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Conserved domains on  [gi|1469307036|ref|WP_117648466|]
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HAD family hydrolase [Collinsella sp. TM09-10AT]

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

 Zoom to residue level

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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 ...
 8-271 1.03e-48

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: 159.53  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   8 IKAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEglvDVLVGCGGAEVIDRAHNIn 87
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLD---DPLITSNGALIYDPDGEV- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  88 ELSYPLPGETIARICKHMADLpatpvcprdgvfyvpesnacvehlsrvdGVPYQVVDFAEFlrepqpkvmftmapevmpr 167
Cdd:COG0561    78 LYERPLDPEDVREILELLREH----------------------------GLHLQVVVRSGP------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 168 vierastfadntvkaaalqttqRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSAA 247
Cdd:COG0561   111 ----------------------GFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|....
gi 1469307036 248 TRAAADFVTASNDKDGIAIFIEEH 271
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEKL 192
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 8-271 1.03e-48

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: 159.53  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   8 IKAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEglvDVLVGCGGAEVIDRAHNIn 87
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLD---DPLITSNGALIYDPDGEV- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  88 ELSYPLPGETIARICKHMADLpatpvcprdgvfyvpesnacvehlsrvdGVPYQVVDFAEFlrepqpkvmftmapevmpr 167
Cdd:COG0561    78 LYERPLDPEDVREILELLREH----------------------------GLHLQVVVRSGP------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 168 vierastfadntvkaaalqttqRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSAA 247
Cdd:COG0561   111 ----------------------GFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|....
gi 1469307036 248 TRAAADFVTASNDKDGIAIFIEEH 271
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEKL 192
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 11-268 1.11e-47

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 159.33  E-value: 1.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  11 VFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRdaHATEAMYELWGIeGLVDVLVGCGGAEVIDRAHNInELS 90
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGR--PYRAILPVIKEL-GLDDPVICYNGALIYDENGKI-LYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  91 YPLPGETIARICKHMADLPATPVCPRDGVFYVPE---SNACVEHLSRVDGVPYQVVDFAEFLREPQPKVMFTMAPEVMPR 167
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNdneLEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 168 VIERastFADNTVKAAALQTTQRLY-EFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSA 246
Cdd:pfam08282 157 LEKE---LKELFGSLITITSSGPGYlEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASP 233

                         250       260
                  ....*....|....*....|..
gi 1469307036 247 ATRAAADFVTASNDKDGIAIFI 268
Cdd:pfam08282 234 EVKAAADYVTDSNNEDGVAKAL 255
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 11-270 2.71e-46

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: 155.45  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  11 VFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRdahATEAMYELWGIEGLVDVLVGCGGAEVIDRAHNINeLS 90
Cdd:cd07516     2 IALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGR---PLRGAQPYLEELGLDSPLITFNGALVYDPTGKEI-LE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  91 YPLPGETIARICKHMADLPAtpvcprDGVFYVPESNACVEHLSRVDGVPYQVVDFAEFLREPQ----PKVMFTMAPEVMP 166
Cdd:cd07516    78 RLISKEDVKELEEFLRKLGI------GINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPdediTKILFVGEDEELD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 167 RVIERasTFADNTVKAAALQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSA 246
Cdd:cd07516   152 ELIAK--LPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                         250       260
                  ....*....|....*....|....
gi 1469307036 247 ATRAAADFVTASNDKDGIAIFIEE 270
Cdd:cd07516   230 EVKEAADYVTLTNNEDGVAKAIEK 253
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 10-268 8.50e-45

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: 151.65  E-value: 8.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  10 AVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVdvlVGCGGAEVIDraHNINEL 89
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPF---ITANGAAVID--DQGEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  90 S-YPLPGETIARICKHMADLPAT-PVCPRDGVFYVPESNACVEHLSRVDGVPYQVVDFAEFLRE-PQPKVMFTMAPEVMP 166
Cdd:TIGR00099  76 YkKPLDLDLVEEILNFLKKHGLDvILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDdILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 167 RVIER--ASTFADN-TVkaaaLQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMAN 243
Cdd:TIGR00099 156 LLIEAlnKLELEENvSV----VSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGN 231

                         250       260
                  ....*....|....*....|....*
gi 1469307036 244 GSAATRAAADFVTASNDKDGIAIFI 268
Cdd:TIGR00099 232 ADEELKALADYVTDSNNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 8-273 6.07e-33

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 121.34  E-value: 6.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   8 IKAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVDVLVGCGGAeVIDRAHNin 87
Cdd:PRK10513    3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGA-LVQKAAD-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  88 elsyplpGETIARickhmadlpaTPVCPRDGVFYvpesnacvEHLSRVDGVPYQVVDFAEFLREPQ-------------- 153
Cdd:PRK10513   80 -------GETVAQ----------TALSYDDYLYL--------EKLSREVGVHFHALDRNTLYTANRdisyytvhesfltg 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 154 -----------------PKVMFTMAPEVMPRVIERAStfADNTVKAAALQTTQRLYEFMDPRVSKTRGLVRVAELNGMEL 216
Cdd:PRK10513  135 iplvfrevekmdpnlqfPKVMMIDEPEILDAAIARIP--AEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKP 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307036 217 QDICVFGDADNDTCMVADAGVGVAMANGSAATRAAADFVTASNDKDGIAIFIEEHLL 273
Cdd:PRK10513  213 EEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKYVL 269
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 8-271 1.03e-48

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: 159.53  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   8 IKAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEglvDVLVGCGGAEVIDRAHNIn 87
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLD---DPLITSNGALIYDPDGEV- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  88 ELSYPLPGETIARICKHMADLpatpvcprdgvfyvpesnacvehlsrvdGVPYQVVDFAEFlrepqpkvmftmapevmpr 167
Cdd:COG0561    78 LYERPLDPEDVREILELLREH----------------------------GLHLQVVVRSGP------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 168 vierastfadntvkaaalqttqRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSAA 247
Cdd:COG0561   111 ----------------------GFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|....
gi 1469307036 248 TRAAADFVTASNDKDGIAIFIEEH 271
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEKL 192
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 11-268 1.11e-47

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 159.33  E-value: 1.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  11 VFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRdaHATEAMYELWGIeGLVDVLVGCGGAEVIDRAHNInELS 90
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGR--PYRAILPVIKEL-GLDDPVICYNGALIYDENGKI-LYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  91 YPLPGETIARICKHMADLPATPVCPRDGVFYVPE---SNACVEHLSRVDGVPYQVVDFAEFLREPQPKVMFTMAPEVMPR 167
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNdneLEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 168 VIERastFADNTVKAAALQTTQRLY-EFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSA 246
Cdd:pfam08282 157 LEKE---LKELFGSLITITSSGPGYlEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASP 233

                         250       260
                  ....*....|....*....|..
gi 1469307036 247 ATRAAADFVTASNDKDGIAIFI 268
Cdd:pfam08282 234 EVKAAADYVTDSNNEDGVAKAL 255
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 11-270 2.71e-46

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: 155.45  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  11 VFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRdahATEAMYELWGIEGLVDVLVGCGGAEVIDRAHNINeLS 90
Cdd:cd07516     2 IALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGR---PLRGAQPYLEELGLDSPLITFNGALVYDPTGKEI-LE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  91 YPLPGETIARICKHMADLPAtpvcprDGVFYVPESNACVEHLSRVDGVPYQVVDFAEFLREPQ----PKVMFTMAPEVMP 166
Cdd:cd07516    78 RLISKEDVKELEEFLRKLGI------GINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPdediTKILFVGEDEELD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 167 RVIERasTFADNTVKAAALQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSA 246
Cdd:cd07516   152 ELIAK--LPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                         250       260
                  ....*....|....*....|....
gi 1469307036 247 ATRAAADFVTASNDKDGIAIFIEE 270
Cdd:cd07516   230 EVKEAADYVTLTNNEDGVAKAIEK 253
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 10-268 8.50e-45

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: 151.65  E-value: 8.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  10 AVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVdvlVGCGGAEVIDraHNINEL 89
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPF---ITANGAAVID--DQGEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  90 S-YPLPGETIARICKHMADLPAT-PVCPRDGVFYVPESNACVEHLSRVDGVPYQVVDFAEFLRE-PQPKVMFTMAPEVMP 166
Cdd:TIGR00099  76 YkKPLDLDLVEEILNFLKKHGLDvILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDdILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 167 RVIER--ASTFADN-TVkaaaLQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMAN 243
Cdd:TIGR00099 156 LLIEAlnKLELEENvSV----VSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGN 231

                         250       260
                  ....*....|....*....|....*
gi 1469307036 244 GSAATRAAADFVTASNDKDGIAIFI 268
Cdd:TIGR00099 232 ADEELKALADYVTDSNNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 8-273 6.07e-33

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 121.34  E-value: 6.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   8 IKAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVDVLVGCGGAeVIDRAHNin 87
Cdd:PRK10513    3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGA-LVQKAAD-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  88 elsyplpGETIARickhmadlpaTPVCPRDGVFYvpesnacvEHLSRVDGVPYQVVDFAEFLREPQ-------------- 153
Cdd:PRK10513   80 -------GETVAQ----------TALSYDDYLYL--------EKLSREVGVHFHALDRNTLYTANRdisyytvhesfltg 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 154 -----------------PKVMFTMAPEVMPRVIERAStfADNTVKAAALQTTQRLYEFMDPRVSKTRGLVRVAELNGMEL 216
Cdd:PRK10513  135 iplvfrevekmdpnlqfPKVMMIDEPEILDAAIARIP--AEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKP 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307036 217 QDICVFGDADNDTCMVADAGVGVAMANGSAATRAAADFVTASNDKDGIAIFIEEHLL 273
Cdd:PRK10513  213 EEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKYVL 269
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 9-265 1.40e-28

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: 108.08  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   9 KAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVDVlvgcGGAEVIDRahniNE 88
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSYVSY----NGQYVFFE----GE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  89 LSY--PLPGETIARICKHmadlpatpvCPRDGVFYVPESNACvehlsrvdgvPYQVVDFAEFLREPQPKVMFTMAPEVmp 166
Cdd:cd07517    73 VIYknPLPQELVERLTEF---------AKEQGHPVSFYGQLL----------LFEDEEEEQKYEELRPELRFVRWHPL-- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 167 rvierastFADNTVKAaalqttqrlyefmdprVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSA 246
Cdd:cd07517   132 --------STDVIPKG----------------GSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHE 187

                         250
                  ....*....|....*....
gi 1469307036 247 ATRAAADFVTASNDKDGIA 265
Cdd:cd07517   188 ELKEIADYVTKDVDEDGIL 206
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 8-273 3.87e-18

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 80.79  E-value: 3.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   8 IKAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVdvlVGCGGAEVIDRAHNIN 87
Cdd:PRK01158    3 IKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPV---IAENGGVISVGFDGKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  88 ELSYPLPGETIARickhmadlpatpvcprdgvfyvpesnacvEHLSRvdgvpyqvvdfaeflREPQPKVMFTMAPEvMPR 167
Cdd:PRK01158   80 IFLGDIEECEKAY-----------------------------SELKK---------------RFPEASTSLTKLDP-DYR 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 168 VIERA--STFADNTVKAAA--------LQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGV 237
Cdd:PRK01158  115 KTEVAlrRTVPVEEVRELLeelgldleIVDSGFAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGF 194

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1469307036 238 GVAMANGSAATRAAADFVTASNDKDGIAIFIeEHLL 273
Cdd:PRK01158  195 GVAVANADEELKEAADYVTEKSYGEGVAEAI-EHLL 229
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 14-273 1.19e-17

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 80.45  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  14 DIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVdvlVGCGGAEVID-RAHNINElSYP 92
Cdd:PRK10530    9 DLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPA---ICCNGTYLYDyQAKKVLE-ADP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  93 LPgetiarickhmadlpatpvcprdgvfyVPESNACVEHLSRVD--GVPYqvVDFAEFLREPQPKVMFTMA-----PEVM 165
Cdd:PRK10530   85 LP---------------------------VQQALQVIEMLDEHQihGLMY--VDDAMLYEHPTGHVIRTLNwaqtlPPEQ 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 166 PRVIERASTFADNTVKAAAL-------QTTQRLYEFMDpRVSKTRGL---------VRVA--------------ELNGME 215
Cdd:PRK10530  136 RPTFTQVDSLAQAARQVNAIwkfalthEDLPQLQHFAK-HVEHELGLecewswhdqVDIArkgnskgkrltqwvEAQGWS 214

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307036 216 LQDICVFGDADNDTCMVADAGVGVAMANGSAATRAAADFVTASNDKDGIAIFIEEHLL 273
Cdd:PRK10530  215 MKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSHVL 272
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 9-269 4.49e-17

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: 76.85  E-value: 4.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   9 KAVFCDIDGTLLTSQHTV-SPRTVAAIRALRERGVLFGLCTGRdahateamyelwgieglvdvlvgcggaevidrahnin 87
Cdd:cd07518     1 KLIATDMDGTFLNDDKTYdHERFFAILDQLLKKGIKFVVASGR------------------------------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  88 elSYplpgetiARICKHMADLpatpvcpRDGVFYVPESNACVEHlsrvdgvpyqvvdfaeflrepqpKVMFTMAPEVMPR 167
Cdd:cd07518    44 --QY-------YQLISFFPEI-------KDEMSFVAENGAVVYF-----------------------KFTLNVPDEAAPD 84

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 168 VIERASTFADNTVKAAAlqTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSAA 247
Cdd:cd07518    85 IIDELNQKFGGILRAVT--SGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEE 162

                         250       260
                  ....*....|....*....|..
gi 1469307036 248 TRAAADFVTASNDKDGIAIFIE 269
Cdd:cd07518   163 VKAAAKYVAPSNNENGVLQVIE 184
PLN02887 PLN02887
hydrolase family protein
 5-271 9.58e-15

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 73.76  E-value: 9.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   5 FSHIkavFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHAT---EAMYELWGIEGLVD-----------V 70
Cdd:PLN02887  308 FSYI---FCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVidiLKMVDLAGKDGIISesspgvflqglL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  71 LVGCGGAEVIDRahNIN------------ELSYPLPGETIARiCKHMADLPAtpVCPRDGVFYVPESnacvEHLSRVDgv 138
Cdd:PLN02887  385 VYGRQGREIYRS--NLDqevcreaclyslEHKIPLIAFSQDR-CLTLFDHPL--VDSLHTIYHEPKA----EIMSSVD-- 453

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 139 pyQVVDFAEFlrepqPKVMFTMAPEVMPRVIERASTFADNTvKAAALQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQD 218
Cdd:PLN02887  454 --QLLAAADI-----QKVIFLDTAEGVSSVLRPYWSEATGD-RANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDE 525

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1469307036 219 ICVFGDADNDTCMVADAGVGVAMANGSAATRAAADFVTASNDKDGIAIFIEEH 271
Cdd:PLN02887  526 IMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAIYRY 578
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 10-241 1.06e-12

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: 65.48  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  10 AVFCDIDGTLLTSQ-HTVSPRTVAAIRALRERGVLFGLCTGRDahaTEAMYELWGiEGLVDVLVGCGGAEVIDRAHNINE 88
Cdd:TIGR01484   1 LLFFDLDGTLLDPNaHELSPETIEALERLREAGVKVVIVTGRS---LAEIKELLK-QLNLPLPLIAENGALIFYPGEILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  89 LSYPLPGETIARIckhmadlpatpvcprdgvfYVPESNACVEHLSRvdgvpyqvvDFAEFLREpQPKVMFT-------MA 161
Cdd:TIGR01484  77 IEPSDVFEEILGI-------------------KFEEIGAELKSLSE---------HYVGTFIE-DKAIAVAihyvgaeLG 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 162 PEVMPRVIERASTFADNTVKAAALQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAM 241
Cdd:TIGR01484 128 QELDSKMRERLEKIGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 8-268 1.13e-11

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


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 62.45  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   8 IKAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVdvlVGCGGAEVIDRAHNIn 87
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPV---VAENGGVIFYNKEDI- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  88 elsyplpgetiarickhmadlpatpvcprdgVFYVPESNACVEHLSRvdgvpyqvvdfaefLREPQPKVMFTMApevmpr 167
Cdd:TIGR01487  77 -------------------------------FLANMEEEWFLDEEKK--------------KRFPRDRLSNEYP------ 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 168 vieRASTFAD------NTVKAAA------LQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADA 235
Cdd:TIGR01487 106 ---RASLVIMregkdvDEVREIIkerglnLVASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVV 182

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1469307036 236 GVGVAMANGSAATRAAADFVTASNDKDGIAIFI 268
Cdd:TIGR01487 183 GFKVAVANADDQLKEIADYVTSNPYGEGVVEVL 215
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 199-273 1.50e-10

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: 57.98  E-value: 1.50e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307036 199 VSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMANGSAATRAAADFVTASNDKDGIAIFIeEHLL 273
Cdd:cd07514    66 VDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAI-DKLL 139
PRK10976 PRK10976
putative hydrolase; Provisional
 11-243 1.97e-08

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 53.90  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  11 VFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEglvDVLVGCGGAevidRAHNIN-EL 89
Cdd:PRK10976    5 VASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIK---SYMITSNGA----RVHDTDgNL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  90 --SYPLPGETIARICKHMADLP--ATPVCpRDGVFYVPESNACVEHLSRVDGVPYQVVDFAEFLREPQPKVMFTMAPEVM 165
Cdd:PRK10976   78 ifSHNLDRDIASDLFGVVHDNPdiITNVY-RDDEWFMNRHRPEEMRFFKEAVFKYQLYEPGLLEPDGVSKVFFTCDSHEK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036 166 PRVIERA--STFADNTVKAAALQTTqrlYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMAN 243
Cdd:PRK10976  157 LLPLEQAinARWGDRVNVSFSTLTC---LEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGN 233
PRK15126 PRK15126
HMP-PP phosphatase;
10-243 5.19e-08

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 52.77  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  10 AVFcDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRdaHATEaMYELWGIEGLVDVLVGCGGAEVIDraHNINEL 89
Cdd:PRK15126    5 AAF-DMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGR--HVLE-MQHILGALSLDAYLITGNGTRVHS--LEGELL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036  90 -SYPLPGETIARICKHMADLPATPVCPRDGVFYVPESNACVEHLSRVDGVPYQVVDFAEFLREPQPKVMFTMAPEVMPRV 168
Cdd:PRK15126   79 hRQDLPADVAELVLHQQWDTRASMHVFNDDGWFTGKEIPALLQAHVYSGFRYQLIDLKRLPAHGVTKICFCGDHDDLTRL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307036 169 -IERASTFADntvKAAALQTTQRLYEFMDPRVSKTRGLVRVAELNGMELQDICVFGDADNDTCMVADAGVGVAMAN 243
Cdd:PRK15126  159 qIQLNEALGE---RAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGN 231
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 10-84 3.22e-07

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 47.78  E-value: 3.22e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307036  10 AVFCDIDGTLLTsqhtvsprtVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVDVLVGCGGAEVIDRAH 84
Cdd:cd01427     1 AVLFDLDGTLLA---------VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKP 66
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 8-137 1.01e-04

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: 41.35  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307036   8 IKAVFCDIDGTLlTSQH-----------TVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEglvDVLVGcgg 76
Cdd:cd01630     1 IKLLVLDVDGVL-TDGRiyydsngeelkSFNVRDGLGIKLLQKSGIEVAIITGRQSEAVRRRAKELGIE---DLFQG--- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307036  77 aeVIDRAHNINEL--SYPLPGETIARICKHMADLP-----ATPVCPRDGVFYVPEsnaCVEHLSRVDG 137
Cdd:cd01630    74 --VKDKLEALEELleKLGLSDEEVAYMGDDLPDLPvmkrvGLSVAPADAHPEVRE---AADYVTRARG 136
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
 223-260 1.42e-04

uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7; This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319795 [Multi-domain]  Cd Length: 661  Bit Score: 43.04  E-value: 1.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1469307036 223 GDADNDTCMVADAGVGVAMANGSAATRAAADFVTASND 260
Cdd:cd02609   527 GDGVNDVLALKEADCSIAMASGSDATRQVAQVVLLDSD 564
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
2-73 9.94e-04

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 39.53  E-value: 9.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307036   2 DTTFSHIKAVFCDIDGTLLTSQHTVSPRTVAAIRALRERGVLFGLCTGRDAHATEAMYELWGIEGLVDVLVG 73
Cdd:COG0546    61 DEELEELLARFRELYEEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVG 132
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-48 1.11e-03

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 39.71  E-value: 1.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1469307036   1 MDTTFSHIKAVFCDIDGTLLTSqHTVSPRTVAAIRALRERGVLFGLCT 48
Cdd:COG0647     1 MSELADRYDAFLLDLDGVLYRG-DEPIPGAVEALARLRAAGKPVLFLT 47
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
 215-260 3.03e-03

P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319774 [Multi-domain]  Cd Length: 617  Bit Score: 38.73  E-value: 3.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1469307036 215 ELQD----ICVFGDADNDTCMVADAGVGVAMANGSAATRAAADFVTASND 260
Cdd:cd02079   505 ALQAeggpVAMVGDGINDAPALAQADVGIAMGSGTDVAIETADIVLLSND 554
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 11-48 5.06e-03

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 35.52  E-value: 5.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1469307036  11 VFCDIDGTLLTSQHTVsPRTVAAIRALRERGVLFGLCT 48
Cdd:pfam13344   1 FLFDIDGVLWRGGEPI-PGAAEALRALRAAGKPVVFVT 37
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
 219-269 8.04e-03

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 37.64  E-value: 8.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1469307036 219 ICVFGDADNDTCMVADAGVGVAMANGSAATRAAADFVTASNDKDGIAIFIE 269
Cdd:cd07550   487 VAFVGDGINDSPALSYADVGISMRGGTDIARETADVVLLEDDLRGLAEAIE 537
 
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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