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Conserved domains on  [gi|648509774|ref|WP_026201525|]
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MULTISPECIES: triacylglycerol lipase [unclassified Bradyrhizobium]

Protein Classification

esterase/lipase family protein( domain architecture ID 10787203)

esterase/lipase family protein is an alpha/beta hydrolase, such as triacylglycerol lipase that catalyzes the hydrolysis of a triacylglycerol to form the corresponding diacylglycerol and a carboxylate

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016787|GO:0016042
PubMed:  37582413|12369917|19508187|11099800

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 40-141 6.45e-15

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


:

Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 68.70  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774  40 PRGDGHPVLVLPGLVASDASTRALRTFLTSKGYAVSGWrqgrNYGlreGVQHAMVDLVEELSD--------THGRKISLV 111
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYAL----NYP---STNGSIEDSAEQLAAfvdavlaaTGAEKVDLV 73

                         90       100       110
                 ....*....|....*....|....*....|..
gi 648509774 112 GWSLGGLYARQLAKMM--PERVRQVITLGSPF 141
Cdd:COG1075   74 GHSMGGLVARYYLKRLggAAKVARVVTLGTPH 105
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 40-141 6.45e-15

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 68.70  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774  40 PRGDGHPVLVLPGLVASDASTRALRTFLTSKGYAVSGWrqgrNYGlreGVQHAMVDLVEELSD--------THGRKISLV 111
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYAL----NYP---STNGSIEDSAEQLAAfvdavlaaTGAEKVDLV 73

                         90       100       110
                 ....*....|....*....|....*....|..
gi 648509774 112 GWSLGGLYARQLAKMM--PERVRQVITLGSPF 141
Cdd:COG1075   74 GHSMGGLVARYYLKRLggAAKVARVVTLGTPH 105
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 41-147 1.37e-04

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 41.97  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774   41 RGDGHPVLVLPGL------VASDASTRALRTFLTSKGyavsgwrqGRNYGLREGVQHAmVDLVEELSDTHGR-------- 106
Cdd:pfam07819   1 ELSGIPVLFIPGNagsykqVRSIASVAANLYQVLRKL--------LQNDNGFHLDFFS-VDFNEELSAFHGRtlldqaey 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648509774  107 --------------------KISLVGWSLGGLYARQ---LAKMMPERVRQVITLGSPFAGNPRS 147
Cdd:pfam07819  72 lndairyilslyasgrpgptSVILIGHSMGGIVARAaltLPNYIPQSVNTIITLSSPHAKPPLT 135
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 92-139 3.68e-04

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 40.96  E-value: 3.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 648509774   92 AMVDLVEELSDTHGRKISLVGWSLGGLYARQLAKMMPERVRQVITLGS 139
Cdd:TIGR01738  51 SLADMAEAIAAQAPDPAIWLGWSLGGLVALHIAATHPDRVRALVTVAS 98
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
92-139 8.67e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 39.62  E-value: 8.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 648509774  92 AMVDLVEELSDTHGRKISLVGWSLGGLYARQLAKMMPERVRQVITLGS 139
Cdd:PRK10349  60 SLADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVAS 107
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 40-141 6.45e-15

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 68.70  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774  40 PRGDGHPVLVLPGLVASDASTRALRTFLTSKGYAVSGWrqgrNYGlreGVQHAMVDLVEELSD--------THGRKISLV 111
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYAL----NYP---STNGSIEDSAEQLAAfvdavlaaTGAEKVDLV 73

                         90       100       110
                 ....*....|....*....|....*....|..
gi 648509774 112 GWSLGGLYARQLAKMM--PERVRQVITLGSPF 141
Cdd:COG1075   74 GHSMGGLVARYYLKRLggAAKVARVVTLGTPH 105
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 43-234 1.11e-08

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: 53.85  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774  43 DGHPVLVLPGLVASDASTRALRTFLtSKGYAVSGWRQgRNYGLREGVQ-----HAMVDLVEELSDTHG-RKISLVGWSLG 116
Cdd:COG0596   22 DGPPVVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDL-RGHGRSDKPAggytlDDLADDLAALLDALGlERVVLVGHSMG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774 117 GLYARQLAKMMPERVRQVITLGSPFAGNPRSTNAWRVYEWASGRKSDEVDPRFGGELAVPPPVPTTAIFSRTDGVCAWQG 196
Cdd:COG0596  100 GMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPAL 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 648509774 197 C--MEKTGAQTESIEVE-SSHCGMGHHPAVVYAVADRLAQK 234
Cdd:COG0596  180 ArrLAELLPNAELVVLPgAGHFPPLEQPEAFAAALRDFLAR 220
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
33-154 5.45e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.93  E-value: 5.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774  33 LPLLSLAPRGDGHP-VLVLPGLVASDASTRALRTFLTSKGYAV----------SGWRQGRNYGLREgVQHAMVDLVEELS 101
Cdd:COG2267   16 LRGRRWRPAGSPRGtVVLVHGLGEHSGRYAELAEALAAAGYAVlafdlrghgrSDGPRGHVDSFDD-YVDDLRAALDALR 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 648509774 102 DTHGRKISLVGWSLGGLYARQLAKMMPERVRQVITLGSPFAGNPRSTNAWRVY 154
Cdd:COG2267   95 ARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL 147
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
66-141 4.03e-05

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 44.17  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774  66 FLTSKG---YAVSgWR----QGRNYGL----REGVqHAMVDLVEElsDTHGRKISLVGWSLGG----LYARQLAKMMPER 130
Cdd:COG3243  230 YLVDQGftvFLIS-WGnpdaEDRDLGLddyvEDGI-LAAVDAVRE--ITGEDKVNLLGYCLGGtllaIYAALLAARGPDR 305

                         90
                 ....*....|.
gi 648509774 131 VRQVITLGSPF 141
Cdd:COG3243  306 VASLTLLATPL 316
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 41-147 1.37e-04

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 41.97  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774   41 RGDGHPVLVLPGL------VASDASTRALRTFLTSKGyavsgwrqGRNYGLREGVQHAmVDLVEELSDTHGR-------- 106
Cdd:pfam07819   1 ELSGIPVLFIPGNagsykqVRSIASVAANLYQVLRKL--------LQNDNGFHLDFFS-VDFNEELSAFHGRtlldqaey 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648509774  107 --------------------KISLVGWSLGGLYARQ---LAKMMPERVRQVITLGSPFAGNPRS 147
Cdd:pfam07819  72 lndairyilslyasgrpgptSVILIGHSMGGIVARAaltLPNYIPQSVNTIITLSSPHAKPPLT 135
Palm_thioest pfam02089
Palmitoyl protein thioesterase;
46-143 1.38e-04

Palmitoyl protein thioesterase;


Pssm-ID: 460441 [Multi-domain]  Cd Length: 248  Bit Score: 42.23  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774   46 PVLVLPGLVASDAST--RALRTFLTSKG---YAVS-----GWRQGRNYG----LREGVQHAMVDLVEELSDthgRKISLV 111
Cdd:pfam02089   1 PVVIWHGLGDSCASPgmQSLAELIKEAHpgtYVHSidigdGPSEDRKASffgnMNEQVEAVCEQLKPELPA---NGFNAI 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 648509774  112 GWSLGGLYARQLAKMMPE-RVRQVITLGSPFAG 143
Cdd:pfam02089  78 GFSQGGLFLRGLVERCPDpPVHNLISLGGPHMG 110
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
35-141 1.57e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.93  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774  35 LLSLAPRGDGHPVLVLP--GLVASDASTRALRTFLTSKGYAVSGWrQGRNYGLREGV--------QHAMVDLVEELSDTH 104
Cdd:COG1506   13 WLYLPADGKKYPVVVYVhgGPGSRDDSFLPLAQALASRGYAVLAP-DYRGYGESAGDwggdevddVLAAIDYLAARPYVD 91

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 648509774 105 GRKISLVGWSLGGLYARQLAKMMPERVRQVITLGSPF 141
Cdd:COG1506   92 PDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS 128
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 46-140 3.47e-04

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: 40.95  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774   46 PVLVLPGLVASDASTRALRTFLTSKGYAVSGWRQgRNYG-------LREGVQHAMVDLVEELSDTHG-RKISLVGWSLGG 117
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDL-RGFGkssrpkaQDDYRTDDLAEDLEYILEALGlEKVNLVGHSMGG 80

                          90       100
                  ....*....|....*....|...
gi 648509774  118 LYARQLAKMMPERVRQVITLGSP 140
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGAL 103
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 92-139 3.68e-04

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 40.96  E-value: 3.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 648509774   92 AMVDLVEELSDTHGRKISLVGWSLGGLYARQLAKMMPERVRQVITLGS 139
Cdd:TIGR01738  51 SLADMAEAIAAQAPDPAIWLGWSLGGLVALHIAATHPDRVRALVTVAS 98
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
47-186 4.56e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 40.70  E-value: 4.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648509774  47 VLVLPGLVASDASTRALRTFLTSKGYAVSG---------WRQGRNYGLREGVQHAmVDLVEELSDTHgRKISLVGWSLGG 117
Cdd:COG1647   18 VLLLHGFTGSPAEMRPLAEALAKAGYTVYAprlpghgtsPEDLLKTTWEDWLEDV-EEAYEILKAGY-DKVIVIGLSMGG 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648509774 118 LYARQLAKMMPErVRQVITLGSPFAGNPRSTNAWRVYEWASG--RKSDEVDPRFGGELAVPPPVPTTAIFS 186
Cdd:COG1647   96 LLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYLARslRGIGSDIEDPEVAEYAYDRTPLRALAE 165
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
92-139 8.67e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 39.62  E-value: 8.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 648509774  92 AMVDLVEELSDTHGRKISLVGWSLGGLYARQLAKMMPERVRQVITLGS 139
Cdd:PRK10349  60 SLADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVAS 107
 
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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