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Conserved domains on  [gi|1722177270|ref|WP_146491622|]
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MULTISPECIES: HAD-IA family hydrolase [Vibrio]

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 ...
 5-188 1.46e-58

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 PRK10563:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 221  Bit Score: 184.90  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   5 QTKCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLYRTELEAL 84
Cdd:PRK10563    3 QIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVARL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  85 FQRHLKPMDGAIELIEFLKrqdIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFDANSWKPEPDLIMYTAMNMGFLP 164
Cdd:PRK10563   83 FDSELEPIAGANALLESIT---VPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNV 159

                         170       180
                  ....*....|....*....|....
gi 1722177270 165 NECIYVDDTLKGIEAGVRAGIQSF 188
Cdd:PRK10563  160 ENCILVDDSSAGAQSGIAAGMEVF 183
 
Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 5-188 1.46e-58

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 184.90  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   5 QTKCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLYRTELEAL 84
Cdd:PRK10563    3 QIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVARL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  85 FQRHLKPMDGAIELIEFLKrqdIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFDANSWKPEPDLIMYTAMNMGFLP 164
Cdd:PRK10563   83 FDSELEPIAGANALLESIT---VPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNV 159

                         170       180
                  ....*....|....*....|....
gi 1722177270 165 NECIYVDDTLKGIEAGVRAGIQSF 188
Cdd:PRK10563  160 ENCILVDDSSAGAQSGIAAGMEVF 183
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 7-192 1.91e-50

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 161.33  E-value: 1.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGFGAklnvidcyahfqggkladilmdtqerlglsisidtleplyrtELEALFQ 86
Cdd:cd07526     1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGA------------------------------------------RVLAAFE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 RHLKPMDGAIELIEFLkrqDIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFDANSWKPEPDLIMYTAMNMGFLPNE 166
Cdd:cd07526    39 AELQPIPGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPER 115

                         170       180
                  ....*....|....*....|....*.
gi 1722177270 167 CIYVDDTLKGIEAGVRAGIQSFRLRP 192
Cdd:cd07526   116 CLVIEDSPTGVRAALAAGMTVFGFTG 141
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-219 4.67e-49

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 159.99  E-value: 4.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNViDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLYRTELEALFQ 86
Cdd:COG0637     3 KAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTE-EEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 R-HLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSWKPEPDLIMYTAMNMGFLPN 165
Cdd:COG0637    82 EeGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDV-IVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1722177270 166 ECIYVDDTLKGIEAGVRAGIQSFrlrpsideAVVDPEAGSTELAVQDIY--SLEEI 219
Cdd:COG0637   161 ECVVFEDSPAGIRAAKAAGMRVV--------GVPDGGTAEEELAGADLVvdDLAEL 208
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 8-187 1.73e-25

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 98.26  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   8 CVIFDCDGTLIDSEKL-CCQALVNVFSGFGAKLnVIDCYAHFQggkladiLMDTQERLglsISIDTLEPLYRTELEALFQ 86
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAiAKLINREELGLVPDEL-GVSAVGRLE-------LALRRFKA---QYGRTISPEDAQLLYKQLF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 RH-------LKPMDGAIELIEFLKRQDIEFCIASNAPKSRvESSLAMTGMLDDFKGKVFSaFDANSWKPEPDLIMYTAMN 159
Cdd:TIGR01509  70 YEqieeeakLKPLPGVRALLEALRARGKKLALLTNSPRAH-KLVLALLGLRDLFDVVIDS-SDVGLGKPDPDIYLQALKA 147

                         170       180
                  ....*....|....*....|....*...
gi 1722177270 160 MGFLPNECIYVDDTLKGIEAGVRAGIQS 187
Cdd:TIGR01509 148 LGLEPSECVFVDDSPAGIEAAKAAGMHT 175
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
9-187 2.71e-25

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 97.66  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLYRTELealFQRH 88
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEEL---HDKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  89 LKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKgKVFSAFDANSWKPEPDLIMYTAMNMGFLPNECI 168
Cdd:pfam13419  78 VKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFD-VIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                         170
                  ....*....|....*....
gi 1722177270 169 YVDDTLKGIEAGVRAGIQS 187
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKV 175
 
Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 5-188 1.46e-58

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 184.90  E-value: 1.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   5 QTKCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLYRTELEAL 84
Cdd:PRK10563    3 QIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVARL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  85 FQRHLKPMDGAIELIEFLKrqdIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFDANSWKPEPDLIMYTAMNMGFLP 164
Cdd:PRK10563   83 FDSELEPIAGANALLESIT---VPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNV 159

                         170       180
                  ....*....|....*....|....
gi 1722177270 165 NECIYVDDTLKGIEAGVRAGIQSF 188
Cdd:PRK10563  160 ENCILVDDSSAGAQSGIAAGMEVF 183
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 7-192 1.91e-50

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 161.33  E-value: 1.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGFGAklnvidcyahfqggkladilmdtqerlglsisidtleplyrtELEALFQ 86
Cdd:cd07526     1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGA------------------------------------------RVLAAFE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 RHLKPMDGAIELIEFLkrqDIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFDANSWKPEPDLIMYTAMNMGFLPNE 166
Cdd:cd07526    39 AELQPIPGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPER 115

                         170       180
                  ....*....|....*....|....*.
gi 1722177270 167 CIYVDDTLKGIEAGVRAGIQSFRLRP 192
Cdd:cd07526   116 CLVIEDSPTGVRAALAAGMTVFGFTG 141
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-219 4.67e-49

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 159.99  E-value: 4.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNViDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLYRTELEALFQ 86
Cdd:COG0637     3 KAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTE-EEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 R-HLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSWKPEPDLIMYTAMNMGFLPN 165
Cdd:COG0637    82 EeGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDV-IVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1722177270 166 ECIYVDDTLKGIEAGVRAGIQSFrlrpsideAVVDPEAGSTELAVQDIY--SLEEI 219
Cdd:COG0637   161 ECVVFEDSPAGIRAAKAAGMRVV--------GVPDGGTAEEELAGADLVvdDLAEL 208
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-187 7.32e-31

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 113.49  E-value: 7.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKLADILMDTqerLGLSIS--IDTLEPLYRTELEAL 84
Cdd:COG0546     2 KLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRL---LGEDPDeeLEELLARFRELYEEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  85 FQRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSWKPEPDLIMYTAMNMGFLP 164
Cdd:COG0546    79 LLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDA-IVGGDDVPPAKPKPEPLLEALERLGLDP 157

                         170       180
                  ....*....|....*....|...
gi 1722177270 165 NECIYVDDTLKGIEAGVRAGIQS 187
Cdd:COG0546   158 EEVLMVGDSPHDIEAARAAGVPF 180
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 8-187 1.73e-25

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 98.26  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   8 CVIFDCDGTLIDSEKL-CCQALVNVFSGFGAKLnVIDCYAHFQggkladiLMDTQERLglsISIDTLEPLYRTELEALFQ 86
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAiAKLINREELGLVPDEL-GVSAVGRLE-------LALRRFKA---QYGRTISPEDAQLLYKQLF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 RH-------LKPMDGAIELIEFLKRQDIEFCIASNAPKSRvESSLAMTGMLDDFKGKVFSaFDANSWKPEPDLIMYTAMN 159
Cdd:TIGR01509  70 YEqieeeakLKPLPGVRALLEALRARGKKLALLTNSPRAH-KLVLALLGLRDLFDVVIDS-SDVGLGKPDPDIYLQALKA 147

                         170       180
                  ....*....|....*....|....*...
gi 1722177270 160 MGFLPNECIYVDDTLKGIEAGVRAGIQS 187
Cdd:TIGR01509 148 LGLEPSECVFVDDSPAGIEAAKAAGMHT 175
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
9-187 2.71e-25

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 97.66  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLYRTELealFQRH 88
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEEL---HDKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  89 LKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKgKVFSAFDANSWKPEPDLIMYTAMNMGFLPNECI 168
Cdd:pfam13419  78 VKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFD-VIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                         170
                  ....*....|....*....
gi 1722177270 169 YVDDTLKGIEAGVRAGIQS 187
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKV 175
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-219 1.89e-24

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 96.64  E-value: 1.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGK-------------LADILMDTQERLGLSISIDTL 73
Cdd:COG1011     2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEyalwrryergeitFAELLRRLLEELGLDLAEELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  74 EplyrtELEALFQRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSWKPEPDLI 153
Cdd:COG1011    82 E-----AFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDA-VVSSEEVGVRKPDPEIF 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722177270 154 MYTAMNMGFLPNECIYVDDTLKG-IEAGVRAGIQSFRLRPSIDEAVVDPEAgstELAVQDIYSLEEI 219
Cdd:COG1011   156 ELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRP---DYVISDLAELLEL 219
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-184 2.99e-21

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: 87.64  E-value: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGF-----------GAKLNVIDCYAHFQGGKLADIL-MDTQERLGLSISIDTLE 74
Cdd:pfam00702   2 KAVVFDLDGTLTDGEPVVTEAIAELASEHplakaivaaaeDLPIPVEDFTARLLLGKRDWLEeLDILRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  75 PLYRTELEALF-QRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFDANSwKPEPDLI 153
Cdd:pfam00702  82 VVLVELLGVIAlADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVG-KPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1722177270 154 MYTAMNMGFLPNECIYVDDTLKGIEAGVRAG 184
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 9-185 6.69e-21

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 85.36  E-value: 6.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLccqalvnvfsgfgaklnvidcyaHFQggklADILMDtqerlglsisidtlepLYRTELEALFQRH 88
Cdd:cd07505     2 VIFDMDGVLIDTEPL-----------------------HRQ----AWQLLE----------------RKNALLLELIASE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  89 L-KPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFDANSWKPEPDLIMYTAMNMGFLPNEC 167
Cdd:cd07505    39 GlKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                         170
                  ....*....|....*...
gi 1722177270 168 IYVDDTLKGIEAGVRAGI 185
Cdd:cd07505   119 LVFEDSLAGIEAAKAAGM 136
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 9-185 1.17e-17

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 77.30  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEklccqalvnvfsgfgaklnvidcYAHFQggkladilmdtqerlglsISIDTLEPLYRTELEALF--Q 86
Cdd:cd16423     2 VIFDFDGVIVDTE-----------------------PLWYE------------------AWQELLNERRNELIKRQFseK 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 RHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKgKVFSAFDANSWKPEPDLIMYTAMNMGFLPNE 166
Cdd:cd16423    41 TDLPPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFE-VIVTGDDVEKSKPDPDLYLEAAERLGVNPEE 119

                         170
                  ....*....|....*....
gi 1722177270 167 CIYVDDTLKGIEAGVRAGI 185
Cdd:cd16423   120 CVVIEDSRNGVLAAKAAGM 138
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 9-219 1.08e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 78.74  E-value: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270    9 VIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDcYAHFQGGKLADILMDTQERLGLSiSIDTLEPLYRTeLEALFQRH 88
Cdd:PLN02919    78 VLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVED-FVPFMGTGEANFLGGVASVKGVK-GFDPDAAKKRF-FEIYLEKY 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   89 LKP-----MDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGM-LDDFKGKVfSAFDANSWKPEPDLIMYTAMNMGF 162
Cdd:PLN02919   155 AKPnsgigFPGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLpLSMFDAIV-SADAFENLKPAPDIFLAAAKILGV 233

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1722177270  163 LPNECIYVDDTLKGIEAGVRAGIQSFRLRPSIDEAVVDpEAGSTeLAVQDI--YSLEEI 219
Cdd:PLN02919   234 PTSECVVIEDALAGVQAARAAGMRCIAVTTTLSEEILK-DAGPS-LIRKDIgnISLSDI 290
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 9-187 7.83e-16

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 73.47  E-value: 7.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLCCQALVNVFSGFGakLNVI---DCYAHFQGGkladiLMDTQERLgLSISIDTLEPLYRTELEALF 85
Cdd:cd02616     4 ILFDLDGTLIDTNELIIKSFNHTLKEYG--LEGYtreEVLPFIGPP-----LRETFEKI-DPDKLEDMVEEFRKYYREHN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  86 QRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGmLDDFKGKVFSAFDANSWKPEPDLIMYTAMNMGFLPN 165
Cdd:cd02616    76 DDLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLG-LDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPE 154

                         170       180
                  ....*....|....*....|..
gi 1722177270 166 ECIYVDDTLKGIEAGVRAGIQS 187
Cdd:cd02616   155 EALMVGDSPHDILAGKNAGVKT 176
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-188 3.94e-15

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 70.83  E-value: 3.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNvIDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLyrTELEALFQ 86
Cdd:TIGR02009   2 KAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFD-KQYNESLKGLSREDILRAILKLRGDGLSLEEIHQL--AERKNELY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 RHL------KPMDGAIELIEFLKRQDIEFCIAS---NAPksRVessLAMTGMLDDFKGKVfSAFDANSWKPEPDLIMYTA 157
Cdd:TIGR02009  79 RELlrltgvAVLPGIRNLLKRLKAKGIAVGLGSsskNAP--RI---LAKLGLRDYFDAIV-DASEVKNGKPHPETFLLAA 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1722177270 158 MNMGFLPNECIYVDDTLKGIEAGVRAGIQSF 188
Cdd:TIGR02009 153 ELLGVPPNECIVFEDALAGVQAARAAGMFAV 183
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 9-186 3.37e-14

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 68.53  E-value: 3.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLCCQALVNVFSGFGaKLNVIDCYAHFQG---GKLADILMDTqerLGLSISIDTLEPLYRTELEALF 85
Cdd:cd07529     4 CIFDMDGLLLDTERIYTETTQEILARYG-KTYTWDVKAKMMGrpaSEAARIIVDE---LKLPMSLEEEFDEQQEALAELF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  86 QRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFD---ANSWKPEPDlIMYTAMNMgF 162
Cdd:cd07529    80 MGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDpevKGRGKPAPD-IFLVAAKR-F 157

                         170       180
                  ....*....|....*....|....*....
gi 1722177270 163 -----LPNECIYVDDTLKGIEAGVRAGIQ 186
Cdd:cd07529   158 neppkDPSKCLVFEDSPNGVKAAKAAGMQ 186
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 9-185 1.40e-13

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 67.02  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLCCQALVNVFSGFgAKLNV---IDCYAHFQ---GGKlaDILMDTQERLG--LSISIDTLEPL---- 76
Cdd:cd07528     2 LIFDVDGTLAETEELHRRAFNNAFFAE-RGLDWywdRELYGELLrvgGGK--ERIAAYFEKVGwpESAPKDLKELIadlh 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  77 -----YRTELEALFQRHLKPmdGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTgmLDDFKGKVFSAF----DANSWK 147
Cdd:cd07528    79 kakteRYAELIAAGLLPLRP--GVARLIDEAKAAGVRLAIATTTSPANVDALLSAL--LGPERRAIFDAIaagdDVAEKK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1722177270 148 PEPDLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGI 185
Cdd:cd07528   155 PDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGL 192
PLN02940 PLN02940
riboflavin kinase
 8-194 9.59e-13

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 66.78  E-value: 9.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   8 CVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDcyAHFQGGKL-----ADILMDtqerLGLSISIDTleplYRTELE 82
Cdd:PLN02940   13 HVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGRE--AQKIVGKTpleaaATVVED----YGLPCSTDE----FNSEIT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  83 ALFQR---HLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAFDANSWKPEPDLIMYTAMN 159
Cdd:PLN02940   83 PLLSEqwcNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKR 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1722177270 160 MGFLPNECIYVDDTLKGIEAGVRAGIQSFRLrPSI 194
Cdd:PLN02940  163 LNVEPSNCLVIEDSLPGVMAGKAAGMEVIAV-PSI 196
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 74-179 1.24e-11

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 62.74  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  74 EPLYRTELEALFQrhLKPmdGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMlDDFKGKVFSAFDANSWKPEPDLI 153
Cdd:PLN03243   97 EDLYEYMQGGLYR--LRP--GSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGM-EGFFSVVLAAEDVYRGKPDPEMF 171

                          90       100
                  ....*....|....*....|....*.
gi 1722177270 154 MYTAMNMGFLPNECIYVDDTLKGIEA 179
Cdd:PLN03243  172 MYAAERLGFIPERCIVFGNSNSSVEA 197
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 9-184 2.38e-11

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 60.10  E-value: 2.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAhfQGGKLADILMDtqerlglSISIDTLEPLYRTELEALFQRH 88
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALK--QAGGLAEEEWY-------RIATSALEELQGRFWSEYDAEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  89 LKpMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFkgKVFSAFDANSWKPEPDLIMYTAMNMGfLPNECI 168
Cdd:TIGR01549  73 AY-IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYF--ELILVSDEPGSKPEPEIFLAALESLG-VPPEVL 148

                         170
                  ....*....|....*.
gi 1722177270 169 YVDDTLKGIEAGVRAG 184
Cdd:TIGR01549 149 HVGDNLNDIEGARNAG 164
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-188 2.31e-09

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 55.59  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   1 MRLEQTKCVIFDCDGTLIDSEK---LCCQAlvnVFSGFGAKLNVIDCYAHFQGGKlADILMdtqERlGLSISIDTLEPLY 77
Cdd:PRK13222    1 MKFMDIRAVAFDLDGTLVDSAPdlaAAVNA---ALAALGLPPAGEERVRTWVGNG-ADVLV---ER-ALTWAGREPDEEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  78 RTELEALFQRHL--------KPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFkGKVFSAFDANSWKPE 149
Cdd:PRK13222   73 LEKLRELFDRHYaenvaggsRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYF-SVVIGGDSLPNKKPD 151

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1722177270 150 PDLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGIQSF 188
Cdd:PRK13222  152 PAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSV 190
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 9-213 2.45e-09

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 54.99  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLccqalvnvfsgfgaklnvidcyaHFQG-GKLADILMDTQERLGLsisidtleplYRTELEALFQR 87
Cdd:cd02598     2 VIFDLDGVITDTAEY-----------------------HYRAwKKLADKEELAARKNRI----------YVELIEELTPV 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  88 HLKPmdGAIELIEFLKRQDIEFCIAS---NAPKSrvessLAMTGMLDDFKGKVFSAFDANSwKPEPDLIMYTAMNMGFLP 164
Cdd:cd02598    49 DVLP--GIASLLVDLKAKGIKIALASaskNAPKI-----LEKLGLAEYFDAIVDGAVLAKG-KPDPDIFLAAAEGLGLNP 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1722177270 165 NECIYVDDTLKGIEAGVRAGIQSF---RLRPSIDEAVVDPEAgSTELAVQDI 213
Cdd:cd02598   121 KDCIGVEDAQAGIRAIKAAGFLVVgvgREEDLLGADIVVPDT-TADLTIEEL 171
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 92-190 3.65e-09

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: 52.78  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  92 MDG---AIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFkGKVFSAFDANSWKPEPDLIMYTAMNMGFLPNECI 168
Cdd:cd01427     6 LDGtllAVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLF-DGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVL 84

                          90       100
                  ....*....|....*....|..
gi 1722177270 169 YVDDTLKGIEAGVRAGIQSFRL 190
Cdd:cd01427    85 FVGDSENDIEAARAAGGRTVAV 106
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 9-221 4.80e-09

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 54.66  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSeklccQALVNVFSGFGAKLNVIDCYAHFQ---GGKLAD---ILMDTQERLGLSISIDTLEPL-YRTEL 81
Cdd:cd07527     2 LLFDMDGTLVDS-----TPAVERAWHKWAKEHGVDPEEVLKvshGRRAIDvirKLAPDDADIELVLALETEEPEsYPEGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  82 EAlfqrhlkpMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMlddFKGKVF-SAFDANSWKPEPDLIMYTAMNM 160
Cdd:cd07527    77 IA--------IPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGL---PHPEVLvTADDVKNGKPDPEPYLLGAKLL 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722177270 161 GFLPNECIYVDDTLKGIEAGVRAGIQSFRLRPSIDEAVVDPeagstELAVQDIYSLEEISV 221
Cdd:cd07527   146 GLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEA-----AGADLVVEDLSDISV 201
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 6-195 7.48e-09

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 53.89  E-value: 7.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   6 TKCVIFDCDGTLI--DSEKLCCQALVNVFSGFGAKLNVIDCYAHFQ---GGKLADILMDTQ--ERLGLSISIDTLEplyr 78
Cdd:cd02603     1 IRAVLFDFGGVLIdpDPAAAVARFEALTGEPSEFVLDTEGLAGAFLeleRGRITEEEFWEElrEELGRPLSAELFE---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  79 teleALFQRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMT-GMLDDFKGKVFSaFDANSWKPEPDliMYTA 157
Cdd:cd02603    77 ----ELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLpRRGDLFDGVVES-CRLGVRKPDPE--IYQL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1722177270 158 M--NMGFLPNECIYVDDTLKGIEAGVRAGIQSFRLRPSID 195
Cdd:cd02603   150 AleRLGVKPEEVLFIDDREENVEAARALGIHAILVTDAED 189
PRK10826 PRK10826
hexitol phosphatase HxpB;
5-218 1.37e-08

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 53.41  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   5 QTKCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDcyahfqggkladilmDTQERLGLsiSIDTLEPL-YR----- 78
Cdd:PRK10826    6 QILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRRE---------------ELPDTLGL--RIDQVVDLwYArqpwn 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  79 ------------TELEALFQRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSW 146
Cdd:PRK10826   69 gpsrqevvqriiARVISLIEETRPLLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDA-LASAEKLPYS 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722177270 147 KPEPDLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGIQSFrlrpsideAVVDPE-AGSTELAVQDI--YSLEE 218
Cdd:PRK10826  148 KPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSI--------VVPAPEqQNDPRWALADVklESLTE 214
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 9-188 1.49e-08

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 53.17  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLCCQALVNVFSGFGakLNVIDcyahfqggkladiLMDTQERLGLS--ISIDTLEPLYRTELEALFQ 86
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLG--LPVPS-------------AAEVRSIIGLSldEAIARLLPMATPALVAVAE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  87 RHLK-------------PM-DGAIELIEFLKRQDIEFCIASNapKSR--VESSLAMTGMLDDFKgkVFSAFDANSWKPEP 150
Cdd:cd07533    67 RYKEafdilrllpehaePLfPGVREALDALAAQGVLLAVATG--KSRrgLDRVLEQHGLGGYFD--ATRTADDTPSKPHP 142

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1722177270 151 DLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGIQSF 188
Cdd:cd07533   143 EMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAHAV 180
PRK11587 PRK11587
putative phosphatase; Provisional
 5-221 5.10e-08

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 51.92  E-value: 5.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   5 QTKCVIFDCDGTLIDS----EKLCC----------QALVNVFSGFGAklnvIDCYAHFQGGKLADILMDTqerlglsisI 70
Cdd:PRK11587    2 RCKGFLFDLDGTLVDSlpavERAWSnwadrhgiapDEVLNFIHGKQA----ITSLRHFMAGASEAEIQAE---------F 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  71 DTLEPLYRTELEALfqrhlKPMDGAIELIEFLKRQDIEFCIASNA--PksrVESSLAMTGMLDdfKGKVF-SAFDANSWK 147
Cdd:PRK11587   69 TRLEQIEATDTEGI-----TALPGAIALLNHLNKLGIPWAIVTSGsvP---VASARHKAAGLP--APEVFvTAERVKRGK 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722177270 148 PEPDLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGIQSFrlrpsideaVVDPEAGSTELAVQD--IYSLEEISV 221
Cdd:PRK11587  139 PEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVI---------AVNAPADTPRLDEVDlvLHSLEQLTV 205
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 10-185 6.80e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 52.02  E-value: 6.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  10 IFDCDGTLIDSEK-LCCQALVNVFSGFGAKLNV--IDCYAHFQ---GGK----------------LADILMDTQERLGLs 67
Cdd:PLN02779   44 LFDCDGVLVETERdGHRVAFNDAFKEFGLRPVEwdVELYDELLnigGGKermtwyfnengwptstIEKAPKDEEERKEL- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  68 isIDTLEpLYRTEL--EALFQRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKG-KVFSAFDAN 144
Cdd:PLN02779  123 --VDSLH-DRKTELfkELIESGALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVNTLLGPERAQGlDVFAGDDVP 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1722177270 145 SWKPEPDLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGI 185
Cdd:PLN02779  200 KKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGM 240
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 7-184 7.41e-08

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 51.53  E-value: 7.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLC-CQALVNVFSGFGAKLNV--------IDCYAHFQG-GKLADILMDTQERLGLSISIDTLEPL 76
Cdd:cd02586     2 EAVIFDWAGTTVDYGSFApVNAFVEAFAQRGVQITLeearkpmgLLKIDHIRAlLEMPRVAEAWRAVFGRLPTEADVDAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  77 YRTELEALFQR---HLKPMDGAIELIEFLKRQDIEFCIASNAPK---SRVESSLAMTGMLDDFkgkVFSAFDANSWKPEP 150
Cdd:cd02586    82 YEEFEPILIASlaeYSSPIPGVLEVIAKLRARGIKIGSTTGYTRemmDIVLPEAAAQGYRPDS---LVTPDDVPAGRPYP 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1722177270 151 DLIMYTAMNMGFLP-NECIYVDDTLKGIEAGVRAG 184
Cdd:cd02586   159 WMCYKNAIELGVYDvAAVVKVGDTVPDIKEGLNAG 193
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 7-187 8.61e-08

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 51.18  E-value: 8.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSgfgaklnvidcyaHFQGGKLA--DI-------LMDTQERLGLSiSIDTLEPLY 77
Cdd:PRK13288    4 NTVLFDLDGTLINTNELIISSFLHTLK-------------TYYPNQYKreDVlpfigpsLHDTFSKIDES-KVEEMITTY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  78 RTELEALFQRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGmLDDFKGKVFSAFDANSWKPEPDLIMYTA 157
Cdd:PRK13288   70 REFNHEHHDELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTG-LDEFFDVVITLDDVEHAKPDPEPVLKAL 148

                         170       180       190
                  ....*....|....*....|....*....|
gi 1722177270 158 MNMGFLPNECIYVDDTLKGIEAGVRAGIQS 187
Cdd:PRK13288  149 ELLGAKPEEALMVGDNHHDILAGKNAGTKT 178
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 7-170 9.74e-08

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


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 50.80  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALvNVFSGFGAKLNVI---------------DCYAHFQgGKLADILMDTQERLGLSISID 71
Cdd:TIGR01428   2 KALVFDVYGTLFDVHSVAERAA-ELYGGRGEALSQLwrqkqleyswlrtlmGPYKDFW-DLTREALRYLLGRLGLEDDES 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  72 TLEPLYRtelealFQRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSWKPEPD 151
Cdd:TIGR01428  80 AADRLAE------AYLRLPPHPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDA-VLSADAVRAYKPAPQ 152

                         170
                  ....*....|....*....
gi 1722177270 152 LIMYTAMNMGFLPNECIYV 170
Cdd:TIGR01428 153 VYQLALEALGVPPDEVLFV 171
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 93-191 1.52e-07

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 48.31  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  93 DGAIELIEFLKrQDIEFCIASNAPKSRVESSLAMTGMLDDFKgKVFSAFDANSWKPEPDLIMYTAMNMGFLPNECIYVDD 172
Cdd:cd04305    12 PGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFD-HIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGD 89

                          90       100
                  ....*....|....*....|
gi 1722177270 173 TL-KGIEAGVRAGIQSFRLR 191
Cdd:cd04305    90 SLeSDILGAKNAGIKTVWFN 109
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 2-185 1.54e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 50.61  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   2 RLEQTKCVIFDCDGTLIDSEKLCCQAlvnvfsgFGAKLNVIDcyahFQGGK-------LADILMDTQERLGLSISIDTLE 74
Cdd:PLN02770   18 GLAPLEAVLFDVDGTLCDSDPLHYYA-------FREMLQEIN----FNGGVpiteeffVENIAGKHNEDIALGLFPDDLE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  75 P--LYRTELEALFQR----HLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGKVFSAfDANSWKP 148
Cdd:PLN02770   87 RglKFTDDKEALFRKlaseQLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGS-ECEHAKP 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1722177270 149 EPDLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGI 185
Cdd:PLN02770  166 HPDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGM 202
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 7-184 1.58e-07

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 50.63  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEklCC---QALVNVFSGFGAKLNV-----------IDcyaHFQG-GKLADILMDTQERLGLSISID 71
Cdd:PRK13478    5 QAVIFDWAGTTVDFG--SFaptQAFVEAFAQFGVEITLeeargpmglgkWD---HIRAlLKMPRVAARWQAVFGRLPTEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  72 TLEPLYRTELEALFQ---RHLKPMDGAIELIEFLKRQDIEfcIASNapksrvesslamTG----MLD------------- 131
Cdd:PRK13478   80 DVDALYAAFEPLQIAklaDYATPIPGVLEVIAALRARGIK--IGST------------TGytreMMDvvvplaaaqgyrp 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1722177270 132 DFkgkVFSAFDANSWKPEPDLIMYTAMNMG-FLPNECIYVDDTLKGIEAGVRAG 184
Cdd:PRK13478  146 DH---VVTTDDVPAGRPYPWMALKNAIELGvYDVAACVKVDDTVPGIEEGLNAG 196
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 93-221 1.52e-05

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 45.24  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  93 DGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGmLDDFKGKVFSAFDANSWKPEPDLIMYTAMNMGFLPNECIYVDD 172
Cdd:PLN02575  219 TGSQEFVNVLMNYKIPMALVSTRPRKTLENAIGSIG-IRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGN 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1722177270 173 TLKGIEAGVRAGIQSFRLrpsideAVVDP--EAGSTELAVQdiySLEEISV 221
Cdd:PLN02575  298 SNQTVEAAHDARMKCVAV------ASKHPiyELGAADLVVR---RLDELSI 339
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 7-170 1.76e-05

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


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 44.18  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCcQALVNVFSGFGAKL------NVID---------CYAHFQGgKLADILMDTQERLGLSISID 71
Cdd:cd02588     1 KALVFDVYGTLIDWHSGL-AAAERAFPGRGEELsrlwrqKQLEytwlvtlmgPYVDFDE-LTRDALRATAAELGLELDES 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  72 TLEPLYRtelealFQRHLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSWKPEPD 151
Cdd:cd02588    79 DLDELGD------AYLRLPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDA-VLSAEDVRAYKPAPA 151

                         170
                  ....*....|....*....
gi 1722177270 152 LIMYTAMNMGFLPNECIYV 170
Cdd:cd02588   152 VYELAAERLGVPPDEILHV 170
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 9-191 1.90e-05

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. 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: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 44.15  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSE---KLCCQALVNVFSGFGAKLNVIDCYAhfqgGKLADILMdtqER-LGLSISIDTLEPLYRtELEAL 84
Cdd:cd16417     2 VAFDLDGTLVDSApdlAEAANAMLAALGLPPLPEETVRTWI----GNGADVLV---ERaLTGAREAEPDEELFK-EARAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  85 FQRHL--------KPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGmLDDFKGKVFSAFDANSWKPEPDLIMYT 156
Cdd:cd16417    74 FDRHYaetlsvhsHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALG-ISDYFSLVLGGDSLPEKKPDPAPLLHA 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1722177270 157 AMNMGFLPNECIYVDDTLKGIEAGVRAGIQSFRLR 191
Cdd:cd16417   153 CEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLT 187
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 8-187 2.45e-05

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 43.73  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   8 CVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKLADILMDtqerLGLSISIDTLEPL--YRTELEA-- 83
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRE----LLPFDEEEAQRAVdaYREYYKEkg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  84 LFQrhLKPMDGAIELIEFLKRQDIEFCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSWKPEPDLIMYTAMNMGFL 163
Cdd:cd04302    77 LFE--NEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDG-IAGASLDGSRVHKADVIRYALDTLGIA 153

                         170       180
                  ....*....|....*....|....
gi 1722177270 164 PNECIYVDDTLKGIEAGVRAGIQS 187
Cdd:cd04302   154 PEQAVMIGDRKHDIIGARANGIDS 177
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 10-187 2.65e-05

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 43.52  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  10 IFDCDGTLIDSEKLCCQALVNVFSGFGAKlnvIDCYAHFQGGKLAdilmDTQERLGLSISIDTLEPLYRtELEALFQRHL 89
Cdd:cd07523     3 IWDLDGTLLDSYPAMTKALSETLADFGIP---QDLETVYKIIKES----SVQFAIQYYAEVPDLEEEYK-ELEAEYLAKP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  90 KPMDGAIELIEFLKRQDIEFCIASNAPKSrVESSLAMTGMLDDFKGKVFSAFDANSwKPEPDLIMYTAMNMGFLPNECIY 169
Cdd:cd07523    75 ILFPGAKAVLRWIKEQGGKNFLMTHRDHS-ALTILKKDGIASYFTEIVTSDNGFPR-KPNPEAINYLLNKYQLNPEETVM 152

                         170
                  ....*....|....*...
gi 1722177270 170 VDDTLKGIEAGVRAGIQS 187
Cdd:cd07523   153 IGDRELDIEAGHNAGIST 170
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 7-113 6.39e-05

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: 42.90  E-value: 6.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSE------KLCCQALVNVFSGFGAKlnVIDCYAHFQGGKL--ADILmdtQERLGLsisidtLEPLYR 78
Cdd:COG0560     4 RLAVFDLDGTLIAGEsidelaRFLGRRGLVDRREVLEE--VAAITERAMAGELdfEESL---RFRVAL------LAGLPE 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1722177270  79 TELEALFQR----HLKPMDGAIELIEFLKRQDIEFCIAS 113
Cdd:COG0560    73 EELEELAERlfeeVPRLYPGARELIAEHRAAGHKVAIVS 111
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 7-200 1.17e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 42.16  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   7 KCVIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKlADILMdtQERLGLSI---SIDTLEPLYRTEL-- 81
Cdd:PRK13223   14 RLVMFDLDGTLVDSVPDLAAAVDRMLLELGRPPAGLEAVRHWVGNG-APVLV--RRALAGSIdhdGVDDELAEQALALfm 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  82 EALFQRH----LKPmdGAIELIEFLKRQDIEFCIASNAPKSRVESslamtgMLDDFK-GKVFsafdanSW---------- 146
Cdd:PRK13223   91 EAYADSHeltvVYP--GVRDTLKWLKKQGVEMALITNKPERFVAP------LLDQMKiGRYF------RWiiggdtlpqk 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722177270 147 KPEPDLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGIQSFRL-------RPSIDEA---VVD 200
Cdd:PRK13223  157 KPDPAALLFVMKMAGVPPSQSLFVGDSRSDVLAAKAAGVQCVALsygynhgRPIAEESpalVID 220
HAD pfam12710
haloacid dehalogenase-like hydrolase;
9-117 2.44e-04

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 40.59  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270   9 VIFDCDGTLIDSEKLCCQALVNVFSGFGAKLNVIDCYAHFQGGKLADILMDTQERLGLSISIDTLEPLYRTELEALFQRH 88
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERFVAEV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1722177270  89 LKP--MDGAIELIEFLKRQDIEFCIASNAPK 117
Cdd:pfam12710  81 ALPrlHPGALELLAAHRAAGDRVVVVTGGLR 111
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
10-185 4.81e-04

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 39.67  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  10 IFDCDGTLIDSEKLCCQALVNVFSGFG--------AKLN----------VIDcyaHFQGGKLADILMDTQERLGLSISID 71
Cdd:PRK10725    9 IFDMDGTILDTEPTHRKAWREVLGRYGlqfdeqamVALNgsptwriaqaIIE---LNQADLDPHALAREKTEAVKSMLLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  72 TLEPLYRTEL-EALFQRhlKPMdgaielieflkrqdiefCIASNAPKSRVESSLAMTGMLDDFKGkVFSAFDANSWKPEP 150
Cdd:PRK10725   86 SVEPLPLIEVvKAWHGR--RPM-----------------AVGTGSESAIAEALLAHLGLRRYFDA-VVAADDVQHHKPAP 145

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1722177270 151 DLIMYTAMNMGFLPNECIYVDDTLKGIEAGVRAGI 185
Cdd:PRK10725  146 DTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGM 180
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 92-185 1.95e-03

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. 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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 36.67  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722177270  92 MDGAI---ELIEFLKRQDIEFCIASNAPKSRVEsslamtgMLDD--FKGK---VFSAFDANSWKPEPDLIMYTAMNMGFL 163
Cdd:cd16421     6 LDGTLlilELLKALRQKGIKLAVLSNKPNEAVQ-------VLVEelFPGSfdfVLGEKEGIRRKPDPT*ALECAKVLGVP 78

                          90       100
                  ....*....|....*....|..
gi 1722177270 164 PNECIYVDDTLKGIEAGVRAGI 185
Cdd:cd16421    79 PDEVLYVGDSGVDMQTARNAGM 100
 
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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