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Conserved domains on  [gi|554669307|ref|WP_023171570|]
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HAD family hydrolase [Gloeobacter kilaueensis]

Protein Classification

HAD family hydrolase( domain architecture ID 11426169)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-217 6.07e-36

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: 132.95  E-value: 6.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   3 YLALACDYDGTLA-ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASRE--AV 79
Cdd:COG0561    2 IKLIALDLDGTLLnDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVlyER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  80 PLAAAPPEAFVERLKEQNVSPlsvgHVIVATWEpnetavlaairdlglelqvifnkGAVMVLPAGINKASGLAAALAELG 159
Cdd:COG0561   82 PLDPEDVREILELLREHGLHL----QVVVRSGP-----------------------GFLEILPKGVSKGSALKKLAERLG 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 554669307 160 LSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVTGGARGAGVIELIERL 217
Cdd:COG0561  135 IPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
HerA super family cl33869
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 312-401 4.51e-07

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0433:

Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 52.30  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307 312 VLELLERPDHNVVVNLLGIPLADRPAFFADLLPQLQQLRVQTAR------PHWIVVDEAHHLLPSTWDPATLTLPQALK- 384
Cdd:COG0433  209 LEDLLRTDGRVTVIDLSGLPEELQSTFVLWLLRELFEARPEVGDaddrklPLVLVIDEAHLLAPAAPSALLEILERIARe 288

                         90       100
                 ....*....|....*....|...
gi 554669307 385 ------GMILVTVHPESVSPAAL 401
Cdd:COG0433  289 grkfgvGLILATQRPSDIDEDVL 311
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-217 6.07e-36

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: 132.95  E-value: 6.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   3 YLALACDYDGTLA-ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASRE--AV 79
Cdd:COG0561    2 IKLIALDLDGTLLnDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVlyER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  80 PLAAAPPEAFVERLKEQNVSPlsvgHVIVATWEpnetavlaairdlglelqvifnkGAVMVLPAGINKASGLAAALAELG 159
Cdd:COG0561   82 PLDPEDVREILELLREHGLHL----QVVVRSGP-----------------------GFLEILPKGVSKGSALKKLAERLG 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 554669307 160 LSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVTGGARGAGVIELIERL 217
Cdd:COG0561  135 IPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-187 7.53e-22

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: 93.98  E-value: 7.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307    5 ALACDYDGTLA--ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPA-------- 74
Cdd:TIGR01484   1 LLFFDLDGTLLdpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGeilyieps 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   75 ------SREAVPLAAAPPEAFVERLKEQNVSPLSVGHVIVA----TWEPNETAVLAAIRDLG---LELQVIF-NKGAVMV 140
Cdd:TIGR01484  81 dvfeeiLGIKFEEIGAELKSLSEHYVGTFIEDKAIAVAIHYvgaeLGQELDSKMRERLEKIGrndLELEAIYsGKTDLEV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 554669307  141 LPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAV 187
Cdd:TIGR01484 161 LPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-219 1.23e-17

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 82.33  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   1 MHYLALACDYDGTLA-ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASREAV 79
Cdd:PRK01158   1 MKIKAIAIDIDGTITdKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPVIAENGGVISVGFDGKRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  80 PLAAAP-------------PEAFVERlkEQNVSPLSVGHVIVATWEPNETaVLAAIRDLGLELQVIFNKGAVMVLPAGIN 146
Cdd:PRK01158  81 FLGDIEecekayselkkrfPEASTSL--TKLDPDYRKTEVALRRTVPVEE-VRELLEELGLDLEIVDSGFAIHIKSPGVN 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554669307 147 KASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVTGGARGAGVIELIERLVE 219
Cdd:PRK01158 158 KGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVAEAIEHLLL 230
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-203 1.86e-17

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 82.29  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307    6 LACDYDGTLA-ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLY---------RPAS 75
Cdd:pfam08282   1 IASDLDGTLLnSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYdengkilysNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   76 REAVplaaappEAFVERLKEQNVS--------------------------PLSVGHVIVATWEPNETAVL---------- 119
Cdd:pfam08282  81 KEAV-------KEIIEYLKENNLEillytddgvyilndnelekilkelnyTKSFVPEIDDFELLEDEDINkililldeed 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  120 -----AAIRDLGLELQVIFN--KGAVMVLPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALP 192
Cdd:pfam08282 154 ldeleKELKELFGSLITITSsgPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASP 233

                         250
                  ....*....|.
gi 554669307  193 ALKDLADFVTG 203
Cdd:pfam08282 234 EVKAAADYVTD 244
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-203 2.02e-14

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: 73.40  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   6 LACDYDGTL-AADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASREavPLAAA 84
Cdd:cd07516    2 IALDLDGTLlNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKE--ILERL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  85 PPEAFVERLKEQNVSPLSVGHVIVAT------WEPNETA----VLAAIRDLGLELQVIFNKGAVM--------------- 139
Cdd:cd07516   80 ISKEDVKELEEFLRKLGIGINIYTNDdwadtiYEENEDDeiikPAEILDDLLLPPDEDITKILFVgedeeldeliaklpe 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307 140 -----------------VLPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVT 202
Cdd:cd07516  160 effddlsvvrsapfyleIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAADYVT 239


                 .
gi 554669307 203 G 203
Cdd:cd07516  240 L 240
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 312-401 4.51e-07

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 52.30  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307 312 VLELLERPDHNVVVNLLGIPLADRPAFFADLLPQLQQLRVQTAR------PHWIVVDEAHHLLPSTWDPATLTLPQALK- 384
Cdd:COG0433  209 LEDLLRTDGRVTVIDLSGLPEELQSTFVLWLLRELFEARPEVGDaddrklPLVLVIDEAHLLAPAAPSALLEILERIARe 288

                         90       100
                 ....*....|....*....|...
gi 554669307 385 ------GMILVTVHPESVSPAAL 401
Cdd:COG0433  289 grkfgvGLILATQRPSDIDEDVL 311
 
Name Accession Description Interval E-value
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-217 6.07e-36

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: 132.95  E-value: 6.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   3 YLALACDYDGTLA-ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASRE--AV 79
Cdd:COG0561    2 IKLIALDLDGTLLnDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVlyER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  80 PLAAAPPEAFVERLKEQNVSPlsvgHVIVATWEpnetavlaairdlglelqvifnkGAVMVLPAGINKASGLAAALAELG 159
Cdd:COG0561   82 PLDPEDVREILELLREHGLHL----QVVVRSGP-----------------------GFLEILPKGVSKGSALKKLAERLG 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 554669307 160 LSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVTGGARGAGVIELIERL 217
Cdd:COG0561  135 IPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-187 7.53e-22

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: 93.98  E-value: 7.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307    5 ALACDYDGTLA--ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPA-------- 74
Cdd:TIGR01484   1 LLFFDLDGTLLdpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGeilyieps 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   75 ------SREAVPLAAAPPEAFVERLKEQNVSPLSVGHVIVA----TWEPNETAVLAAIRDLG---LELQVIF-NKGAVMV 140
Cdd:TIGR01484  81 dvfeeiLGIKFEEIGAELKSLSEHYVGTFIEDKAIAVAIHYvgaeLGQELDSKMRERLEKIGrndLELEAIYsGKTDLEV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 554669307  141 LPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAV 187
Cdd:TIGR01484 161 LPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 5-214 7.44e-21

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: 91.34  E-value: 7.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307    5 ALACDYDGTLAADGRV-DEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENG-ALLYRPASREavpLA 82
Cdd:TIGR01487   3 LVAIDIDGTLTDPNRMiSERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGgVIFYNKEDIF---LA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   83 AAPPEAFVERLKE--------QNVSPLSVGHVIVATWEPNEtaVLAAIRDLGLELqviFNKG-AVMVLPAGINKASGLAA 153
Cdd:TIGR01487  80 NMEEEWFLDEEKKkrfprdrlSNEYPRASLVIMREGKDVDE--VREIIKERGLNL---VASGfAIHIMKKGVDKGVGVEK 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 554669307  154 ALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVTGGARGAGVIELI 214
Cdd:TIGR01487 155 LKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIADYVTSNPYGEGVVEVL 215
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-219 1.23e-17

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 82.33  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   1 MHYLALACDYDGTLA-ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASREAV 79
Cdd:PRK01158   1 MKIKAIAIDIDGTITdKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPVIAENGGVISVGFDGKRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  80 PLAAAP-------------PEAFVERlkEQNVSPLSVGHVIVATWEPNETaVLAAIRDLGLELQVIFNKGAVMVLPAGIN 146
Cdd:PRK01158  81 FLGDIEecekayselkkrfPEASTSL--TKLDPDYRKTEVALRRTVPVEE-VRELLEELGLDLEIVDSGFAIHIKSPGVN 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554669307 147 KASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVTGGARGAGVIELIERLVE 219
Cdd:PRK01158 158 KGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVAEAIEHLLL 230
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-203 1.86e-17

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 82.29  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307    6 LACDYDGTLA-ADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLY---------RPAS 75
Cdd:pfam08282   1 IASDLDGTLLnSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYdengkilysNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   76 REAVplaaappEAFVERLKEQNVS--------------------------PLSVGHVIVATWEPNETAVL---------- 119
Cdd:pfam08282  81 KEAV-------KEIIEYLKENNLEillytddgvyilndnelekilkelnyTKSFVPEIDDFELLEDEDINkililldeed 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  120 -----AAIRDLGLELQVIFN--KGAVMVLPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALP 192
Cdd:pfam08282 154 ldeleKELKELFGSLITITSsgPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASP 233

                         250
                  ....*....|.
gi 554669307  193 ALKDLADFVTG 203
Cdd:pfam08282 234 EVKAAADYVTD 244
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-211 1.61e-16

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: 79.04  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307    6 LACDYDGTLAADGR-VDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASREAVPLAAA 84
Cdd:TIGR01482   1 IASDIDGTLTDPNRaINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGGEISYNEGLDDIFLAYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   85 PPEAF----------VERLKEQnvSPLSVG-HVIVATWEPNEtaVLAAIRDLGLELQVIFNKGAVMVLPAGINKASGLAA 153
Cdd:TIGR01482  81 EEEWFldiviaktfpFSRLKVQ--YPRRASlVKMRYGIDVDT--VREIIKELGLNLVAVDSGFDIHILPQGVNKGVAVKK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 554669307  154 ALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVT------GGARGAGVI 211
Cdd:TIGR01482 157 LKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADYVTespygeGGAEAIGEI 220
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-203 2.02e-14

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: 73.40  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   6 LACDYDGTL-AADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASREavPLAAA 84
Cdd:cd07516    2 IALDLDGTLlNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKE--ILERL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  85 PPEAFVERLKEQNVSPLSVGHVIVAT------WEPNETA----VLAAIRDLGLELQVIFNKGAVM--------------- 139
Cdd:cd07516   80 ISKEDVKELEEFLRKLGIGINIYTNDdwadtiYEENEDDeiikPAEILDDLLLPPDEDITKILFVgedeeldeliaklpe 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307 140 -----------------VLPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVT 202
Cdd:cd07516  160 effddlsvvrsapfyleIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAADYVT 239


                 .
gi 554669307 203 G 203
Cdd:cd07516  240 L 240
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 5-217 7.42e-14

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: 68.77  E-value: 7.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   5 ALACDYDGTLA-ADGRVDEATLQALRKLRNSGRKLLLVTGRELeDLERAFPHLELFER-VVAENGALlyrpasreavpla 82
Cdd:cd07514    1 LIAVDIDGTLTdRRRSIDLRAIEAIRKLEKAGIPVVLVTGNSL-PVARALAKYLGLSGpVVAENGGV------------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  83 aappeafverlkeqnvsplSVGhvivatwepneTAVLAAIRDLGLElqvifnkgavmvlpaginkasglaaalaelglsP 162
Cdd:cd07514   67 -------------------DKG-----------TGLEKLAERLGID---------------------------------P 83

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 554669307 163 HNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVTGGARGAGVIELIERL 217
Cdd:cd07514   84 EEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKL 138
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-214 2.44e-13

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: 69.99  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307    5 ALACDYDGTLAADG-RVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYRPASRE--AVPL 81
Cdd:TIGR00099   1 LIFIDLDGTLLNDDhTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEIlyKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   82 AAAPPEAFVERLKEQNVS-----------PLSVGHVIVAT----WEPN---------------------ETAVLAAIRD- 124
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDvilygddsiyaSKNDPEYFTIFkkflGEPKlevvdiqylpddilkilllflDPEDLDLLIEa 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  125 ---LGLELQ---VIFNKGAVMVLPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLA 198
Cdd:TIGR00099 161 lnkLELEENvsvVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALA 240

                         250
                  ....*....|....*.
gi 554669307  199 DFVTGGARGAGVIELI 214
Cdd:TIGR00099 241 DYVTDSNNEDGVALAL 256
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 9-202 1.24e-11

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: 64.17  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   9 DYDGTL-AADGRVDEATLQALRKLRNSGRKLLLVTGR---ELEDLERAFPhlelFERVVAENGA-------LLYrpasre 77
Cdd:cd07517    6 DIDGTLlDEDTTIPESTKEAIAALKEKGILVVIATGRapfEIQPIVKALG----IDSYVSYNGQyvffegeVIY------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  78 AVPLAAAPPEAFVERLKEQNVsPLSVGHVIVATWEPNETAVLAAIRDlglELQVI-FNKGAVMVLPAGINKASGLAAALA 156
Cdd:cd07517   76 KNPLPQELVERLTEFAKEQGH-PVSFYGQLLLFEDEEEEQKYEELRP---ELRFVrWHPLSTDVIPKGGSKAKGIQKVIE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 554669307 157 ELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVT 202
Cdd:cd07517  152 HLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYVT 197
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 5-215 1.47e-11

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: 63.37  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   5 ALACDYDGT-LAADGRVDEATLQA-LRKLRNSGRKLLLVTGRELEDLERAFPhlELFERV--VAENGALLYrpaSREAVP 80
Cdd:cd07518    2 LIATDMDGTfLNDDKTYDHERFFAiLDQLLKKGIKFVVASGRQYYQLISFFP--EIKDEMsfVAENGAVVY---FKFTLN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  81 LAAAPPEAFVERLKEQnvspLSVGHVIVATwepnetavlaairdlglelqvifNKGAVMVLPAGINKASGLAAALAELGL 160
Cdd:cd07518   77 VPDEAAPDIIDELNQK----FGGILRAVTS-----------------------GFGSIDIIPPGVNKATGLKQLLKHWGI 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 554669307 161 SPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVTGGARGAGVIELIE 215
Cdd:cd07518  130 SPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE 184
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
4-147 2.04e-10

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 61.36  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   4 LALACDYDGTLA------ADGRVDEATLQALRKL-RNSGRKLLLVTGRELEDLERAFPHLELFerVVAENGA-LLYRPAS 75
Cdd:COG1877    4 LLLFLDFDGTLApivpdpDAARPPPELRELLRRLaARPGGAVAIVSGRDLADLDRLLGPLGLP--LAGSHGAeRRLPGGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  76 REAVPLAAAPPE------------------AFVERlKeqnvsPLSVG-HVI-VATWEPNE--TAVLAAIRDLGLELQVIF 133
Cdd:COG1877   82 WEVLPLAAEAPEwldalraalealaartpgVLVED-K-----GASLAlHYRqAPPEEAEElrAALRELAARLGPGLEVLP 155

                        170
                 ....*....|....
gi 554669307 134 NKGAVMVLPAGINK 147
Cdd:COG1877  156 GKKVVELRPAGVDK 169
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 5-147 2.01e-09

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. 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: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 58.07  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   5 ALACDYDGTLA------ADGRVDEATLQALRKLRNSGRKLL-LVTGRELEDLERAFPHLELFerVVAENGALLYRPASRE 77
Cdd:cd01627    1 LLFLDYDGTLApivpdpDAAVPSPELLEALKKLAADPKNAVaIVSGRDLDDLDKWLGLPGIG--LAGEHGAEIRLPGGGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  78 AVPLAAAP-------------------PEAFVERlKE-------QNVSPLSVGHVivatwepnETAVLAAIRDLGLELQV 131
Cdd:cd01627   79 WVTLAPKAdlewkeeveaifkyftertPGSLVED-KGaslawhyRNADPEGARAA--------LELALHLASDLLKALEV 149

                        170
                 ....*....|....*.
gi 554669307 132 IFNKGAVMVLPAGINK 147
Cdd:cd01627  150 VPGKKVVEVRPVGVNK 165
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 6-218 4.08e-07

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 51.62  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   6 LACDYDGTL-AADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELF---ERVVAENGALLYRPASREAVPL 81
Cdd:PRK10513   6 IAIDMDGTLlLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEqpgDYCITNNGALVQKAADGETVAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  82 AAAPPE--AFVERLK----------------------------EQNVSPLSVGHVIVATWEPN----------ETAVL-A 120
Cdd:PRK10513  86 TALSYDdyLYLEKLSrevgvhfhaldrntlytanrdisyytvhESFLTGIPLVFREVEKMDPNlqfpkvmmidEPEILdA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307 121 AIRDLGLELqviFNKGAVM--------VLPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALP 192
Cdd:PRK10513 166 AIARIPAEV---KERYTVLksapyfleILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIP 242

                        250       260
                 ....*....|....*....|....*.
gi 554669307 193 ALKDLADFVTGGARGAGVIELIERLV 218
Cdd:PRK10513 243 SVKEVAQFVTKSNLEDGVAFAIEKYV 268
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 312-401 4.51e-07

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 52.30  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307 312 VLELLERPDHNVVVNLLGIPLADRPAFFADLLPQLQQLRVQTAR------PHWIVVDEAHHLLPSTWDPATLTLPQALK- 384
Cdd:COG0433  209 LEDLLRTDGRVTVIDLSGLPEELQSTFVLWLLRELFEARPEVGDaddrklPLVLVIDEAHLLAPAAPSALLEILERIARe 288

                         90       100
                 ....*....|....*....|...
gi 554669307 385 ------GMILVTVHPESVSPAAL 401
Cdd:COG0433  289 grkfgvGLILATQRPSDIDEDVL 311
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-218 3.49e-06

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 48.87  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   1 MHYLALACDYDGT-LAADGRVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGALLYR-PASR-- 76
Cdd:PRK10530   1 MTYRVIALDLDGTlLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDyQAKKvl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  77 EAVPLAAAPPEAFVERLKEQNVSPL-----------SVGHVI-VATW--------EPNETAV---LAAIRD--------- 124
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHQIHGLmyvddamlyehPTGHVIrTLNWaqtlppeqRPTFTQVdslAQAARQvnaiwkfal 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307 125 ------------------LGLEL------QVIFNKgavmvlpAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSA 180
Cdd:PRK10530 161 thedlpqlqhfakhveheLGLECewswhdQVDIAR-------KGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEA 233

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 554669307 181 CECAVAVANALPALKDLADFVTGGARGAGVIELIERLV 218
Cdd:PRK10530 234 AGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSHV 271
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 6-215 4.75e-05

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: 45.03  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   6 LACDYDGTLAADGRVDEAT--LQALRKLRNSGRKLLLV--TGRELEDLERAFPHLELFE--RVVAENGALLYRPASREAV 79
Cdd:cd02605    2 LVSDLDETLVGHDTNLQALerLQDLLEQLTADNDVILVyaTGRSPESVLELIKEVMLPKpdFIISDVGTEIYYGESGYLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307  80 P--------LAAAPPEAFVERLKEQNVSPLSVG----------HVIVATWEPNETAVLAAIRDLGLELQVIFNKGAVM-- 139
Cdd:cd02605   82 PdtywnevlSEGWERFLFEAIADLFKQLKPQSEleqnphkisfYLDPQNDAAVIEQLEEMLLKAGLTVRIIYSSGLAYdl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307 140 -VLPAGINKASGLAAALAELGLSPHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVT--GGARG---AGVIEL 213
Cdd:cd02605  162 dILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTrsRLAKGpyaGGILEG 241


                 ..
gi 554669307 214 IE 215
Cdd:cd02605  242 LA 243
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-100 8.31e-05

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: 42.00  E-value: 8.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554669307   5 ALACDYDGTLAAdgrvdeatLQALRKLRNSGRKLLLVTGRELEDLERAFPHLEL---FERVVAENGALLYRPAsreavpl 81
Cdd:cd01427    1 AVLFDLDGTLLA--------VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLgdlFDGIIGSDGGGTPKPK------- 65

                         90
                 ....*....|....*....
gi 554669307  82 aaapPEAFVERLKEQNVSP 100
Cdd:cd01427   66 ----PKPLLLLLLKLGVDP 80
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
 9-70 8.66e-04

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 42.22  E-value: 8.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 554669307   9 DYDGTLA------ADGRVDEATLQALRKLRNSGR-KLLLVTGRELEDLERAFPHLELFerVVAENGALL 70
Cdd:PRK14501 498 DYDGTLVpfapdpELAVPDKELRDLLRRLAADPNtDVAIISGRDRDTLERWFGDLPIH--LVAEHGAWS 564
HAD_PTase cd07519
hydrolase domain of the bifunctional HAD hydrolase/UbiA family prenyltransferase proteins and ...
 5-69 8.67e-04

hydrolase domain of the bifunctional HAD hydrolase/UbiA family prenyltransferase proteins and related domains; belongs to the haloacid dehalogenase-like superfamily; This family includes bifunctional enzymes that have both an N-terminal HAD hydrolase domain and a C-terminal UbiA family prenyltransferase domain. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases (PTases) and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. PTases catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 319821  Cd Length: 105  Bit Score: 38.87  E-value: 8.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554669307   5 ALACDYDGTLAADgrVDEATLQALRKLRNSGRKLLLVTGRELEDLERAFPHLELFERVVAENGAL 69
Cdd:cd07519    1 PLVVDLDGTLLLP--YNAEVLDYIQAARAEGRSIVLATASDQRIADRIAAHLGLFDGVFASDGRL 63
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
162-220 7.27e-03

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 37.99  E-value: 7.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 554669307 162 PHNVAGVGDAENDHAFLSACECAVAVANALPALKDLADFVT--GGARGAgVIELIERLVES 220
Cdd:PRK09484 112 PEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTriAGGRGA-VREVCDLLLLA 171
 
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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