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Conserved domains on  [gi|1037265919|gb|ANL06009|]
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HAD superfamily hydrolase protein (plasmid) [Rhizobium esperanzae]

Protein Classification

HAD family hydrolase( domain architecture ID 11426169)

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 16-225 5.98e-11

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


:

Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 60.15  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  16 VRYLFTDIDDTL-TTEGKLLPSTYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPV-AAVIGESGAYaVMRRNGEVVFE 93
Cdd:COG0561     2 IKLIALDLDGTLlNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLdDPLITSNGAL-IYDPDGEVLYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  94 YwengalqgerqrqhlgaieklisekggtfKIAHDQVFRLADVAIDIQGHntrdvedLASDIRAMGGTVAISSIHINTWI 173
Cdd:COG0561    81 R-----------------------------PLDPEDVREILELLREHGLH-------LQVVVRSGPGFLEILPKGVSKGS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1037265919 174 GVydkRAMSERLltgmfEVDPAElpsvTAFVGDSRNDAPMFGFIRNSFGVGN 225
Cdd:COG0561   125 AL---KKLAERL-----GIPPEE----VIAFGDSGNDLEMLEAAGLGVAMGN 164
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 16-225 5.98e-11

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 60.15  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  16 VRYLFTDIDDTL-TTEGKLLPSTYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPV-AAVIGESGAYaVMRRNGEVVFE 93
Cdd:COG0561     2 IKLIALDLDGTLlNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLdDPLITSNGAL-IYDPDGEVLYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  94 YwengalqgerqrqhlgaieklisekggtfKIAHDQVFRLADVAIDIQGHntrdvedLASDIRAMGGTVAISSIHINTWI 173
Cdd:COG0561    81 R-----------------------------PLDPEDVREILELLREHGLH-------LQVVVRSGPGFLEILPKGVSKGS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1037265919 174 GVydkRAMSERLltgmfEVDPAElpsvTAFVGDSRNDAPMFGFIRNSFGVGN 225
Cdd:COG0561   125 AL---KKLAERL-----GIPPEE----VIAFGDSGNDLEMLEAAGLGVAMGN 164
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 18-223 3.05e-10

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: 58.16  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  18 YLFTDIDDTLTT--EGKLLPSTYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPVAAVIGESGAYAvMRRNGEVVFEYW 95
Cdd:TIGR01484   1 LLFFDLDGTLLDpnAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGAL-IFYPGEILYIEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  96 ENGAL-QGERQRQHLGAIEKLISEKG-GTF----KIAHDQVFRLADVAIDIQGHNTRDVEDLASDIRAMggTVAISSIHI 169
Cdd:TIGR01484  80 SDVFEeILGIKFEEIGAELKSLSEHYvGTFiedkAIAVAIHYVGAELGQELDSKMRERLEKIGRNDLEL--EAIYSGKTD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037265919 170 NTWI--GVyDKRAMSERLLtgmfEVDPAELPSvTAFVGDSRNDAPMFGFIRNSFGV 223
Cdd:TIGR01484 158 LEVLpaGV-NKGSALQALL----QELNGKKDE-ILAFGDSGNDEEMFEVAGLAVAV 207
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 22-225 8.95e-07

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 48.43  E-value: 8.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  22 DIDDTLTTEGKLLP-STYEALWELSRAGIAVVPVTGGSAgwceHIVRAwpVAAVIGESGAyaVMRRNGEVVFEywengal 100
Cdd:PRK01158    9 DIDGTITDKDRRLSlKAVEAIRKAEKLGIPVILATGNVL----CFARA--AAKLIGTSGP--VIAENGGVISV------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919 101 QGERQRQHLGAIEK------LISEKGGTFKIAH---DQVFRLADVAIdiqgHNTRDVEDLASDIRAMGGTVAIS----SI 167
Cdd:PRK01158   74 GFDGKRIFLGDIEEcekaysELKKRFPEASTSLtklDPDYRKTEVAL----RRTVPVEEVRELLEELGLDLEIVdsgfAI 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037265919 168 HI-NTWIgvyDKrAMSERLLTGMFEVDPAELpsvtAFVGDSRNDAPMFGFIRNSFGVGN 225
Cdd:PRK01158  150 HIkSPGV---NK-GTGLKKLAELMGIDPEEV----AAIGDSENDLEMFEVAGFGVAVAN 200
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 19-93 3.94e-06

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 46.45  E-value: 3.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037265919  19 LFTDIDDTLTTEGKLLP-STYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPVAAVIGESGAYAVMRrnGEVVFE 93
Cdd:cd07517     3 VFFDIDGTLLDEDTTIPeSTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSYVSYNGQYVFFE--GEVIYK 76
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 19-93 1.96e-03

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 38.76  E-value: 1.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037265919  19 LFTDIDDTLTTEGK-LLPSTYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPV-AAVIGESGAYAVMrRNGEVVFE 93
Cdd:pfam08282   1 IASDLDGTLLNSDKkISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLdDPVICYNGALIYD-ENGKILYS 76
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 16-225 5.98e-11

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 60.15  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  16 VRYLFTDIDDTL-TTEGKLLPSTYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPV-AAVIGESGAYaVMRRNGEVVFE 93
Cdd:COG0561     2 IKLIALDLDGTLlNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLdDPLITSNGAL-IYDPDGEVLYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  94 YwengalqgerqrqhlgaieklisekggtfKIAHDQVFRLADVAIDIQGHntrdvedLASDIRAMGGTVAISSIHINTWI 173
Cdd:COG0561    81 R-----------------------------PLDPEDVREILELLREHGLH-------LQVVVRSGPGFLEILPKGVSKGS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1037265919 174 GVydkRAMSERLltgmfEVDPAElpsvTAFVGDSRNDAPMFGFIRNSFGVGN 225
Cdd:COG0561   125 AL---KKLAERL-----GIPPEE----VIAFGDSGNDLEMLEAAGLGVAMGN 164
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 18-223 3.05e-10

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: 58.16  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  18 YLFTDIDDTLTT--EGKLLPSTYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPVAAVIGESGAYAvMRRNGEVVFEYW 95
Cdd:TIGR01484   1 LLFFDLDGTLLDpnAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGAL-IFYPGEILYIEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  96 ENGAL-QGERQRQHLGAIEKLISEKG-GTF----KIAHDQVFRLADVAIDIQGHNTRDVEDLASDIRAMggTVAISSIHI 169
Cdd:TIGR01484  80 SDVFEeILGIKFEEIGAELKSLSEHYvGTFiedkAIAVAIHYVGAELGQELDSKMRERLEKIGRNDLEL--EAIYSGKTD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037265919 170 NTWI--GVyDKRAMSERLLtgmfEVDPAELPSvTAFVGDSRNDAPMFGFIRNSFGV 223
Cdd:TIGR01484 158 LEVLpaGV-NKGSALQALL----QELNGKKDE-ILAFGDSGNDEEMFEVAGLAVAV 207
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 22-225 8.95e-07

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 48.43  E-value: 8.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  22 DIDDTLTTEGKLLP-STYEALWELSRAGIAVVPVTGGSAgwceHIVRAwpVAAVIGESGAyaVMRRNGEVVFEywengal 100
Cdd:PRK01158    9 DIDGTITDKDRRLSlKAVEAIRKAEKLGIPVILATGNVL----CFARA--AAKLIGTSGP--VIAENGGVISV------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919 101 QGERQRQHLGAIEK------LISEKGGTFKIAH---DQVFRLADVAIdiqgHNTRDVEDLASDIRAMGGTVAIS----SI 167
Cdd:PRK01158   74 GFDGKRIFLGDIEEcekaysELKKRFPEASTSLtklDPDYRKTEVAL----RRTVPVEEVRELLEELGLDLEIVdsgfAI 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037265919 168 HI-NTWIgvyDKrAMSERLLTGMFEVDPAELpsvtAFVGDSRNDAPMFGFIRNSFGVGN 225
Cdd:PRK01158  150 HIkSPGV---NK-GTGLKKLAELMGIDPEEV----AAIGDSENDLEMFEVAGFGVAVAN 200
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 22-252 3.73e-06

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


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 46.66  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919  22 DIDDTLTTEGKLL-PSTYEALWELSRAGIAVVPVTGGSAgwceHIVRAwpVAAVIGESGAyaVMRRNGEVVFEYWENGAL 100
Cdd:TIGR01487   7 DIDGTLTDPNRMIsERAIEAIRKAEKKGIPVSLVTGNTV----PFARA--LAVLIGTSGP--VVAENGGVIFYNKEDIFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037265919 101 QGERQRQHLGAIEKLISEKGGTfkiahDQVFRLADVAIDIQGhntRDVEDLASDIRAMGGTVAIS--SIHI-NTWIgvyD 177
Cdd:TIGR01487  79 ANMEEEWFLDEEKKKRFPRDRL-----SNEYPRASLVIMREG---KDVDEVREIIKERGLNLVASgfAIHImKKGV---D 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037265919 178 KRAMSERL--LTGmfeVDPAELpsvtAFVGDSRNDAPMFGFIRNSFGVGNILPVlpyLQHVPRWISSQPAGLGFADI 252
Cdd:TIGR01487 148 KGVGVEKLkeLLG---IKPEEV----AAIGDSENDIDLFRVVGFKVAVANADDQ---LKEIADYVTSNPYGEGVVEV 214
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 19-93 3.94e-06

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 46.45  E-value: 3.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037265919  19 LFTDIDDTLTTEGKLLP-STYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPVAAVIGESGAYAVMRrnGEVVFE 93
Cdd:cd07517     3 VFFDIDGTLLDEDTTIPeSTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSYVSYNGQYVFFE--GEVIYK 76
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 19-93 1.96e-03

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 38.76  E-value: 1.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037265919  19 LFTDIDDTLTTEGK-LLPSTYEALWELSRAGIAVVPVTGGSAGWCEHIVRAWPV-AAVIGESGAYAVMrRNGEVVFE 93
Cdd:pfam08282   1 IASDLDGTLLNSDKkISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLdDPVICYNGALIYD-ENGKILYS 76
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 18-56 7.07e-03

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 36.86  E-value: 7.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1037265919  18 YLFTDIDDTLTTEGKLL-PSTYEALWELSRAGIAVVPVTG 56
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTIsPSTKEALAKLREKGIKVVLATG 40
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 19-56 9.84e-03

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 36.42  E-value: 9.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1037265919  19 LFTDIDDTLTT-EGKLLPSTYEALWELSRAGIAVVPVTG 56
Cdd:cd07516     2 IALDLDGTLLNsDKEISPRTKEAIKKAKEKGIKVVIATG 40
 
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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