NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499867825|ref|WP_011548559|]
View 

MULTISPECIES: alpha/beta hydrolase [Burkholderia]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
86-293 9.80e-85

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: 254.06  E-value: 9.80e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825   86 FMFFHGGGWILGDYPTHERLVRDLVVQSGSAAVFVEYTPSPEARYPVAINEAYAATKWVAAHGAEIGVDGARLAVVGNSV 165
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825  166 GGNMAAVVSQMAKDRQGPAIRFQGLMWPVADHAFDNASYDA--FANGYFLSRDMMKWFWNAYTIDEGeRNERYASPLRAS 243
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAreFADGPLLTRAAMDWFWRLYLPGAD-RDDPLASPLFAS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 499867825  244 ldELKGLPPALIQTAQFDVLRDEGEAYGYRLDQAGNDVTTIQYKGTIHDF 293
Cdd:pfam07859 160 --DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
86-293 9.80e-85

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: 254.06  E-value: 9.80e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825   86 FMFFHGGGWILGDYPTHERLVRDLVVQSGSAAVFVEYTPSPEARYPVAINEAYAATKWVAAHGAEIGVDGARLAVVGNSV 165
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825  166 GGNMAAVVSQMAKDRQGPAIRFQGLMWPVADHAFDNASYDA--FANGYFLSRDMMKWFWNAYTIDEGeRNERYASPLRAS 243
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAreFADGPLLTRAAMDWFWRLYLPGAD-RDDPLASPLFAS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 499867825  244 ldELKGLPPALIQTAQFDVLRDEGEAYGYRLDQAGNDVTTIQYKGTIHDF 293
Cdd:pfam07859 160 --DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
73-320 5.22e-65

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 203.57  E-value: 5.22e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825  73 VVKPQDSRGVLPVFMFFHGGGWILGDYPTHERLVRDLVVQSGSAAVFVEYTPSPEARYPVAINEAYAATKWVAAHGAEIG 152
Cdd:COG0657    3 VYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825 153 VDGARLAVVGNSVGGNMAAVVSQMAKDRQGPAIRFQGLMWPVADHAfdnasydafangyflsrdmmkwfwnaytideger 232
Cdd:COG0657   83 IDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT---------------------------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825 233 neryASPLRASldeLKGLPPALIQTAQFDVLRDEGEAYGYRLDQAGNDVTTIQYKGTIHDFGLLNVLaadAPTRAAMQQM 312
Cdd:COG0657  129 ----ASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGL---PEARAALAEI 198

                 ....*...
gi 499867825 313 ATALKTHL 320
Cdd:COG0657  199 AAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
85-293 1.11e-31

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 120.59  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825  85 VFMFFHGGGWILGDYPTHERLVRDLVVQSGSAAVFVEYTPSPEARYPVAINEAYAATKWVAAHGAEIGVDGARLAVVGNS 164
Cdd:PRK10162  83 TLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGDS 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825 165 VGGNMAAVVSQMAKDRQGPAIRFQG-LMWPVADHAFDNASYDAFANGY-FLSRDMMKWFWNAYTIDEGERNERYASPLRA 242
Cdd:PRK10162 163 AGAMLALASALWLRDKQIDCGKVAGvLLWYGLYGLRDSVSRRLLGGVWdGLTQQDLQMYEEAYLSNDADRESPYYCLFNN 242
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499867825 243 SLDelKGLPPALIQTAQFDVLRDEGEAYGYRLDQAGNDVTTIQYKGTIHDF 293
Cdd:PRK10162 243 DLT--RDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAF 291
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
86-293 9.80e-85

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: 254.06  E-value: 9.80e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825   86 FMFFHGGGWILGDYPTHERLVRDLVVQSGSAAVFVEYTPSPEARYPVAINEAYAATKWVAAHGAEIGVDGARLAVVGNSV 165
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825  166 GGNMAAVVSQMAKDRQGPAIRFQGLMWPVADHAFDNASYDA--FANGYFLSRDMMKWFWNAYTIDEGeRNERYASPLRAS 243
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAreFADGPLLTRAAMDWFWRLYLPGAD-RDDPLASPLFAS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 499867825  244 ldELKGLPPALIQTAQFDVLRDEGEAYGYRLDQAGNDVTTIQYKGTIHDF 293
Cdd:pfam07859 160 --DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
73-320 5.22e-65

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 203.57  E-value: 5.22e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825  73 VVKPQDSRGVLPVFMFFHGGGWILGDYPTHERLVRDLVVQSGSAAVFVEYTPSPEARYPVAINEAYAATKWVAAHGAEIG 152
Cdd:COG0657    3 VYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825 153 VDGARLAVVGNSVGGNMAAVVSQMAKDRQGPAIRFQGLMWPVADHAfdnasydafangyflsrdmmkwfwnaytideger 232
Cdd:COG0657   83 IDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT---------------------------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825 233 neryASPLRASldeLKGLPPALIQTAQFDVLRDEGEAYGYRLDQAGNDVTTIQYKGTIHDFGLLNVLaadAPTRAAMQQM 312
Cdd:COG0657  129 ----ASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGL---PEARAALAEI 198

                 ....*...
gi 499867825 313 ATALKTHL 320
Cdd:COG0657  199 AAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
85-293 1.11e-31

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 120.59  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825  85 VFMFFHGGGWILGDYPTHERLVRDLVVQSGSAAVFVEYTPSPEARYPVAINEAYAATKWVAAHGAEIGVDGARLAVVGNS 164
Cdd:PRK10162  83 TLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGDS 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825 165 VGGNMAAVVSQMAKDRQGPAIRFQG-LMWPVADHAFDNASYDAFANGY-FLSRDMMKWFWNAYTIDEGERNERYASPLRA 242
Cdd:PRK10162 163 AGAMLALASALWLRDKQIDCGKVAGvLLWYGLYGLRDSVSRRLLGGVWdGLTQQDLQMYEEAYLSNDADRESPYYCLFNN 242
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499867825 243 SLDelKGLPPALIQTAQFDVLRDEGEAYGYRLDQAGNDVTTIQYKGTIHDF 293
Cdd:PRK10162 243 DLT--RDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAF 291
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
75-171 6.06e-13

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: 66.82  E-value: 6.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825   75 KPQDSRGVLPVFMFFHGGGWILGD--------YPTHERLvrdlvVQSGSAAVFVEYTPSPEARYPVAINEAYAATKWVAA 146
Cdd:pfam20434   5 LPKNAKGPYPVVIWIHGGGWNSGDkeadmgfmTNTVKAL-----LKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRA 79
                          90       100
                  ....*....|....*....|....*
gi 499867825  147 HGAEIGVDGARLAVVGNSVGGNMAA 171
Cdd:pfam20434  80 NAAKYGIDTNKIALMGFSAGGHLAL 104
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
65-321 2.28e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.87  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825  65 DGLVVSLVVVKPQDSRGvLPVFMFFHGGGWilGDYPTHERLVRDLVvQSGSAAVFVEYT---PSPEARYPVAINEAYAAT 141
Cdd:COG1506    6 DGTTLPGWLYLPADGKK-YPVVVYVHGGPG--SRDDSFLPLAQALA-SRGYAVLAPDYRgygESAGDWGGDEVDDVLAAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825 142 KWVAAHGaeiGVDGARLAVVGNSVGGNMAAVVsqMAKDRQgpaiRFQGLmwpVADHAF-DNASYDAFAngyflsrdmmKW 220
Cdd:COG1506   82 DYLAARP---YVDPDRIGIYGHSYGGYMALLA--AARHPD----RFKAA---VALAGVsDLRSYYGTT----------RE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499867825 221 FWNAYTIDEGERNERYA--SPLRAsLDELKGlpPALIQTAQFD--VLRDEGEAYGYRLDQAGNDVTTIQYKGTIHDFgll 296
Cdd:COG1506  140 YTERLMGGPWEDPEAYAarSPLAY-ADKLKT--PLLLIHGEADdrVPPEQAERLYEALKKAGKPVELLVYPGEGHGF--- 213
                        250       260
                 ....*....|....*....|....*
gi 499867825 297 nvlaADAPTRAAMQQMATALKTHLQ 321
Cdd:COG1506  214 ----SGAGAPDYLERILDFLDRHLK 234
 
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