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Conserved domains on  [gi|822956185|gb|KLG80588|]
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hypothetical protein WR12_00305 [Escherichia coli]

Protein Classification

HAD family hydrolase( domain architecture ID 11576336)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like cd07520
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 5-240 2.99e-67

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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: 319822  Cd Length: 144  Bit Score: 204.99  E-value: 2.99e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185   5 VVLSDLDDTLFQTRRKMVDELALEPfrtGAVDRTLNPRSFMTEEQSMLVDWLLEQAELIPVTARGTEEISRVRIPFHSWA 84
Cdd:cd07520    1 LVFVDLDDTLFQTARKLPGHGRLAP---ATVDKRGNALSYMTPAQTAFVDWLLAGAVLIPVTARSVEAMSRVTLPFRSWA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  85 ITTHGAVILTPEGKPDEEwkahmlgqlapyqekltsmqrlitemmdakginawarlnfeygetavymvmkhrdstrldel 164
Cdd:cd07520   78 ICSHGGVILTPDGEPDPE-------------------------------------------------------------- 95

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822956185 165 naiadeietvfptegfyihrnsnnvaWLPTPVEKGLAVSWLLEKLRaERGVFPVIGLGDSLSDHRFMKLCSWFGIP 240
Cdd:cd07520   96 --------------------------WLPRPVGKAQAVRWLLERHL-FPGARPTLGFGDSLSDLGFMRLCDWAGTP 144
PLN02205 super family cl31841
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
 65-252 4.77e-04

alpha,alpha-trehalose-phosphate synthase [UDP-forming]


The actual alignment was detected with superfamily member PLN02205:

Pssm-ID: 177855 [Multi-domain]  Cd Length: 854  Bit Score: 41.16  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  65 VTARGTEEISRVRIPFHSWAITTHGAVILTPEGkpDEEWKAHMLGQLAPYQEKLTSMQRLITEMMDAKGInawarlnfEY 144
Cdd:PLN02205 639 VSARSRKTLADWFSPCEKLGIAAEHGYFLRLKR--DVEWETCVPVADCSWKQIAEPVMQLYTETTDGSTI--------ED 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185 145 GETAVYMVMKHRD----STRLDELnaiADEIETVFPTEGFYIHRNSNNVAWLPTPVEKGLAVSWLLEKLRaERGVFP--V 218
Cdd:PLN02205 709 KETALVWCYEDADpdfgSCQAKEL---LDHLESVLANEPVTVKSGQNIVEVKPQGVSKGLVAKRLLSIMQ-ERGMLPdfV 784

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 822956185 219 IGLGDSLSDH-RFMKLCSWFG----IPRQSQFADAISQR 252
Cdd:PLN02205 785 LCIGDDRSDEdMFEVITSSMAgpsiAPRAEVFACTVGQK 823
 
Name Accession Description Interval E-value
HAD_like cd07520
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 5-240 2.99e-67

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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: 319822  Cd Length: 144  Bit Score: 204.99  E-value: 2.99e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185   5 VVLSDLDDTLFQTRRKMVDELALEPfrtGAVDRTLNPRSFMTEEQSMLVDWLLEQAELIPVTARGTEEISRVRIPFHSWA 84
Cdd:cd07520    1 LVFVDLDDTLFQTARKLPGHGRLAP---ATVDKRGNALSYMTPAQTAFVDWLLAGAVLIPVTARSVEAMSRVTLPFRSWA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  85 ITTHGAVILTPEGKPDEEwkahmlgqlapyqekltsmqrlitemmdakginawarlnfeygetavymvmkhrdstrldel 164
Cdd:cd07520   78 ICSHGGVILTPDGEPDPE-------------------------------------------------------------- 95

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822956185 165 naiadeietvfptegfyihrnsnnvaWLPTPVEKGLAVSWLLEKLRaERGVFPVIGLGDSLSDHRFMKLCSWFGIP 240
Cdd:cd07520   96 --------------------------WLPRPVGKAQAVRWLLERHL-FPGARPTLGFGDSLSDLGFMRLCDWAGTP 144
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 35-228 6.58e-06

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 45.83  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185   35 VDRTLNPRSFMteEQSMLVDWLLEQAE-----LIPVTARGTEEISRVR--IPFHSWAITTHGAVILTPEGKPDEEWKAHM 107
Cdd:TIGR01484   6 LDGTLLDPNAH--ELSPETIEALERLReagvkVVIVTGRSLAEIKELLkqLNLPLPLIAENGALIFYPGEILYIEPSDVF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  108 LGQLAPYQEKLTSMQRLITEMMDAKGINAWA-RLNFEYGETAVYMVMKHRDSTRLDELNAIADEIETVFPTEGFyihrns 186
Cdd:TIGR01484  84 EEILGIKFEEIGAELKSLSEHYVGTFIEDKAiAVAIHYVGAELGQELDSKMRERLEKIGRNDLELEAIYSGKTD------ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 822956185  187 nnVAWLPTPVEKGLAVSWLLEKLRAERGVfpVIGLGDSLSDH 228
Cdd:TIGR01484 158 --LEVLPAGVNKGSALQALLQELNGKKDE--ILAFGDSGNDE 195
PLN02205 PLN02205
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
 65-252 4.77e-04

alpha,alpha-trehalose-phosphate synthase [UDP-forming]


Pssm-ID: 177855 [Multi-domain]  Cd Length: 854  Bit Score: 41.16  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  65 VTARGTEEISRVRIPFHSWAITTHGAVILTPEGkpDEEWKAHMLGQLAPYQEKLTSMQRLITEMMDAKGInawarlnfEY 144
Cdd:PLN02205 639 VSARSRKTLADWFSPCEKLGIAAEHGYFLRLKR--DVEWETCVPVADCSWKQIAEPVMQLYTETTDGSTI--------ED 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185 145 GETAVYMVMKHRD----STRLDELnaiADEIETVFPTEGFYIHRNSNNVAWLPTPVEKGLAVSWLLEKLRaERGVFP--V 218
Cdd:PLN02205 709 KETALVWCYEDADpdfgSCQAKEL---LDHLESVLANEPVTVKSGQNIVEVKPQGVSKGLVAKRLLSIMQ-ERGMLPdfV 784

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 822956185 219 IGLGDSLSDH-RFMKLCSWFG----IPRQSQFADAISQR 252
Cdd:PLN02205 785 LCIGDDRSDEdMFEVITSSMAgpsiAPRAEVFACTVGQK 823
 
Name Accession Description Interval E-value
HAD_like cd07520
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 5-240 2.99e-67

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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: 319822  Cd Length: 144  Bit Score: 204.99  E-value: 2.99e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185   5 VVLSDLDDTLFQTRRKMVDELALEPfrtGAVDRTLNPRSFMTEEQSMLVDWLLEQAELIPVTARGTEEISRVRIPFHSWA 84
Cdd:cd07520    1 LVFVDLDDTLFQTARKLPGHGRLAP---ATVDKRGNALSYMTPAQTAFVDWLLAGAVLIPVTARSVEAMSRVTLPFRSWA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  85 ITTHGAVILTPEGKPDEEwkahmlgqlapyqekltsmqrlitemmdakginawarlnfeygetavymvmkhrdstrldel 164
Cdd:cd07520   78 ICSHGGVILTPDGEPDPE-------------------------------------------------------------- 95

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822956185 165 naiadeietvfptegfyihrnsnnvaWLPTPVEKGLAVSWLLEKLRaERGVFPVIGLGDSLSDHRFMKLCSWFGIP 240
Cdd:cd07520   96 --------------------------WLPRPVGKAQAVRWLLERHL-FPGARPTLGFGDSLSDLGFMRLCDWAGTP 144
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 35-228 6.58e-06

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 45.83  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185   35 VDRTLNPRSFMteEQSMLVDWLLEQAE-----LIPVTARGTEEISRVR--IPFHSWAITTHGAVILTPEGKPDEEWKAHM 107
Cdd:TIGR01484   6 LDGTLLDPNAH--ELSPETIEALERLReagvkVVIVTGRSLAEIKELLkqLNLPLPLIAENGALIFYPGEILYIEPSDVF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  108 LGQLAPYQEKLTSMQRLITEMMDAKGINAWA-RLNFEYGETAVYMVMKHRDSTRLDELNAIADEIETVFPTEGFyihrns 186
Cdd:TIGR01484  84 EEILGIKFEEIGAELKSLSEHYVGTFIEDKAiAVAIHYVGAELGQELDSKMRERLEKIGRNDLELEAIYSGKTD------ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 822956185  187 nnVAWLPTPVEKGLAVSWLLEKLRAERGVfpVIGLGDSLSDH 228
Cdd:TIGR01484 158 --LEVLPAGVNKGSALQALLQELNGKKDE--ILAFGDSGNDE 195
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 5-227 2.31e-04

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. 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: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 41.58  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185   5 VVLSDLDDTLfqtrrkmvdelalepfrtgavdrtLNPRSFMTEEQSMLVDWLLE-QAELIPVTARGTEEISRVR--IPFH 81
Cdd:cd07507    1 VIFTDLDGTL------------------------LDHHTYSFDPARPALERLKErGIPVVPCTSKTRAEVEYLRkeLGIE 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  82 SWAITTHGAVILTPEGKPDEEWKAHMLGQL------APYqEKLTSMQRLITEM----------MDAKGINAWARLNF--- 142
Cdd:cd07507   57 DPFIVENGGAIFIPRGYFKFPGRCKSEGGYevielgKPY-REIRAALEKIREEtgfkitgfgdLTEEEIAELTGLPRera 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185 143 ------EYGETAVYMVMKHRDSTRLDELNAIADEIetvfpTEG--FY-IHRNSNNvawlptpveKGLAVSWLLEKLRAER 213
Cdd:cd07507  136 alakerEYSETIILRSDEEEDEKVLEALEERGLKI-----TKGgrFYhVLGAGAD---------KGKAVAILAALYRQLY 201

                        250
                 ....*....|....
gi 822956185 214 GVFPVIGLGDSLSD 227
Cdd:cd07507  202 EAIVTVGLGDSPND 215
PLN02205 PLN02205
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
 65-252 4.77e-04

alpha,alpha-trehalose-phosphate synthase [UDP-forming]


Pssm-ID: 177855 [Multi-domain]  Cd Length: 854  Bit Score: 41.16  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185  65 VTARGTEEISRVRIPFHSWAITTHGAVILTPEGkpDEEWKAHMLGQLAPYQEKLTSMQRLITEMMDAKGInawarlnfEY 144
Cdd:PLN02205 639 VSARSRKTLADWFSPCEKLGIAAEHGYFLRLKR--DVEWETCVPVADCSWKQIAEPVMQLYTETTDGSTI--------ED 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822956185 145 GETAVYMVMKHRD----STRLDELnaiADEIETVFPTEGFYIHRNSNNVAWLPTPVEKGLAVSWLLEKLRaERGVFP--V 218
Cdd:PLN02205 709 KETALVWCYEDADpdfgSCQAKEL---LDHLESVLANEPVTVKSGQNIVEVKPQGVSKGLVAKRLLSIMQ-ERGMLPdfV 784

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 822956185 219 IGLGDSLSDH-RFMKLCSWFG----IPRQSQFADAISQR 252
Cdd:PLN02205 785 LCIGDDRSDEdMFEVITSSMAgpsiAPRAEVFACTVGQK 823
 
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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