NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|893705012|ref|WP_048933648|]
View 

MULTISPECIES: alpha/beta hydrolase [Ralstonia]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  37582413|12369917|19508187

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
76-308 1.81e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 108.81  E-value: 1.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012  76 DVFTPEGpSTTPRPVLIFVhgggfvggdkH----AAGSP-FYDNVMLW-ATQHGMVGVNINHRLAPQNPWPAGTEDVGLA 149
Cdd:COG0657    2 DVYRPAG-AKGPLPVVVYF----------HgggwVSGSKdTHDPLARRlAARAGAAVVSVDYRLAPEHPFPAALEDAYAA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012 150 VRWVQENIAAQGGDPQRVYLLGHSAGGSLAASYVGQAQFHGSSGVglAGAIFLSAnIFDPTTSepsaPLKAYFGDDPnry 229
Cdd:COG0657   71 LRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPRP--AAQVLIYP-VLDLTAS----PLRADLAGLP--- 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 893705012 230 tersafpglvqtglPMLIAVSALEpqPFERQALQLQQARCRLDRCASFVRLAGHNHLSTIFSLNTPDQSVGDAILAFIR 308
Cdd:COG0657  141 --------------PTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARAALAEIAAFLR 203
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
76-308 1.81e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 108.81  E-value: 1.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012  76 DVFTPEGpSTTPRPVLIFVhgggfvggdkH----AAGSP-FYDNVMLW-ATQHGMVGVNINHRLAPQNPWPAGTEDVGLA 149
Cdd:COG0657    2 DVYRPAG-AKGPLPVVVYF----------HgggwVSGSKdTHDPLARRlAARAGAAVVSVDYRLAPEHPFPAALEDAYAA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012 150 VRWVQENIAAQGGDPQRVYLLGHSAGGSLAASYVGQAQFHGSSGVglAGAIFLSAnIFDPTTSepsaPLKAYFGDDPnry 229
Cdd:COG0657   71 LRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPRP--AAQVLIYP-VLDLTAS----PLRADLAGLP--- 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 893705012 230 tersafpglvqtglPMLIAVSALEpqPFERQALQLQQARCRLDRCASFVRLAGHNHLSTIFSLNTPDQSVGDAILAFIR 308
Cdd:COG0657  141 --------------PTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARAALAEIAAFLR 203
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 75-180 5.22e-15

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 72.60  E-value: 5.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012   75 LDVFTPEGpSTTPRPVLIFVHGGGFVGGDKHAAgSPFYDNVMLWATQHGMVGVNINHRLAPQNPWPAGTEDVGLAVRWVQ 154
Cdd:pfam20434   1 LDIYLPKN-AKGPYPVVIWIHGGGWNSGDKEAD-MGFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLR 78

                          90       100
                  ....*....|....*....|....*.
gi 893705012  155 ENIAAQGGDPQRVYLLGHSAGGSLAA 180
Cdd:pfam20434  79 ANAAKYGIDTNKIALMGFSAGGHLAL 104
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 75-196 1.66e-14

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 73.91  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012  75 LDVFTPEGPSTT-PRPVLIFVhgggfvggdkH-------AAGSPFYDNVMlwATQHGMVGVNINHRLAP-------QNPW 139
Cdd:cd00312   81 LNVYTPKNTKPGnSLPVMVWI----------HgggfmfgSGSLYPGDGLA--REGDNVIVVSINYRLGVlgflstgDIEL 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893705012 140 P--AGTEDVGLAVRWVQENIAAQGGDPQRVYLLGHSAGGS----LAASYVGQAQFHG---SSGVGL 196
Cdd:cd00312  149 PgnYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGAsvslLLLSPDSKGLFHRaisQSGSAL 214
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
76-308 1.81e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 108.81  E-value: 1.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012  76 DVFTPEGpSTTPRPVLIFVhgggfvggdkH----AAGSP-FYDNVMLW-ATQHGMVGVNINHRLAPQNPWPAGTEDVGLA 149
Cdd:COG0657    2 DVYRPAG-AKGPLPVVVYF----------HgggwVSGSKdTHDPLARRlAARAGAAVVSVDYRLAPEHPFPAALEDAYAA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012 150 VRWVQENIAAQGGDPQRVYLLGHSAGGSLAASYVGQAQFHGSSGVglAGAIFLSAnIFDPTTSepsaPLKAYFGDDPnry 229
Cdd:COG0657   71 LRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPRP--AAQVLIYP-VLDLTAS----PLRADLAGLP--- 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 893705012 230 tersafpglvqtglPMLIAVSALEpqPFERQALQLQQARCRLDRCASFVRLAGHNHLSTIFSLNTPDQSVGDAILAFIR 308
Cdd:COG0657  141 --------------PTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARAALAEIAAFLR 203
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 75-180 5.22e-15

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 72.60  E-value: 5.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012   75 LDVFTPEGpSTTPRPVLIFVHGGGFVGGDKHAAgSPFYDNVMLWATQHGMVGVNINHRLAPQNPWPAGTEDVGLAVRWVQ 154
Cdd:pfam20434   1 LDIYLPKN-AKGPYPVVIWIHGGGWNSGDKEAD-MGFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLR 78

                          90       100
                  ....*....|....*....|....*.
gi 893705012  155 ENIAAQGGDPQRVYLLGHSAGGSLAA 180
Cdd:pfam20434  79 ANAAKYGIDTNKIALMGFSAGGHLAL 104
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 123-226 1.24e-14

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 71.47  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012  123 GMVGVNINHRLAPQNPWPAGTEDVGLAVRWVQENIAAQGGDPQRVYLLGHSAGGSLAASyVGQAqFHGSSGVGLAGAIFL 202
Cdd:pfam07859  29 GAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSAGGNLAAA-VALR-ARDEGLPKPAGQVLI 106

                          90       100
                  ....*....|....*....|....
gi 893705012  203 SANIfDPTTSEPSAPLKAYfGDDP 226
Cdd:pfam07859 107 YPGT-DLRTESPSYLAREF-ADGP 128
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 75-196 1.66e-14

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 73.91  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012  75 LDVFTPEGPSTT-PRPVLIFVhgggfvggdkH-------AAGSPFYDNVMlwATQHGMVGVNINHRLAP-------QNPW 139
Cdd:cd00312   81 LNVYTPKNTKPGnSLPVMVWI----------HgggfmfgSGSLYPGDGLA--REGDNVIVVSINYRLGVlgflstgDIEL 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893705012 140 P--AGTEDVGLAVRWVQENIAAQGGDPQRVYLLGHSAGGS----LAASYVGQAQFHG---SSGVGL 196
Cdd:cd00312  149 PgnYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGAsvslLLLSPDSKGLFHRaisQSGSAL 214
COesterase pfam00135
Carboxylesterase family;
75-209 1.39e-13

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 71.18  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012   75 LDVFTPEG--PSTTPRPVLIFVhgggfvggdkHAAG-----SPFYDNVMLwATQHGMVGVNINHRL------------AP 135
Cdd:pfam00135  88 LNVYTPKElkENKNKLPVMVWI----------HGGGfmfgsGSLYDGSYL-AAEGDVIVVTINYRLgplgflstgddeAP 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 893705012  136 QNpwpAGTEDVGLAVRWVQENIAAQGGDPQRVYLLGHSAGGSLAA----SYVGQAQFHgssgvglaGAIFLSANIFDP 209
Cdd:pfam00135 157 GN---YGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSllllSPLSKGLFH--------RAILMSGSALSP 223
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
75-181 2.83e-13

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 69.92  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012  75 LDVFTPEGPSTTPRPVL--IfvhgggfvggdkH-------AAGSPFYDNVMLwaTQHGMVGVNINHRL------------ 133
Cdd:COG2272   92 LNVWTPALAAGAKLPVMvwI------------HgggfvsgSGSEPLYDGAAL--ARRGVVVVTINYRLgalgflalpals 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 893705012 134 APQNPWPA--GTEDVGLAVRWVQENIAAQGGDPQRVYLLGHSAGG----SLAAS 181
Cdd:COG2272  158 GESYGASGnyGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAasvaALLAS 211
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
105-308 2.76e-09

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.56  E-value: 2.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012 105 HAAGSPFYDNVMLWAtQHGMVGVNINHRLAPQNPWPAGT---EDVGLAVRWVQENiaaQGGDPQRVYLLGHSAGGSLAAS 181
Cdd:COG1506   34 GSRDDSFLPLAQALA-SRGYAVLAPDYRGYGESAGDWGGdevDDVLAAIDYLAAR---PYVDPDRIGIYGHSYGGYMALL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012 182 YVGQA--QFHGssGVGLAGaiFLSANIFDPTTSEPSAPLKAYFGDDPNRYTERSAFPGLVQTGLPMLIAVSALEPQ-PFE 258
Cdd:COG1506  110 AAARHpdRFKA--AVALAG--VSDLRSYYGTTREYTERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRvPPE 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 893705012 259 rQALQLQQARCRLDRCASFVRLAGHNHLSTifslNTPDQSVGDAILAFIR 308
Cdd:COG1506  186 -QAERLYEALKKAGKPVELLVYPGEGHGFS----GAGAPDYLERILDFLD 230
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
144-308 4.99e-05

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 43.84  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012 144 EDVGLAVRWvqenIAAQGGDPqrVYLLGHSAGGSLAASYVGQAqfhgssGVGLAGAIFLS-ANIFDPTTSEPSAPLKAYF 222
Cdd:COG2267   84 DDLRAALDA----LRARPGLP--VVLLGHSMGGLIALLYAARY------PDRVAGLVLLApAYRADPLLGPSARWLRALR 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012 223 gddpnrytersAFPGLVQTGLPMLIAVSALEPQPFERQALQLQQarcRLDRCASFVRLAGHNHLstiFSLNTPDQSVGDA 302
Cdd:COG2267  152 -----------LAEALARIDVPVLVLHGGADRVVPPEAARRLAA---RLSPDVELVLLPGARHE---LLNEPAREEVLAA 214


                 ....*.
gi 893705012 303 ILAFIR 308
Cdd:COG2267  215 ILAWLE 220
COG4099 COG4099
Predicted peptidase [General function prediction only];
133-182 1.30e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.57  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 893705012 133 LAPQNP----WpAGTEDVGLAVRWVQENIAAQGGDPQRVYLLGHSAGG----SLAASY 182
Cdd:COG4099   90 LAPQCPeddyW-SDTKALDAVLALLDDLIAEYRIDPDRIYLTGLSMGGygtwDLAARY 146
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
151-239 4.91e-03

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 37.14  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705012 151 RWVQENIAAQGGDPQRVYLLGHSAGGSLAASYVGQAQfhgssgVGLAGAIFLSAniFDPTTSEPSAPLKAYFGDDPnryT 230
Cdd:COG3545   40 DWLAALDAAVAAADGPVVLVAHSLGCLAVAHWAARLP------RKVAGALLVAP--PDPERPGFLPELDAGFAPIP---R 108


                 ....*....
gi 893705012 231 ERSAFPGLV 239
Cdd:COG3545  109 APLPFPSIV 117
YpfH COG0400
Predicted esterase [General function prediction only];
151-219 7.12e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.19  E-value: 7.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893705012 151 RWVQENIAAQGGDPQRVYLLGHSAGGSLAASYV--GQAQFHGssGVGLAGAIflsanIFDPTTSEPSAPLK 219
Cdd:COG0400   75 AFIDELEARYGIDPERIVLAGFSQGAAMALSLAlrRPELLAG--VVALSGYL-----PGEEALPAPEAALA 138
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
151-224 8.94e-03

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 37.23  E-value: 8.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 893705012 151 RWVQE-----NIAAQGGDpqRVYLLGHSAGGSLAASYvgqAQFHGSsgvgLAGAIFLSANIFDPTTSEPSAPLKAYFGD 224
Cdd:COG1647   67 DWLEDveeayEILKAGYD--KVIVIGLSMGGLLALLL---AARYPD----VAGLVLLSPALKIDDPSAPLLPLLKYLAR 136
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH