGV 232
Cdd:PRK10530 158 FALTHEDlpqlqHFAKHVEHELGLEcEWSWHD-QVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGL 236

                        250       260       270
                 ....*....|....*....|....*....|...
gi 505740944 233 GVAMGNAHHQLKTVADHVTLPIKEHGIEYFLKQ 265
Cdd:PRK10530 237 GVAMGNADDAVKARADLVIGDNTTPSIAEFIYS 269
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 12-236 2.33e-17

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: 78.19  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   12 IVFFDIDETLLVKDEDYIPATVVPAIRKLKENGIVPAIATGRTLSnfppKIKGLIEQTDMNLFV-TMNGQYVSYQNEPIR 90
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEALERLREAGVKVVIVTGRSLA----EIKELLKQLNLPLPLiAENGALIFYPGEILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   91 KHPLSKAKIQEfvdfcdqhqivyaqvsptdtavSAITDQVRDALDPLKGHYHVDKDYFKHHDVfqILAFYDATQDQFVQD 170
Cdd:TIGR01484  77 IEPSDVFEEIL----------------------GIKFEEIGAELKSLSEHYVGTFIEDKAIAV--AIHYVGAELGQELDS 132

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505740944  171 S---------GVLKGLQSVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAM 236
Cdd:TIGR01484 133 KmrerlekigRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 185-261 1.29e-16

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 77.43  E-value: 1.29e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505740944 185 YSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHVTLPIKEHGIEY 261
Cdd:PRK10513 186 YFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAF 262
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 10-263 2.97e-15

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 72.70  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  10 IKIVFFDIDETLLVKDEDyIPATVVPAIRKLKENGIVPAIATGRTLSnFPPKIKGLIEQTDMnlFVTMNGQYVSYQNepi 89
Cdd:PRK01158   3 IKAIAIDIDGTITDKDRR-LSLKAVEAIRKAEKLGIPVILATGNVLC-FARAAAKLIGTSGP--VIAENGGVISVGF--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  90 rkhplskakiqefvdfcDQHQIVYAQVSPTDTAVSAITDQVRDALDPLKghyHVDKDYFKHHDVF----------QILAF 159
Cdd:PRK01158  76 -----------------DGKRIFLGDIEECEKAYSELKKRFPEASTSLT---KLDPDYRKTEVALrrtvpveevrELLEE 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 160 YDAtqDQFVQDSGvlkglqsvrwhkYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNA 239
Cdd:PRK01158 136 LGL--DLEIVDSG------------FAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANA 201

                        250       260       270
                 ....*....|....*....|....*....|
gi 505740944 240 HHQLKTVADHVTLpiKEHG------IEYFL 263
Cdd:PRK01158 202 DEELKEAADYVTE--KSYGegvaeaIEHLL 229
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 16-260 3.57e-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: 72.50  E-value: 3.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   16 DIDETLlVKDEDYIPATVVPAIRKLKENGIVPAIATGRTlSNFPPKIKGLIEQTDmnLFVTMNGQYVSYQnepirkhpls 95
Cdd:TIGR01482   4 DIDGTL-TDPNRAINESALEAIRKAESKGIPVVLVTGNS-VQFARALAKLIGTPD--PVIAENGGEISYN---------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   96 KAKIQEFVDFCDQHQIVYAQVSPTDtAVSAITDQVRDALDPLKGHYHVDKDYFKhhDVFQILafydaTQDQFVQDSGvlk 175
Cdd:TIGR01482  70 EGLDDIFLAYLEEEWFLDIVIAKTF-PFSRLKVQYPRRASLVKMRYGIDVDTVR--EIIKEL-----GLNLVAVDSG--- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  176 glqsvrwhkYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHVTLPIK 255
Cdd:TIGR01482 139 ---------FDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADYVTESPY 209


                  ....*
gi 505740944  256 EHGIE 260
Cdd:TIGR01482 210 GEGGA 214
PRK15126 PRK15126
HMP-PP phosphatase;
15-257 4.01e-14

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 70.49  E-value: 4.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  15 FDIDETLLVKDEDYIPATVVpAIRKLKENGIVPAIATGRTLSnfppKIKGLIEQTDMNLF-VTMNGQYV-SYQNEPIRKH 92
Cdd:PRK15126   7 FDMDGTLLMPDHHLGEKTLS-TLARLRERDITLTFATGRHVL----EMQHILGALSLDAYlITGNGTRVhSLEGELLHRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  93 PLSkAKIQEFVdfcdQHQivyaqvsPTDTAVSA--------ITDQVRDALdpLKGHyHVDKDYFKHHDVFQILAfYDATQ 164
Cdd:PRK15126  82 DLP-ADVAELV----LHQ-------QWDTRASMhvfnddgwFTGKEIPAL--LQAH-VYSGFRYQLIDLKRLPA-HGVTK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 165 DQFVQDSGVLKGLQsVRWHKYSVDLFDEKIS-------------KATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAG 231
Cdd:PRK15126 146 ICFCGDHDDLTRLQ-IQLNEALGERAHLCFSatdclevlpvgcnKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVG 224

                        250       260
                 ....*....|....*....|....*.
gi 505740944 232 VGVAMGNAHHQLKTVADHvtLPIKEH 257
Cdd:PRK15126 225 RGFIMGNAMPQLRAELPH--LPVIGH 248
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 194-251 3.45e-13

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: 64.92  E-value: 3.45e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 505740944 194 ISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHVT 251
Cdd:cd07514   66 VDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVT 123
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 10-251 9.92e-12

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: 62.84  E-value: 9.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   10 IKIVFFDIDETLLVKDEdYIPATVVPAIRKLKENGIVPAIATGRTlSNFPPKIKGLIEQTDMnlFVTMNGQYVSYQNEPI 89
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNR-MISERAIEAIRKAEKKGIPVSLVTGNT-VPFARALAVLIGTSGP--VVAENGGVIFYNKEDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944   90 RkhpLSKAKIQEFVDfcdqhqivyaqvsptdtavsaitdqvrdalDPLKGHYHVDK---DYFKHHDVFQILAFYDATQDQ 166
Cdd:TIGR01487  77 F---LANMEEEWFLD------------------------------EEKKKRFPRDRlsnEYPRASLVIMREGKDVDEVRE 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  167 FVQDSGVlkglqSVRWHKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTV 246
Cdd:TIGR01487 124 IIKERGL-----NLVASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEI 198


                  ....*
gi 505740944  247 ADHVT 251
Cdd:TIGR01487 199 ADYVT 203
PLN02887 PLN02887
hydrolase family protein
 195-259 6.01e-10

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 59.12  E-value: 6.01e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505740944 195 SKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHVTLPIKEHGI 259
Cdd:PLN02887 507 SKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGV 571
PRK10976 PRK10976
putative hydrolase; Provisional
 194-244 2.16e-09

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 56.60  E-value: 2.16e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505740944 194 ISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLK 244
Cdd:PRK10976 189 VSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNAHQRLK 239
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 196-254 1.95e-06

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: 47.52  E-value: 1.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944 196 KATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMgNAHHQLKTVAD-HVTLPI 254
Cdd:COG0560  156 KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAADrERGWPV 214
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 205-235 6.00e-06

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: 45.62  E-value: 6.00e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 505740944 205 QHFGFAMENVMAFGDGLNDIEMLSTAGVGVA 235
Cdd:cd07500  147 ARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 183-261 6.58e-06

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: 46.19  E-value: 6.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505740944 183 HKYSVDLFDEKISKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHVTLPIKEHGIEY 261
Cdd:cd02605  157 LAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKGPYA 235
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 195-250 3.72e-05

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: 43.88  E-value: 3.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 505740944  195 SKATGIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMgNAHHQLKTVADHV 250
Cdd:TIGR00338 152 YKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKADIC 206
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
212-269 6.74e-04

Soluble P-type ATPase [General function prediction only];


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 39.37  E-value: 6.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740944 212 ENVMAFGDGLNDIEMLSTAGVGVA-MGN--AHHQLKTVADHVTLPIkEHGIEYFLKQAKLI 269
Cdd:COG4087   92 ETTVAIGNGRNDVLMLKEAALGIAvIGPegASVKALLAADIVVKSI-LDALDLLLNPKRLI 151
serB PRK11133
phosphoserine phosphatase; Provisional
 205-235 8.63e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 39.93  E-value: 8.63e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 505740944 205 QHFGFAMENVMAFGDGLNDIEMLSTAGVGVA 235
Cdd:PRK11133 258 QEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 13-54 1.10e-03

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: 37.76  E-value: 1.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 505740944  13 VFFDIDETLLVKDedyipatvvpAIRKLKENGIVPAIATGRT 54
Cdd:cd01427    2 VLFDLDGTLLAVE----------LLKRLRAAGIKLAIVTNRS 33
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 203-231 1.49e-03

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: 38.72  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|....*....
gi 505740944  203 AIQHFGFAMENVMAFGDGLNDIEMLSTAG 231
Cdd:pfam00702 163 ALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 213-241 2.01e-03

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 38.77  E-value: 2.01e-03
                         10        20
                 ....*....|....*....|....*....
gi 505740944 213 NVMAFGDGLNDIEMLSTAGVGVAMGNAHH 241
Cdd:PRK00192 209 ETIALGDSPNDLPMLEAADIAVVVPGPDG 237
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 11-106 2.87e-03

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 38.39  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  11 KIVFFDIDETlLVKDEDYIPATVVPAIRKLKENGIVPAIATGrtlSNFpPKIKGLIEQTDMNLF---VTMNGQYVSYQNE 87
Cdd:PTZ00174   6 TILLFDVDGT-LTKPRNPITQEMKDTLAKLKSKGFKIGVVGG---SDY-PKIKEQLGEDVLEDFdyvFSENGLVAYKDGE 80

                         90       100
                 ....*....|....*....|...
gi 505740944  88 PIRKHPLSKA----KIQEFVDFC 106
Cdd:PTZ00174  81 LFHSQSILKFlgeeKLKKFINFC 103
copA PRK10671
copper-exporting P-type ATPase CopA;
199-252 3.37e-03

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 38.57  E-value: 3.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505740944 199 GIACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNA-------------HHQLKTVADHVTL 252
Cdd:PRK10671 700 GKAEAIKRLQSQGRQVAMVGDGINDAPALAQADVGIAMGGGsdvaietaaitlmRHSLMGVADALAI 766
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 205-251 3.53e-03

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: 37.12  E-value: 3.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 505740944 205 QHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADHVT 251
Cdd:cd01630   86 EKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT 132
AKR_AKR3B1-3 cd19118
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ...
 36-118 3.70e-03

AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.


Pssm-ID: 381344 [Multi-domain]  Cd Length: 283  Bit Score: 38.16  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  36 AIRKLKENGIVPAIAtgrtLSNFPPK-IKGLIEQTdmnlfvtmngQYVSYQNEpIRKHPLSKAkiQEFVDFCDQHQIVYA 114
Cdd:cd19118  144 AMVELKKTGKVKSIG----VSNFSIDhLQAIIEET----------GVVPAVNQ-IEAHPLLLQ--DELVDYCKSKNIHIT 206


                 ....
gi 505740944 115 QVSP 118
Cdd:cd19118  207 AYSP 210
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 192-269 3.94e-03

ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.


Pssm-ID: 273656 [Multi-domain]  Cd Length: 545  Bit Score: 38.45  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740944  192 EKISKATGI-----------ACAIQHFGFAMENVMAFGDGLNDIEMLSTAGVGVAMGNAhHQLKTVADHVTLPIKEHGIE 260
Cdd:TIGR01494 418 KAIAKELGIdvfarvkpeekAAIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMGSG-DVAKAAADIVLLDDDLSTIV 496


                  ....*....
gi 505740944  261 YFLKQAKLI 269
Cdd:TIGR01494 497 EAVKEGRKT 505
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 214-249 5.59e-03

Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 37.50  E-value: 5.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 505740944 214 VMAFGDGLNDIEMLSTAGVGVAMGNAHHQLKTVADH 249
Cdd:COG3769  210 TIALGDSPNDIPMLEAADIAVVIRSPHGAPPELEDK 245
 
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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