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Conserved domains on  [gi|1278332014|gb|PIY75358|]
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alpha/beta hydrolase [Rhodobacterales bacterium CG_4_10_14_0_8_um_filter_70_9]

Protein Classification

dienelactone hydrolase family protein( domain architecture ID 10785456)

dienelactone hydrolase family protein plays a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917
SCOP:  3000102

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
6-173 3.60e-16

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


:

Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 77.31  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014   6 ELRVETAAVGATPVTITRPASEAPAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGH-GRNPGPMTGDVTTEDG 84
Cdd:COG0412     5 TVTIPTPDGVTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRgGPGDDPDEARALMGAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  85 ATAALVAELGRVADFARALPGVD-GRLAVLGHSMAGDVIARYALATPAVAATVGvsmFSPVVDADQPRN--------LLM 155
Cdd:COG0412    85 DPELLAADLRAALDWLKAQPEVDaGRVGVVGFCFGGGLALLAAARGPDLAAAVS---FYGGLPADDLLDlaarikapVLL 161
                         170
                  ....*....|....*...
gi 1278332014 156 IVGAWEAGLTDEAVRVLR 173
Cdd:COG0412   162 LYGEKDPLVPPEQVAALE 179
 
Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
6-173 3.60e-16

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 77.31  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014   6 ELRVETAAVGATPVTITRPASEAPAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGH-GRNPGPMTGDVTTEDG 84
Cdd:COG0412     5 TVTIPTPDGVTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRgGPGDDPDEARALMGAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  85 ATAALVAELGRVADFARALPGVD-GRLAVLGHSMAGDVIARYALATPAVAATVGvsmFSPVVDADQPRN--------LLM 155
Cdd:COG0412    85 DPELLAADLRAALDWLKAQPEVDaGRVGVVGFCFGGGLALLAAARGPDLAAAVS---FYGGLPADDLLDlaarikapVLL 161
                         170
                  ....*....|....*...
gi 1278332014 156 IVGAWEAGLTDEAVRVLR 173
Cdd:COG0412   162 LYGEKDPLVPPEQVAALE 179
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
31-149 4.60e-08

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 54.05  E-value: 4.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  31 PAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGHGRNPGPMTGDvtteDGATAALVAELgrvaDFARALPGVDgRL 110
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQD----DYRTDDLAEDL----EYILEALGLE-KV 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1278332014 111 AVLGHSMAGDVIARYALATP-AVAATVGVSMFSPVVDADQ 149
Cdd:pfam00561  72 NLVGHSMGGLIALAYAAKYPdRVKALVLLGALDPPHELDE 111
 
Name Accession Description Interval E-value
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
6-173 3.60e-16

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 77.31  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014   6 ELRVETAAVGATPVTITRPASEAPAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGH-GRNPGPMTGDVTTEDG 84
Cdd:COG0412     5 TVTIPTPDGVTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRgGPGDDPDEARALMGAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  85 ATAALVAELGRVADFARALPGVD-GRLAVLGHSMAGDVIARYALATPAVAATVGvsmFSPVVDADQPRN--------LLM 155
Cdd:COG0412    85 DPELLAADLRAALDWLKAQPEVDaGRVGVVGFCFGGGLALLAAARGPDLAAAVS---FYGGLPADDLLDlaarikapVLL 161
                         170
                  ....*....|....*...
gi 1278332014 156 IVGAWEAGLTDEAVRVLR 173
Cdd:COG0412   162 LYGEKDPLVPPEQVAALE 179
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
24-147 1.32e-15

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 76.49  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  24 PASEAPAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGHGRNPG-P-MTGDVTTEDGATAalvaelgrvADFAR 101
Cdd:COG1073    31 AGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGePrEEGSPERRDARAA---------VDYLR 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1278332014 102 ALPGVD-GRLAVLGHSMAGDVIARYALATPAVAATVGVSMFSPVVDA 147
Cdd:COG1073   102 TLPGVDpERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDL 148
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
18-162 4.88e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 74.28  E-value: 4.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  18 PVTITRPASEAPAPAVVIAHGFSGSR-PLMRAFSATLARNGYVAVSFDFLGHGRNPGPMTGDvttedgataaLVAELGRV 96
Cdd:COG1506    11 PGWLYLPADGKKYPVVVYVHGGPGSRdDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGD----------EVDDVLAA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278332014  97 ADFARALPGVDG-RLAVLGHSMAGDVIARYALATP----AVAATVGVSMFSPVVDADQPRNLLMIVGAWEA 162
Cdd:COG1506    81 IDYLAARPYVDPdRIGIYGHSYGGYMALLAAARHPdrfkAAVALAGVSDLRSYYGTTREYTERLMGGPWED 151
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
24-148 2.04e-13

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 69.26  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  24 PASEAPAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGHGRNPGPMTGDVTTEDgataaLVAELGRVADFARAL 103
Cdd:COG2267    22 RPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDD-----YVDDLRAALDALRAR 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1278332014 104 PGvdGRLAVLGHSMAGDVIARYALATPAVAAtvGVSMFSPVVDAD 148
Cdd:COG2267    97 PG--LPVVLLGHSMGGLIALLYAARYPDRVA--GLVLLAPAYRAD 137
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
27-160 2.41e-10

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 60.73  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  27 EAPAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGHGRNPGPMTGdVTTEDGATAALVAelgrvadFARALPGV 106
Cdd:COG1647    12 EGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLK-TTWEDWLEDVEEA-------YEILKAGY 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1278332014 107 DgRLAVLGHSMAGDVIARYALATPAVAATVgvsMFSPVVDADQPRNLLMIVGAW 160
Cdd:COG1647    84 D-KVIVIGLSMGGLLALLLAARYPDVAGLV---LLSPALKIDDPSAPLLPLLKY 133
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
31-149 4.60e-08

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 54.05  E-value: 4.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  31 PAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGHGRNPGPMTGDvtteDGATAALVAELgrvaDFARALPGVDgRL 110
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQD----DYRTDDLAEDL----EYILEALGLE-KV 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1278332014 111 AVLGHSMAGDVIARYALATP-AVAATVGVSMFSPVVDADQ 149
Cdd:pfam00561  72 NLVGHSMGGLIALAYAAKYPdRVKALVLLGALDPPHELDE 111
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
24-146 1.84e-07

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 52.84  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  24 PASEAPAPAVVIAHGFSGS--RPLMRAFSATLARNGYVAVSFDFLGHG----RNPGPMTgdvtteDGATaalvAELGRVA 97
Cdd:COG0429    55 DPPAPSKPLVVLLHGLEGSsdSHYARGLARALYARGWDVVRLNFRGCGgepnLLPRLYH------SGDT----EDLVWVL 124
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1278332014  98 DFARALPGvDGRLAVLGHSMAGDVIARYALATPAVAATV-GVSMFSPVVD 146
Cdd:COG0429   125 AHLRARYP-YAPLYAVGFSLGGNLLLKYLGEQGDDAPPLkAAVAVSPPLD 173
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
22-119 1.87e-07

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 52.89  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  22 TRPASEAPAPAVVIAHGFSGSRPLMRAfSATLARNGYVAVSFDFLGHGRNPGPmTGDVTTEDGATAA------------- 88
Cdd:COG3458    74 LRPKGEGPLPAVVEFHGYGGGRGLPHE-DLDWAAAGYAVLVMDTRGQGSSWGD-TPDPGGYSGGALPgymtrgiddpdty 151
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1278332014  89 ----LVAELGRVADFARALPGVDG-RLAVLGHSMAG 119
Cdd:COG3458   152 yyrrVYLDAVRAVDALRSLPEVDGkRIGVTGGSQGG 187
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
28-131 9.33e-07

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 49.91  E-value: 9.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  28 APAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGHGRNPGPmTGDVTTEDgataALVAELGRVADFARAlPGVD 107
Cdd:pfam12146   2 EPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGK-RGHVPSFD----DYVDDLDTFVDKIRE-EHPG 75
                          90       100
                  ....*....|....*....|....
gi 1278332014 108 GRLAVLGHSMAGDVIARYALATPA 131
Cdd:pfam12146  76 LPLFLLGHSMGGLIAALYALRYPD 99
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
26-143 1.01e-06

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 47.13  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  26 SEAPAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFlghgrnpGPMTGDVttedgatAALVAELGRVADFARALPG 105
Cdd:COG1075     1 YAATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYALNY-------PSTNGSI-------EDSAEQLAAFVDAVLAATG 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1278332014 106 VDgRLAVLGHSMAGdVIARYALATPAVAATVG--VSMFSP 143
Cdd:COG1075    67 AE-KVDLVGHSMGG-LVARYYLKRLGGAAKVArvVTLGTP 104
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
18-119 1.05e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 47.41  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  18 PVTITRPA-------SEAPAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGHGRNPGPMTGDVTTEDGATAALV 90
Cdd:COG4188    43 PVDVWYPAtapadapAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNAADLSAALDGLADALDPEELW 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1278332014  91 AelgRVADFARAL----------PGVDGRL-----AVLGHSMAG 119
Cdd:COG4188   123 E---RPLDLSFVLdqllalnksdPPLAGRLdldriGVIGHSLGG 163
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
30-131 1.31e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 46.15  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  30 APAVVIAHGFSGSRPLMRAFSATLARnGYVAVSFDFLGHGRNPGPmTGDVTTED--GATAALVAELGrvadfaralpgvD 107
Cdd:COG0596    23 GPPVVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKP-AGGYTLDDlaDDLAALLDALG------------L 88
                          90       100
                  ....*....|....*....|....
gi 1278332014 108 GRLAVLGHSMAGDVIARYALATPA 131
Cdd:COG0596    89 ERVVLVGHSMGGMVALELAARHPE 112
DLH pfam01738
Dienelactone hydrolase family;
28-149 3.77e-05

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 44.65  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  28 APAPAVVIAHGFSGSRPLMRAFSATLARNGYVAVSFDFLGHGRNPG-----PMTGDVTTEDGATAALVAELGRVADFARA 102
Cdd:pfam01738  10 PPWPVVVVFQEIFGVNDNIREIADRLADEGYVALAPDLYFRQGDPNdeadaARAMFELVSKRVMEKVLDDLEAAVNYLKS 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1278332014 103 LPGVD-GRLAVLGHSMAGDVIARYALATPAVAATV---GVSMFSPVVDADQ 149
Cdd:pfam01738  90 QPEVSpKKVGVVGYCMGGALAVLLAAKGPLVDAAVgfyGVGPEPPLIEAPD 140
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
27-136 1.06e-03

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


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 40.25  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278332014  27 EAPAPAVVIAHGFSGSR--PLMRAFSATLARNGYVAVSFDF---LGHGRNPGPMtgdvttedgatAALVAELGRVADFAR 101
Cdd:COG3571     6 EDPRATLLLAHGAGAGMdsPFMVALAEALAAAGIAVARFEFpymVAGRRPPDRA-----------PVLDAAWRAVIAALR 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1278332014 102 ALPgVDGRLAVLGHSMAGDVIARYALATPAVAATV 136
Cdd:COG3571    75 ARL-AGLPLVIGGKSMGGRVASMLAAEGGGAAGLV 108
 
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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