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Conserved domains on  [gi|1620919188|gb|THD79949|]
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MAG: alpha/beta hydrolase [Phenylobacterium sp.]

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

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List of domain hits

 Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
63-302 3.47e-44

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 150.02  E-value: 3.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188  63 MTVYAPKGRNTGVAVVVF-PGGGYQVLAMDlEGTEICDWLTS-RGVTCVLLKYRvpnsgptLVDGHRYypkvQTALQDAQ 140
Cdd:COG0657     1 MDVYRPAGAKGPLPVVVYfHGGGWVSGSKD-THDPLARRLAArAGAAVVSVDYR-------LAPEHPF----PAALEDAY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 141 RTLGLVRQHAAQWHVDPHKVGVIGFSAGGHLVAAVSTHfahrtyqpvdAADALSCRPDFAIAVYPGHlwahedeghatrk 220
Cdd:COG0657    69 AALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALR----------ARDRGGPRPAAQVLIYPVL------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 221 eeDLSLRPDIRVRADTPPTFLLQAENDEVdgVQQSLAYYVALHKAGVPTEMHLYAKGGHAFGLRAGKLPIGRWPDLVEQW 300
Cdd:COG0657   126 --DLTASPLRADLAGLPPTLIVTGEADPL--VDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARAALAEIAAF 201


                  ..
gi 1620919188 301 LR 302
Cdd:COG0657   202 LR 203
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
63-302 3.47e-44

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 150.02  E-value: 3.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188  63 MTVYAPKGRNTGVAVVVF-PGGGYQVLAMDlEGTEICDWLTS-RGVTCVLLKYRvpnsgptLVDGHRYypkvQTALQDAQ 140
Cdd:COG0657     1 MDVYRPAGAKGPLPVVVYfHGGGWVSGSKD-THDPLARRLAArAGAAVVSVDYR-------LAPEHPF----PAALEDAY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 141 RTLGLVRQHAAQWHVDPHKVGVIGFSAGGHLVAAVSTHfahrtyqpvdAADALSCRPDFAIAVYPGHlwahedeghatrk 220
Cdd:COG0657    69 AALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALR----------ARDRGGPRPAAQVLIYPVL------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 221 eeDLSLRPDIRVRADTPPTFLLQAENDEVdgVQQSLAYYVALHKAGVPTEMHLYAKGGHAFGLRAGKLPIGRWPDLVEQW 300
Cdd:COG0657   126 --DLTASPLRADLAGLPPTLIVTGEADPL--VDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARAALAEIAAF 201


                  ..
gi 1620919188 301 LR 302
Cdd:COG0657   202 LR 203
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 126-281 1.22e-12

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: 65.70  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 126 HRYypkvQTALQDAQRTLGLVRQHAAQWHVDPHKVGVIGFSAGGHLVAAVsthfAHRtyqpvdAADALSCRPDFAIAVYP 205
Cdd:pfam07859  43 HPF----PAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSAGGNLAAAV----ALR------ARDEGLPKPAGQVLIYP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 206 GHLWAHEDEGHATRKEEDLSLRPDIRVR-------------------------ADTPPTFLLQAEND-EVDgvqQSLAYY 259
Cdd:pfam07859 109 GTDLRTESPSYLAREFADGPLLTRAAMDwfwrlylpgadrddplasplfasdlSGLPPALVVVAEFDpLRD---EGEAYA 185

                         170       180
                  ....*....|....*....|..
gi 1620919188 260 VALHKAGVPTEMHLYAKGGHAF 281
Cdd:pfam07859 186 ERLRAAGVPVELIEYPGMPHGF 207
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
63-302 3.47e-44

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 150.02  E-value: 3.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188  63 MTVYAPKGRNTGVAVVVF-PGGGYQVLAMDlEGTEICDWLTS-RGVTCVLLKYRvpnsgptLVDGHRYypkvQTALQDAQ 140
Cdd:COG0657     1 MDVYRPAGAKGPLPVVVYfHGGGWVSGSKD-THDPLARRLAArAGAAVVSVDYR-------LAPEHPF----PAALEDAY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 141 RTLGLVRQHAAQWHVDPHKVGVIGFSAGGHLVAAVSTHfahrtyqpvdAADALSCRPDFAIAVYPGHlwahedeghatrk 220
Cdd:COG0657    69 AALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALR----------ARDRGGPRPAAQVLIYPVL------------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 221 eeDLSLRPDIRVRADTPPTFLLQAENDEVdgVQQSLAYYVALHKAGVPTEMHLYAKGGHAFGLRAGKLPIGRWPDLVEQW 300
Cdd:COG0657   126 --DLTASPLRADLAGLPPTLIVTGEADPL--VDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARAALAEIAAF 201


                  ..
gi 1620919188 301 LR 302
Cdd:COG0657   202 LR 203
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
64-302 1.54e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 74.28  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188  64 TVYAPKGrNTGVAVVVFPGGGYQvlAMDLEGTEICDWLTSRGVTCVLLKYRvpNSGPTLVDGHRYypkvqtALQDAQRTL 143
Cdd:COG1506    13 WLYLPAD-GKKYPVVVYVHGGPG--SRDDSFLPLAQALASRGYAVLAPDYR--GYGESAGDWGGD------EVDDVLAAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 144 GLVRQHAaqwHVDPHKVGVIGFSAGGHLVAAVSTHFAHRtyqpVDAADALSCRPDFAIAVYPGHLWAHEDEGHATRKEED 223
Cdd:COG1506    82 DYLAARP---YVDPDRIGIYGHSYGGYMALLAAARHPDR----FKAAVALAGVSDLRSYYGTTREYTERLMGGPWEDPEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 224 L-SLRPDIRVRADTPPTFLLQAENDEVDGVQQSLAYYVALHKAGVPTEMHLYAKGGHAFglraGKLPIGRWPDLVEQWLR 302
Cdd:COG1506   155 YaARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGF----SGAGAPDYLERILDFLD 230
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
64-281 5.43e-13

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 66.91  E-value: 5.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188  64 TVYAPKGRNTGVAVVVFPGGGyqvlAMDLEGTEICDWLTSRGVTCV---LLKYRVPNSGPTLVDGHRYYPKVQTALQDAQ 140
Cdd:COG0412    19 YLARPAGGGPRPGVVVLHEIF----GLNPHIRDVARRLAAAGYVVLapdLYGRGGPGDDPDEARALMGALDPELLAADLR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 141 RTLGLVRQHAAqwhVDPHKVGVIGFSAGGHLVAAVSTHFAhrtyqPVDAAdalscrpdfaIAVYPGHLWAHEDEghatrk 220
Cdd:COG0412    95 AALDWLKAQPE---VDAGRVGVVGFCFGGGLALLAAARGP-----DLAAA----------VSFYGGLPADDLLD------ 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1620919188 221 eedlsLRPDIRVradtpPTFLLQAENDEVDGVQQSLAYYVALHKAGVPTEMHLYAKGGHAF 281
Cdd:COG0412   151 -----LAARIKA-----PVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGHGF 201
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 126-281 1.22e-12

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: 65.70  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 126 HRYypkvQTALQDAQRTLGLVRQHAAQWHVDPHKVGVIGFSAGGHLVAAVsthfAHRtyqpvdAADALSCRPDFAIAVYP 205
Cdd:pfam07859  43 HPF----PAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSAGGNLAAAV----ALR------ARDEGLPKPAGQVLIYP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 206 GHLWAHEDEGHATRKEEDLSLRPDIRVR-------------------------ADTPPTFLLQAEND-EVDgvqQSLAYY 259
Cdd:pfam07859 109 GTDLRTESPSYLAREFADGPLLTRAAMDwfwrlylpgadrddplasplfasdlSGLPPALVVVAEFDpLRD---EGEAYA 185

                         170       180
                  ....*....|....*....|..
gi 1620919188 260 VALHKAGVPTEMHLYAKGGHAF 281
Cdd:pfam07859 186 ERLRAAGVPVELIEYPGMPHGF 207
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 135-262 2.75e-12

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: 64.89  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 135 ALQDAQRTLGLVRQHAAQWHVDPHKVGVIGFSAGGHL--VAAVSTH--------FAHRT---------------YQPVDA 189
Cdd:pfam20434  66 QIQDVKAAIRFLRANAAKYGIDTNKIALMGFSAGGHLalLAGLSNNnkefegnvGDYTPesskesfkvnavvdfYGPTDL 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1620919188 190 ADALSCRPDFAiAVYPGHLWAhedeGHATRKEEDL--SLRPDIRVRADTPPTFLLQAENDEVDGVQQSLAYYVAL 262
Cdd:pfam20434 146 LDMDSCGTHND-AKSPETLLL----GAPPLENPDLakSASPITYVDKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
150-282 1.35e-09

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 57.24  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 150 AAQWHVDPHKVGVIGFSAGGHLVAAVSTHfahrtyqpvdaadalscRPDF---AIAVYP-----------GHLWAHEDEG 215
Cdd:pfam00326  56 IEQGYTDPDRLAIWGGSYGGYLTGAALNQ-----------------RPDLfkaAVAHVPvvdwlaymsdtSLPFTERYME 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1620919188 216 HAT-RKEEDL-----SLRPDIRVRAdTPPTFLLQAENDEVDGVQQSLAYYVALHKAGVPTEMHLYAKGGHAFG 282
Cdd:pfam00326 119 WGNpWDNEEGydylsPYSPADNVKV-YPPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLLIFPDEGHGIG 190
DLH pfam01738
Dienelactone hydrolase family;
95-309 3.30e-05

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 44.26  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188  95 TEICDWLTSRG--VTCVLLKYRVPNSGPTLVDGHRYYPKVQTALQDA--QRTLGLVRQHAAQWHVDPHKVGVIGFSAGGH 170
Cdd:pfam01738  29 REIADRLADEGyvALAPDLYFRQGDPNDEADAARAMFELVSKRVMEKvlDDLEAAVNYLKSQPEVSPKKVGVVGYCMGGA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 171 LVAAVSTHFAhrtyqPVDAAdalscrpdfaiAVYpghlwahedegHATRKEEDLSLRPDIRVradtpPTFLLQAEND--- 247
Cdd:pfam01738 109 LAVLLAAKGP-----LVDAA-----------VGF-----------YGVGPEPPLIEAPDIKA-----PILFHFGEEDhfv 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1620919188 248 ---EVDGVQQslayyvALHKAGVPTEMHLYAKGGHAFglrAGKLPIGRWPDLVEQ-WLRTIGMLGP 309
Cdd:pfam01738 157 padSRELIEE------ALKAANVDHQIHSYPGAGHAF---ANDSRPSYNAAAAEDaWERTLEFFKQ 213
YpfH COG0400
Predicted esterase [General function prediction only];
137-280 1.18e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 42.20  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 137 QDAQRTLGLVRQHAAQWHVDPHKVGVIGFSAGghlvAAVSTHFAHRTYQPVDAADALSCRpdfaiavYPGHLWAHEDEGH 216
Cdd:COG0400    68 AAAEALAAFIDELEARYGIDPERIVLAGFSQG----AAMALSLALRRPELLAGVVALSGY-------LPGEEALPAPEAA 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1620919188 217 ATRkeedlslrpdirvradtPPTFLLQAENDEVDGVQQSLAYYVALHKAGVPTEMHLYAkGGHA 280
Cdd:COG0400   137 LAG-----------------TPVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREYP-GGHE 182
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
63-281 3.46e-03

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 38.06  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188  63 MTVYAPKGRNTGVaVVVFPGGGYQVLAMDlegtEICDWLTSRGVTCVLLKYRvpnsgptlvdGH-------RYYPKVQTA 135
Cdd:COG2267    18 GRRWRPAGSPRGT-VVLVHGLGEHSGRYA----ELAEALAAAGYAVLAFDLR----------GHgrsdgprGHVDSFDDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919188 136 LQDAQRTLGLVRQHAAQwhvdphKVGVIGFSAGGHLVAavstHFAHRTYQPVDAadalscrpdfAIAVYPGHLWaHEDEG 215
Cdd:COG2267    83 VDDLRAALDALRARPGL------PVVLLGHSMGGLIAL----LYAARYPDRVAG----------LVLLAPAYRA-DPLLG 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1620919188 216 HATRKEEDLSLRPDIrvRADTPPTFLLQAENDEVDGVQQSLAYYVALHKAgvpTEMHLYAKGGHAF 281
Cdd:COG2267   142 PSARWLRALRLAEAL--ARIDVPVLVLHGGADRVVPPEAARRLAARLSPD---VELVLLPGARHEL 202
 
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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