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Conserved domains on  [gi|1080238649|gb|OFK33138|]
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hydrolase [Corynebacterium sp. HMSC064E08]

Protein Classification

Cof-type HAD-IIB family hydrolase( domain architecture ID 11576316)

Cof-type haloacid dehalogenase (HAD)-IIB family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction and may function as a phosphatase; 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:  3.1.3.-|3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 18-292 6.18e-55

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 176.24  E-value: 6.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  18 RLVVTDMDGTLLNEDKE-IPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVadagevvsvts 96
Cdd:cd07518     1 KLIATDMDGTFLNDDKTyDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVV----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  97 idhgvvtqlvhairqfndnrvaagrtplsviicgaasayveffpphfnipeevqqlqfneaakyylklqkvddviaaaae 176
Cdd:cd07518       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 177 dgIVKIAAFDPYSVEEESADYLRSQ-SSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELI 255
Cdd:cd07518    70 --YFKFTLNVPDEAAPDIIDELNQKfGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEML 147

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080238649 256 DHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVITTLR 292
Cdd:cd07518   148 KYAGYSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE 184
 
Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 18-292 6.18e-55

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 176.24  E-value: 6.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  18 RLVVTDMDGTLLNEDKE-IPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVadagevvsvts 96
Cdd:cd07518     1 KLIATDMDGTFLNDDKTyDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVV----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  97 idhgvvtqlvhairqfndnrvaagrtplsviicgaasayveffpphfnipeevqqlqfneaakyylklqkvddviaaaae 176
Cdd:cd07518       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 177 dgIVKIAAFDPYSVEEESADYLRSQ-SSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELI 255
Cdd:cd07518    70 --YFKFTLNVPDEAAPDIIDELNQKfGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEML 147

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080238649 256 DHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVITTLR 292
Cdd:cd07518   148 KYAGYSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE 184
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 16-294 2.17e-52

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


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 169.93  E-value: 2.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  16 PYRLVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVAD-AGEVVSV 94
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDpDGEVLYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  95 TSIDHGVVTQLVHAIRQFNdnrvaagrtpLSVIICgaasayveffpphfnipeevqqlqfneaakyylklqkvddviaaa 174
Cdd:COG0561    81 RPLDPEDVREILELLREHG----------LHLQVV--------------------------------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 175 aedgivkiaafdpysveeesadylrsqsshlraVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLEL 254
Cdd:COG0561   106 ---------------------------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEM 152

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1080238649 255 IDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVITTLREL 294
Cdd:COG0561   153 LEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 20-287 1.80e-51

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 169.73  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  20 VVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVADA-GEVVSVTSID 98
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDEnGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  99 HGVVTQLVHAIRQFNdnrvaagrtpLSVIICGAASAYVEffpPHFNIPEEVQQLQFNEAAKYYLKLQKVDDviaaaaEDG 178
Cdd:pfam08282  81 KEAVKEIIEYLKENN----------LEILLYTDDGVYIL---NDNELEKILKELNYTKSFVPEIDDFELLE------DED 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 179 IVKIAAFDPYSVEEESADYLRSQ-SSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDH 257
Cdd:pfam08282 142 INKILILLDEEDLDELEKELKELfGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEA 221

                         250       260       270
                  ....*....|....*....|....*....|
gi 1080238649 258 AGRSFAMSNGHPEIKRRATDIAPSNAEEGV 287
Cdd:pfam08282 222 AGLGVAMGNASPEVKAAADYVTDSNNEDGV 251
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 19-287 3.29e-47

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


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 158.59  E-value: 3.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  19 LVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVAD-AGEVVSVTSI 97
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDdQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  98 DHGVVTQLVHAIRQFNdnrvaagrtpLSVIICGAASAYVEF-FPPHFNIpeevqqlqfnEAAKYYLKLQKVDDViaAAAE 176
Cdd:TIGR00099  81 DLDLVEEILNFLKKHG----------LDVILYGDDSIYASKnDPEYFTI----------FKKFLGEPKLEVVDI--QYLP 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 177 DGIVKIAAFDPysvEEESADYLR------SQSSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLN 250
Cdd:TIGR00099 139 DDILKILLLFL---DPEDLDLLIealnklELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMN 215

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080238649 251 DLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGV 287
Cdd:TIGR00099 216 DIEMLEAAGYGVAMGNADEELKALADYVTDSNNEDGV 252
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 16-287 6.81e-20

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 87.06  E-value: 6.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  16 PYRLVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIP---IIAENGNYV--ADAGE 90
Cdd:PRK10513    2 AIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdyCITNNGALVqkAADGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  91 VVSVTSIDH-------------GVVTQLVHAIRQFNDNRVAAGRTplsviicgAASAYVEFFPPHFNIPEEVQ-QLQFne 156
Cdd:PRK10513   82 TVAQTALSYddylyleklsrevGVHFHALDRNTLYTANRDISYYT--------VHESFLTGIPLVFREVEKMDpNLQF-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 157 aakyyLKLQKVD--DVIAAAaedgIVKIA--AFDPYSVEEESADYLrsqsshlravvsgahwvDLIDANTNKGTALAALQ 232
Cdd:PRK10513  152 -----PKVMMIDepEILDAA----IARIPaeVKERYTVLKSAPYFL-----------------EILDKRVNKGTGVKSLA 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1080238649 233 EALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGV 287
Cdd:PRK10513  206 EHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGV 260
 
Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 18-292 6.18e-55

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 176.24  E-value: 6.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  18 RLVVTDMDGTLLNEDKE-IPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVadagevvsvts 96
Cdd:cd07518     1 KLIATDMDGTFLNDDKTyDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVV----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  97 idhgvvtqlvhairqfndnrvaagrtplsviicgaasayveffpphfnipeevqqlqfneaakyylklqkvddviaaaae 176
Cdd:cd07518       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 177 dgIVKIAAFDPYSVEEESADYLRSQ-SSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELI 255
Cdd:cd07518    70 --YFKFTLNVPDEAAPDIIDELNQKfGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEML 147

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080238649 256 DHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVITTLR 292
Cdd:cd07518   148 KYAGYSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE 184
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 16-294 2.17e-52

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


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 169.93  E-value: 2.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  16 PYRLVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVAD-AGEVVSV 94
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDpDGEVLYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  95 TSIDHGVVTQLVHAIRQFNdnrvaagrtpLSVIICgaasayveffpphfnipeevqqlqfneaakyylklqkvddviaaa 174
Cdd:COG0561    81 RPLDPEDVREILELLREHG----------LHLQVV--------------------------------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 175 aedgivkiaafdpysveeesadylrsqsshlraVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLEL 254
Cdd:COG0561   106 ---------------------------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEM 152

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1080238649 255 IDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVITTLREL 294
Cdd:COG0561   153 LEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 20-287 1.80e-51

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 169.73  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  20 VVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVADA-GEVVSVTSID 98
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDEnGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  99 HGVVTQLVHAIRQFNdnrvaagrtpLSVIICGAASAYVEffpPHFNIPEEVQQLQFNEAAKYYLKLQKVDDviaaaaEDG 178
Cdd:pfam08282  81 KEAVKEIIEYLKENN----------LEILLYTDDGVYIL---NDNELEKILKELNYTKSFVPEIDDFELLE------DED 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 179 IVKIAAFDPYSVEEESADYLRSQ-SSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDH 257
Cdd:pfam08282 142 INKILILLDEEDLDELEKELKELfGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEA 221

                         250       260       270
                  ....*....|....*....|....*....|
gi 1080238649 258 AGRSFAMSNGHPEIKRRATDIAPSNAEEGV 287
Cdd:pfam08282 222 AGLGVAMGNASPEVKAAADYVTDSNNEDGV 251
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 19-287 3.29e-47

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


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 158.59  E-value: 3.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  19 LVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVAD-AGEVVSVTSI 97
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDdQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  98 DHGVVTQLVHAIRQFNdnrvaagrtpLSVIICGAASAYVEF-FPPHFNIpeevqqlqfnEAAKYYLKLQKVDDViaAAAE 176
Cdd:TIGR00099  81 DLDLVEEILNFLKKHG----------LDVILYGDDSIYASKnDPEYFTI----------FKKFLGEPKLEVVDI--QYLP 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 177 DGIVKIAAFDPysvEEESADYLR------SQSSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLN 250
Cdd:TIGR00099 139 DDILKILLLFL---DPEDLDLLIealnklELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMN 215

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080238649 251 DLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGV 287
Cdd:TIGR00099 216 DIEMLEAAGYGVAMGNADEELKALADYVTDSNNEDGV 252
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 19-287 5.76e-35

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: 126.94  E-value: 5.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  19 LVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVADA-GEVVsvtsI 97
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPtGKEI----L 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  98 DHGVVTQLVHAIRQFNDNRVAAGRtpLSVIICGAASAYVEFfpphfnipEEVQQLQFNEAAKYYLKLQKVDdviaaaaed 177
Cdd:cd07516    77 ERLISKEDVKELEEFLRKLGIGIN--IYTNDDWADTIYEEN--------EDDEIIKPAEILDDLLLPPDED--------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 178 gIVKIAAFD-PYSVEEESADYLRSQSSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELID 256
Cdd:cd07516   138 -ITKILFVGeDEELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLE 216

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1080238649 257 HAGRSFAMSNGHPEIKRRATDIAPSNAEEGV 287
Cdd:cd07516   217 YAGLGVAMGNAIDEVKEAADYVTLTNNEDGV 247
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 18-294 1.34e-31

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: 116.94  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  18 RLVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPiAHRIPIIAENGNYVADAGEVVSVTSI 97
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKA-LGIDSYVSYNGQYVFFEGEVIYKNPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  98 DHGVVTQLVHairqfndnrvaagrtplsviicgaasayveffpphfnipeevqqlqfneaakyYLKLQKVDDVIAAAAEd 177
Cdd:cd07517    80 PQELVERLTE-----------------------------------------------------FAKEQGHPVSFYGQLL- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 178 givkiaafdPYSVEEESADYLRSQSsHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDH 257
Cdd:cd07517   106 ---------LFEDEEEEQKYEELRP-ELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEA 175

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080238649 258 AGRSFAMSNGHPEIKRRATDIAPSNAEEGVITTLREL 294
Cdd:cd07517   176 VGIGIAMGNAHEELKEIADYVTKDVDEDGILKALKHF 212
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 16-287 6.81e-20

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 87.06  E-value: 6.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  16 PYRLVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIP---IIAENGNYV--ADAGE 90
Cdd:PRK10513    2 AIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdyCITNNGALVqkAADGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  91 VVSVTSIDH-------------GVVTQLVHAIRQFNDNRVAAGRTplsviicgAASAYVEFFPPHFNIPEEVQ-QLQFne 156
Cdd:PRK10513   82 TVAQTALSYddylyleklsrevGVHFHALDRNTLYTANRDISYYT--------VHESFLTGIPLVFREVEKMDpNLQF-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 157 aakyyLKLQKVD--DVIAAAaedgIVKIA--AFDPYSVEEESADYLrsqsshlravvsgahwvDLIDANTNKGTALAALQ 232
Cdd:PRK10513  152 -----PKVMMIDepEILDAA----IARIPaeVKERYTVLKSAPYFL-----------------EILDKRVNKGTGVKSLA 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1080238649 233 EALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGV 287
Cdd:PRK10513  206 EHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGV 260
PRK15126 PRK15126
HMP-PP phosphatase;
17-272 1.41e-13

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 69.34  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  17 YRLVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVADA-GEVVSVT 95
Cdd:PRK15126    2 ARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLeGELLHRQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  96 SIDHGVVTQLVHA-------IRQFNDNRVAAGrtplsviicgaasayveffpphFNIPEevqQLQFNEAAKYYLKLQKVD 168
Cdd:PRK15126   82 DLPADVAELVLHQqwdtrasMHVFNDDGWFTG----------------------KEIPA---LLQAHVYSGFRYQLIDLK 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 169 DVIAaaaeDGIVKIAAFDPYSveeesaDYLRSQSSHLRAVVSGAHW-------VDLIDANTNKGTALAALQEALGVSPAE 241
Cdd:PRK15126  137 RLPA----HGVTKICFCGDHD------DLTRLQIQLNEALGERAHLcfsatdcLEVLPVGCNKGAALAVLSQHLGLSLAD 206

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1080238649 242 TVCFVDYLNDLELIDHAGRSFAMSNGHPEIK 272
Cdd:PRK15126  207 CMAFGDAMNDREMLGSVGRGFIMGNAMPQLR 237
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 19-264 1.29e-11

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: 62.78  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  19 LVVTDMDGTLLNEDK-EIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVADAGEVVSVTSI 97
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAhELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEILYIEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  98 DHGVVtQLVHAIRQFNDNRVAAGRTPLSVIICGAASAYVeffpphfnipeevqqlqfneaakYYLKLQKVDDVIAAAAED 177
Cdd:TIGR01484  81 DVFEE-ILGIKFEEIGAELKSLSEHYVGTFIEDKAIAVA-----------------------IHYVGAELGQELDSKMRE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 178 GIVKIAAFDPysveeesadylrsqssHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDH 257
Cdd:TIGR01484 137 RLEKIGRNDL----------------ELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEV 200


                  ....*..
gi 1080238649 258 AGRSFAM 264
Cdd:TIGR01484 201 AGLAVAV 207
PRK10976 PRK10976
putative hydrolase; Provisional
 17-295 5.78e-11

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 61.60  E-value: 5.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  17 YRLVVTDMDGTLLNEDKEIpDSFWPVVTELL-DRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVAD-AGEVVSV 94
Cdd:PRK10976    2 YQVVASDLDGTLLSPDHTL-SPYAKETLKLLtARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDtDGNLIFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  95 TSIDHGVVTQLVHAIRQ--------FNDNRVAAGRtplsviicgaasayveffpphfNIPEEVQQlqFNEAAKYYLKLQK 166
Cdd:PRK10976   81 HNLDRDIASDLFGVVHDnpdiitnvYRDDEWFMNR----------------------HRPEEMRF--FKEAVFKYQLYEP 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 167 vddviAAAAEDGIVKIaafdpYSVEEeSADYLRSQSSHLRAvvsgaHWVDLIDAN-------------TNKGTALAALQE 233
Cdd:PRK10976  137 -----GLLEPDGVSKV-----FFTCD-SHEKLLPLEQAINA-----RWGDRVNVSfstltclevmaggVSKGHALEAVAK 200

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238649 234 ALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNGHPEIKrratDIAP------SNAEEGVITTLRELF 295
Cdd:PRK10976  201 KLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNAHQRLK----DLLPelevigSNADDAVPHYLRKLY 264
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 17-292 1.06e-10

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 60.81  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  17 YRLVVTDMDGTLLNEDKEI-PDSFwPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGNYVAD--AGEVVS 93
Cdd:PRK10530    3 YRVIALDLDGTLLTPKKTIlPESL-EALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDyqAKKVLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  94 VTSIDHGVVTQLVHAIRQFN-------DNRVAAGRTPLSVIicgAASAYVEFFPPHfnipeevQQLQFneaakyylklQK 166
Cdd:PRK10530   82 ADPLPVQQALQVIEMLDEHQihglmyvDDAMLYEHPTGHVI---RTLNWAQTLPPE-------QRPTF----------TQ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 167 VDDVIAAAAE-DGIVKIAAFDPYSVEeesadyLRSQSSHLRAVVSGA---HWVDLID---ANTNKGTALAALQEALGVSP 239
Cdd:PRK10530  142 VDSLAQAARQvNAIWKFALTHEDLPQ------LQHFAKHVEHELGLEcewSWHDQVDiarKGNSKGKRLTQWVEAQGWSM 215

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1080238649 240 AETVCFVDYLNDLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVITTLR 292
Cdd:PRK10530  216 KNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIY 268
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 190-294 4.87e-10

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 58.51  E-value: 4.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 190 VEEESADYLRSQSSHLRAVVSGAHW--VDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNG 267
Cdd:cd02605   134 VIEQLEEMLLKAGLTVRIIYSSGLAydLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNA 213

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1080238649 268 HPEIKRRATDIAPSNAEE-----GVITTLREL 294
Cdd:cd02605   214 QPELLKWADRVTRSRLAKgpyagGILEGLAHF 245
PLN02887 PLN02887
hydrolase family protein
 14-287 9.90e-09

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 56.04  E-value: 9.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  14 QPPYRLVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLAD--QFAPIAHRIPIIAENGNYV------ 85
Cdd:PLN02887  305 KPKFSYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDilKMVDLAGKDGIISESSPGVflqgll 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  86 --ADAGEVVSVTSIDHGVVTQ-----LVHAIRQF---NDNRVAAGRTPLsviicgAASAYVEFFPPHFNIPEEVQQLqfn 155
Cdd:PLN02887  385 vyGRQGREIYRSNLDQEVCREaclysLEHKIPLIafsQDRCLTLFDHPL------VDSLHTIYHEPKAEIMSSVDQL--- 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 156 eaakyyLKLQKVDDVIAAAAEDGIVkiAAFDPYSVE--EESADYLRSQSSHLRAVVSGahwvdlidanTNKGTALAALQE 233
Cdd:PLN02887  456 ------LAAADIQKVIFLDTAEGVS--SVLRPYWSEatGDRANVVQAQPDMLEIVPPG----------TSKGNGVKMLLN 517

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1080238649 234 ALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGV 287
Cdd:PLN02887  518 HLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGV 571
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 223-294 1.32e-08

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


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 53.13  E-value: 1.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238649 223 NKGTALAALQEALGVSPAEtVCFV-DYLNDLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVIttlREL 294
Cdd:COG1778    83 DKLEALEELLAKLGLSPEE-VAYIgDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAV---REV 151
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 185-286 1.36e-08

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 54.39  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 185 FDPYSVEEEsADYLRSQsshLRAVVSGAHWvDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDHAGRSFAM 264
Cdd:TIGR01482 116 IDVDTVREI-IKELGLN---LVAVDSGFDI-HILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAV 190

                          90       100
                  ....*....|....*....|..
gi 1080238649 265 SNGHPEIKRRATDIAPSNAEEG 286
Cdd:TIGR01482 191 ANAQPELKEWADYVTESPYGEG 212
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 223-295 3.26e-08

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 51.44  E-value: 3.26e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238649 223 NKGTALAALQEALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVITTLRELF 295
Cdd:cd07514    67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 223-294 1.91e-07

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 49.44  E-value: 1.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238649 223 NKGTALAALQEALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNGHPEIKRRATDIAPSNAEEGVIttlREL 294
Cdd:cd01630    76 DKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAV---REV 144
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 192-294 7.66e-07

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 49.20  E-value: 7.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 192 EESADYLRSQSSHLRAVVSGAHWvDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNGHPEI 271
Cdd:PRK01158  127 EEVRELLEELGLDLEIVDSGFAI-HIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEEL 205

                          90       100
                  ....*....|....*....|...
gi 1080238649 272 KRRATDIAPSNAEEGVITTLREL 294
Cdd:PRK01158  206 KEAADYVTEKSYGEGVAEAIEHL 228
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 186-270 2.83e-05

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 44.56  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 186 DPYSVEEESADYLRSQSSHLRAVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDHAGRSFAMS 265
Cdd:pfam05116 127 AAAAVLAELEQLLRKRGLDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVG 206


                  ....*
gi 1080238649 266 NGHPE 270
Cdd:pfam05116 207 NAQPE 211
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 196-287 5.11e-04

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: 40.49  E-value: 5.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 196 DYLRSQSSHLR-AVVSGAHWVDLIDANTNKGTALAALQEALGVSPAETVCFVDYLNDLELIDHAGRSFAMSNGHPEIKRR 274
Cdd:TIGR01487 119 DEVREIIKERGlNLVASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEI 198

                          90
                  ....*....|...
gi 1080238649 275 ATDIAPSNAEEGV 287
Cdd:TIGR01487 199 ADYVTSNPYGEGV 211
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 19-256 2.47e-03

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: 38.50  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  19 LVVTDMDGTLLNEDKEIPDSFWPVVTELLDRGVHFAPASGRQYATLADQFAPIAHRIPIIAENGnyvadagevvSVTSID 98
Cdd:cd07507     1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENG----------GAIFIP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649  99 HGvvtqlvhairQFNDNRVAAGRTPLSVIICGAasayveffpPHFNIPEEVQQLQFNEAAKYYLKLQKVDDVIAAAAedG 178
Cdd:cd07507    71 RG----------YFKFPGRCKSEGGYEVIELGK---------PYREIRAALEKIREETGFKITGFGDLTEEEIAELT--G 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238649 179 I----VKIAAFDPYSV-------EEESADYLRSQSSHLRAVVSGAHWVDLIDANTNKGTA---LAALQEALGVSPaETVC 244
Cdd:cd07507   130 LprerAALAKEREYSEtiilrsdEEEDEKVLEALEERGLKITKGGRFYHVLGAGADKGKAvaiLAALYRQLYEAI-VTVG 208

                         250
                  ....*....|..
gi 1080238649 245 FVDYLNDLELID 256
Cdd:cd07507   209 LGDSPNDLPMLE 220
 
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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