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Conserved domains on  [gi|1693972354|gb|TPR78912|]
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alpha/beta hydrolase [Acinetobacter baumannii]

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

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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.
75-277 2.26e-71

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: 219.39  E-value: 2.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354  75 IFHIHGGAFFLGSLKTHHAFMTDLAARTQMQIIHVDYPLAPEHPYPEATEALYDVYQSLLVQ----GIQPKDIILSGDSC 150
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQaaelGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 151 GANLALALCLRLKEQPELMPSGLILLSPFLDLTLTSESLRFNQ-KHDALLSLEALQIGIQHYIGNHiAADDPRVSPIF-D 228
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREfADGPLLTRAAMDWFWRLYLPGA-DRDDPLASPLFaS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1693972354 229 NLEGLPPTLVQVGSKEILLDDAKRFREKAEEAGVKVHFKLYTGMWHNFQ 277
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
 
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.
75-277 2.26e-71

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: 219.39  E-value: 2.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354  75 IFHIHGGAFFLGSLKTHHAFMTDLAARTQMQIIHVDYPLAPEHPYPEATEALYDVYQSLLVQ----GIQPKDIILSGDSC 150
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQaaelGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 151 GANLALALCLRLKEQPELMPSGLILLSPFLDLTLTSESLRFNQ-KHDALLSLEALQIGIQHYIGNHiAADDPRVSPIF-D 228
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREfADGPLLTRAAMDWFWRLYLPGA-DRDDPLASPLFaS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1693972354 229 NLEGLPPTLVQVGSKEILLDDAKRFREKAEEAGVKVHFKLYTGMWHNFQ 277
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
74-300 7.03e-58

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 184.69  E-value: 7.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354  74 LIFHIHGGAFFLGSLKTHHAFMTDLAARTQMQIIHVDYPLAPEHPYPEATEALYDVYQSLLVQ----GIQPKDIILSGDS 149
Cdd:COG0657    15 VVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANaaelGIDPDRIAVAGDS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 150 CGANLALALCLRLKEQPELMPSGLILLSPFLDLTltseslrfnqkhdallslealqigiqhyignhiaaddprVSPIFDN 229
Cdd:COG0657    95 AGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT---------------------------------------ASPLRAD 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693972354 230 LEGLPPTLVQVGSKEILLDDAKRFREKAEEAGVKVHFKLYTGMWHNFQMFnAWFEEAKQAMADIAEFAHEL 300
Cdd:COG0657   136 LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLL-AGLPEARAALAEIAAFLRRA 205
PRK10162 PRK10162
acetyl esterase;
68-296 6.88e-27

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 107.11  E-value: 6.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354  68 QDSATQLIFHIHGGAFFLGSLKTHHAFMTDLAARTQMQIIHVDYPLAPEHPYPEATEALYDVYQSLLVQ----GIQPKDI 143
Cdd:PRK10162   77 QPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHaedyGINMSRI 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 144 ILSGDSCGANLALALCLRLKEQPELMPS--GLILLSPFLDLTlTSESLRFNQKHDALLSLEALQIGIQHYIGNhiAADdp 221
Cdd:PRK10162  157 GFAGDSAGAMLALASALWLRDKQIDCGKvaGVLLWYGLYGLR-DSVSRRLLGGVWDGLTQQDLQMYEEAYLSN--DAD-- 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 222 RVSP---IFDN--LEGLPPTLVQVGSKEILLDDAKRFREKAEEAGVKVHFKLYTGMWHNFQMFNAWFEEAKQAMADIAEF 296
Cdd:PRK10162  232 RESPyycLFNNdlTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMDTADDALRDGAQF 311
 
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.
75-277 2.26e-71

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: 219.39  E-value: 2.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354  75 IFHIHGGAFFLGSLKTHHAFMTDLAARTQMQIIHVDYPLAPEHPYPEATEALYDVYQSLLVQ----GIQPKDIILSGDSC 150
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQaaelGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 151 GANLALALCLRLKEQPELMPSGLILLSPFLDLTLTSESLRFNQ-KHDALLSLEALQIGIQHYIGNHiAADDPRVSPIF-D 228
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREfADGPLLTRAAMDWFWRLYLPGA-DRDDPLASPLFaS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1693972354 229 NLEGLPPTLVQVGSKEILLDDAKRFREKAEEAGVKVHFKLYTGMWHNFQ 277
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
74-300 7.03e-58

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 184.69  E-value: 7.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354  74 LIFHIHGGAFFLGSLKTHHAFMTDLAARTQMQIIHVDYPLAPEHPYPEATEALYDVYQSLLVQ----GIQPKDIILSGDS 149
Cdd:COG0657    15 VVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANaaelGIDPDRIAVAGDS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 150 CGANLALALCLRLKEQPELMPSGLILLSPFLDLTltseslrfnqkhdallslealqigiqhyignhiaaddprVSPIFDN 229
Cdd:COG0657    95 AGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT---------------------------------------ASPLRAD 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693972354 230 LEGLPPTLVQVGSKEILLDDAKRFREKAEEAGVKVHFKLYTGMWHNFQMFnAWFEEAKQAMADIAEFAHEL 300
Cdd:COG0657   136 LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLL-AGLPEARAALAEIAAFLRRA 205
PRK10162 PRK10162
acetyl esterase;
68-296 6.88e-27

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 107.11  E-value: 6.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354  68 QDSATQLIFHIHGGAFFLGSLKTHHAFMTDLAARTQMQIIHVDYPLAPEHPYPEATEALYDVYQSLLVQ----GIQPKDI 143
Cdd:PRK10162   77 QPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHaedyGINMSRI 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 144 ILSGDSCGANLALALCLRLKEQPELMPS--GLILLSPFLDLTlTSESLRFNQKHDALLSLEALQIGIQHYIGNhiAADdp 221
Cdd:PRK10162  157 GFAGDSAGAMLALASALWLRDKQIDCGKvaGVLLWYGLYGLR-DSVSRRLLGGVWDGLTQQDLQMYEEAYLSN--DAD-- 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 222 RVSP---IFDN--LEGLPPTLVQVGSKEILLDDAKRFREKAEEAGVKVHFKLYTGMWHNFQMFNAWFEEAKQAMADIAEF 296
Cdd:PRK10162  232 RESPyycLFNNdlTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMDTADDALRDGAQF 311
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
66-156 2.95e-07

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: 50.26  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354  66 KAQDSATQLIFHIHGGAFFLGSLKTHHAFMTDLAAR---TQMQIIHVDYPLAPEHPYPeatEALYDVYQSL--LVQ---- 136
Cdd:pfam20434   7 KNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKAllkAGYAVASINYRLSTDAKFP---AQIQDVKAAIrfLRAnaak 83
                          90       100
                  ....*....|....*....|.
gi 1693972354 137 -GIQPKDIILSGDSCGANLAL 156
Cdd:pfam20434  84 yGIDTNKIALMGFSAGGHLAL 104
YpfH COG0400
Predicted esterase [General function prediction only];
121-286 6.85e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 6.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 121 EATEALYDVYQSLLVQ-GIQPKDIILSGDSCGANLALALCLRLKEQpelmPSGLILLSPFLdltltsesLRFNQKHDALL 199
Cdd:COG0400    68 AAAEALAAFIDELEARyGIDPERIVLAGFSQGAAMALSLALRRPEL----LAGVVALSGYL--------PGEEALPAPEA 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972354 200 SLEALQIGIQHyignhiAADDPRVSPifdnleglpptlvqvgskeillDDAKRFREKAEEAGVKVHFKLYTgMWH----- 274
Cdd:COG0400   136 ALAGTPVFLAH------GTQDPVIPV----------------------ERAREAAEALEAAGADVTYREYP-GGHeispe 186
                         170
                  ....*....|..
gi 1693972354 275 NFQMFNAWFEEA 286
Cdd:COG0400   187 ELADARAWLAER 198
 
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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