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Conserved domains on  [gi|2519104131|ref|WP_284806212|]
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triacylglycerol lipase [Corynebacterium amycolatum]

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

 Zoom to residue level

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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 ...
 84-205 7.85e-22

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


:

Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 89.12  E-value: 7.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  84 PAPGDNPVVMIHGMNSNSYqTYARMAPELKAMGKCLYAFNVGklgpdefsvlgsiptmRNMTPLDTALAELTAKIETLKA 163
Cdd:COG1075     1 YAATRYPVVLVHGLGGSAA-SWAPLAPRLRAAGYPVYALNYP----------------STNGSIEDSAEQLAAFVDAVLA 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2519104131 164 ETGATEVDIVGHSAGGTLAAAYAKQEQGRG-IGTVVSLAGVLH 205
Cdd:COG1075    64 ATGAEKVDLVGHSMGGLVARYYLKRLGGAAkVARVVTLGTPHH 106
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 84-205 7.85e-22

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 89.12  E-value: 7.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  84 PAPGDNPVVMIHGMNSNSYqTYARMAPELKAMGKCLYAFNVGklgpdefsvlgsiptmRNMTPLDTALAELTAKIETLKA 163
Cdd:COG1075     1 YAATRYPVVLVHGLGGSAA-SWAPLAPRLRAAGYPVYALNYP----------------STNGSIEDSAEQLAAFVDAVLA 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2519104131 164 ETGATEVDIVGHSAGGTLAAAYAKQEQGRG-IGTVVSLAGVLH 205
Cdd:COG1075    64 ATGAEKVDLVGHSMGGLVARYYLKRLGGAAkVARVVTLGTPHH 106
Lipase_2 pfam01674
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ...
 88-303 1.41e-11

Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. Lipases or triacylglycerol acylhydrolases hydrolyse ester bonds in triacylglycerol giving diacylglycerol, monoacylglycerol, glycerol and free fatty acids. Swiss:P37957 is an extracellular lipase from B. subtilis 168.


Pssm-ID: 396304 [Multi-domain]  Cd Length: 218  Bit Score: 63.52  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  88 DNPVVMIHGMNSNSYQTYARMAPELKAMG---KCLYAFNVGKlgpdefsvlGSIPTMRNMTPLDTALAELTAKIETLKAE 164
Cdd:pfam01674   1 NQPVIFVHGNSGLAAGGWSKLSQYFKERGytlAELYATTWGD---------GNESTSLQRAEKCEYVKQIRRFIEAVLGY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131 165 TGATEVDIVGHSAGGTLAAAYAKqeQGRGIGTVVSLAGVL---HGT--SLLGISYGLeelnQFDNAGDKAAGyiVSPSLV 239
Cdd:pfam01674  72 TGAAKVDIVAHSMGVPIARKAIL--GGNCVDTNEDLGPPLtslVDTfvSVAGANYGI----CLCPSGDTLFP--ICNMVI 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519104131 240 DLMQHGQFMAKINEGGlEQPGVNYVAISTQVDEAVTPMAASqWNAPTSNSILLQDGCSADLSGH 303
Cdd:pfam01674 144 GLYCYSKFLQDINAQG-KYEGEYVFSIWSTADEVIGKGYMV-CGKDTSLIPGSDGKKIYDRLGH 205
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 84-205 7.85e-22

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 89.12  E-value: 7.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  84 PAPGDNPVVMIHGMNSNSYqTYARMAPELKAMGKCLYAFNVGklgpdefsvlgsiptmRNMTPLDTALAELTAKIETLKA 163
Cdd:COG1075     1 YAATRYPVVLVHGLGGSAA-SWAPLAPRLRAAGYPVYALNYP----------------STNGSIEDSAEQLAAFVDAVLA 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2519104131 164 ETGATEVDIVGHSAGGTLAAAYAKQEQGRG-IGTVVSLAGVLH 205
Cdd:COG1075    64 ATGAEKVDLVGHSMGGLVARYYLKRLGGAAkVARVVTLGTPHH 106
Lipase_2 pfam01674
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ...
 88-303 1.41e-11

Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. Lipases or triacylglycerol acylhydrolases hydrolyse ester bonds in triacylglycerol giving diacylglycerol, monoacylglycerol, glycerol and free fatty acids. Swiss:P37957 is an extracellular lipase from B. subtilis 168.


Pssm-ID: 396304 [Multi-domain]  Cd Length: 218  Bit Score: 63.52  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  88 DNPVVMIHGMNSNSYQTYARMAPELKAMG---KCLYAFNVGKlgpdefsvlGSIPTMRNMTPLDTALAELTAKIETLKAE 164
Cdd:pfam01674   1 NQPVIFVHGNSGLAAGGWSKLSQYFKERGytlAELYATTWGD---------GNESTSLQRAEKCEYVKQIRRFIEAVLGY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131 165 TGATEVDIVGHSAGGTLAAAYAKqeQGRGIGTVVSLAGVL---HGT--SLLGISYGLeelnQFDNAGDKAAGyiVSPSLV 239
Cdd:pfam01674  72 TGAAKVDIVAHSMGVPIARKAIL--GGNCVDTNEDLGPPLtslVDTfvSVAGANYGI----CLCPSGDTLFP--ICNMVI 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519104131 240 DLMQHGQFMAKINEGGlEQPGVNYVAISTQVDEAVTPMAASqWNAPTSNSILLQDGCSADLSGH 303
Cdd:pfam01674 144 GLYCYSKFLQDINAQG-KYEGEYVFSIWSTADEVIGKGYMV-CGKDTSLIPGSDGKKIYDRLGH 205
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 89-204 9.19e-09

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: 55.59  E-value: 9.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  89 NPVVMIHGMNSNSYQtYARMAPELKAMGKCLYAFNVgkLGPDEFSVLGSIPTMRNMTpldtaLAELtakIETLKAETGAT 168
Cdd:pfam00561   1 PPVLLLHGLPGSSDL-WRKLAPALARDGFRVIALDL--RGFGKSSRPKAQDDYRTDD-----LAED---LEYILEALGLE 69

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2519104131 169 EVDIVGHSAGGTLAAAYAKQEQGRgIGTVVSLAGVL 204
Cdd:pfam00561  70 KVNLVGHSMGGLIALAYAAKYPDR-VKALVLLGALD 104
Palm_thioest pfam02089
Palmitoyl protein thioesterase;
90-282 2.29e-06

Palmitoyl protein thioesterase;


Pssm-ID: 460441 [Multi-domain]  Cd Length: 248  Bit Score: 48.39  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  90 PVVMIHGM-NSNSYQTYARMAPELKAMGKCLYAFNVgKLGPDEFSVLGSIPTMrnmtPLDTALAELTAKIETLKAETGat 168
Cdd:pfam02089   1 PVVIWHGLgDSCASPGMQSLAELIKEAHPGTYVHSI-DIGDGPSEDRKASFFG----NMNEQVEAVCEQLKPELPANG-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131 169 eVDIVGHSAGGTLAAAYAKQEQGRGIGTVVSLAGVLHGTSllGISYGLEE---LNQF---DNAGDK--AAGYIVSPSLVD 240
Cdd:pfam02089  74 -FNAIGFSQGGLFLRGLVERCPDPPVHNLISLGGPHMGVF--GLPFACCNallLGGLvysDWVQKHlvQAQYWRDPTDLD 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2519104131 241 L-MQHGQFMAKINEgglEQPGV-------------NYVAISTQVDEAVTPMAASQW 282
Cdd:pfam02089 151 EyLKKSKFLADINN---ERPHRknetykenllsleNLVLVGFPDDTTVVPKESSWF 203
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
90-216 3.92e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 47.30  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  90 PVVMIHGMNSNSYQtYARMAPELKAMGkclyaFNVgkLGPDefsvL----GSIPTMRNMTPLDTALAELTAKIETLKAET 165
Cdd:COG2267    30 TVVLVHGLGEHSGR-YAELAEALAAAG-----YAV--LAFD----LrghgRSDGPRGHVDSFDDYVDDLRAALDALRARP 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2519104131 166 GaTEVDIVGHSAGGTLAAAYAkQEQGRGIGTVVSLAGVLHGTSLLGISYGL 216
Cdd:COG2267    98 G-LPVVLLGHSMGGLIALLYA-ARYPDRVAGLVLLAPAYRADPLLGPSARW 146
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 90-204 1.21e-04

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: 43.07  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  90 PVVMIHGMNSNSYqTYARMAPELKamgkclyafnvgklgpDEFSVLgsIPTMRNM-----TPLDTALAELTAKIETLKAE 164
Cdd:COG0596    25 PVVLLHGLPGSSY-EWRPLIPALA----------------AGYRVI--APDLRGHgrsdkPAGGYTLDDLADDLAALLDA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2519104131 165 TGATEVDIVGHSAGGTLAAAYAKQEQGRgIGTVVSLAGVL 204
Cdd:COG0596    86 LGLERVVLVGHSMGGMVALELAARHPER-VAGLVLVDEVL 124
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
84-210 3.23e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 41.49  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  84 PAPGdnpVVMIHGMNSNSYQtYARMAPELKAMGkclyaFNVgkLGPDEFSVLGSIPT------MRNMTPLDTALAELTAK 157
Cdd:COG0412    28 PRPG---VVVLHEIFGLNPH-IRDVARRLAAAG-----YVV--LAPDLYGRGGPGDDpdearaLMGALDPELLAADLRAA 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2519104131 158 IETLKA--ETGATEVDIVGHSAGGTLAAAYAkqEQGRGIGTVVSLAGVLHGTSLL 210
Cdd:COG0412    97 LDWLKAqpEVDAGRVGVVGFCFGGGLALLAA--ARGPDLAAAVSFYGGLPADDLL 149
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 91-314 6.88e-04

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 40.53  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  91 VVMIHGmnsnSYQTYARMAPELKAmgkclyafNVGKLGPDefsvlgsIPTMRNMTPLDTALAELTAKIETLKAETGATEV 170
Cdd:pfam12697   1 VVLVHG----AGLSAAPLAALLAA--------GVAVLAPD-------LPGHGSSSPPPLDLADLADLAALLDELGAARPV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131 171 DIVGHSAGGTLAAAYAKQEQGRGI---GTVVSLAGVLHGTSLLGISYGLEELNQFDNA--------GDKAAGYIVSPSLV 239
Cdd:pfam12697  62 VLVGHSLGGAVALAAAAAALVVGVlvaPLAAPPGLLAALLALLARLGAALAAPAWLAAeslargflDDLPADAEWAAALA 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519104131 240 DLMQHGQFMAKINEGGLEQPGVNYVAISTQvDEAVTPMAASQWNAPTSNSILLQDGCsadlsGHiGLTFSPRAIA 314
Cdd:pfam12697 142 RLAALLAALALLPLAAWRDLPVPVLVLAEE-DRLVPELAQRLLAALAGARLVVLPGA-----GH-LPLDDPEEVA 209
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
139-186 2.19e-03

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


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 39.94  E-value: 2.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2519104131 139 PTMRNMTpLDTALAE--LTAkIETLKAETGATEVDIVGHSAGGTLAAAYA 186
Cdd:COG3243   248 AEDRDLG-LDDYVEDgiLAA-VDAVREITGEDKVNLLGYCLGGTLLAIYA 295
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 91-199 3.75e-03

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: 38.35  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  91 VVMIHGMNSnSYQTYARMAPELKAMGKCLYAFNV---GKlgpdefsvlgSIPTMRNMTPLDTALAELTAKIETLKAETGA 167
Cdd:pfam12146   7 VVLVHGLGE-HSGRYAHLADALAAQGFAVYAYDHrghGR----------SDGKRGHVPSFDDYVDDLDTFVDKIREEHPG 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2519104131 168 TEVDIVGHSAGGTLAAAYAKQEQGRGIGTVVS 199
Cdd:pfam12146  76 LPLFLLGHSMGGLIAALYALRYPDKVDGLILS 107
YpfH COG0400
Predicted esterase [General function prediction only];
84-206 5.96e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.58  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519104131  84 PAPGDNPVVMIHGMNSNSYQtYARMAPELKAMGKCLYAFNvgklGPDEFSVLG----SIPTMR---NMTPLDTALAELTA 156
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEED-LLPLAPELALPGAAVLAPR----APVPEGPGGrawfDLSFLEgreDEEGLAAAAEALAA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2519104131 157 KIETLKAETGATEVDIV--GHSAGGTLAAAYAKQEQGRgIGTVVSLAGVLHG 206
Cdd:COG0400    76 FIDELEARYGIDPERIVlaGFSQGAAMALSLALRRPEL-LAGVVALSGYLPG 126
 
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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