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Conserved domains on  [gi|71042323|pdb|1ZI9|A]
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Chain A, Carboxymethylenebutenolidase

Protein Classification

dienelactone hydrolase family protein( domain architecture ID 11123939)

dienelactone hydrolase family protein such as carboxymethylenebutenolidase, which catalyzes the reaction between 4-carboxymethylenebut-2-en-4-olide and water to produce 4-oxohex-2-enedioate

CATH:  3.40.50.1820
EC:  3.-.-.-|3.1.-.-
Gene Ontology:  GO:0005829|GO:0016787
PubMed:  2380986|19508187|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
17-230 2.71e-85

Dienelactone hydrolase family;


:

Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 252.27  E-value: 2.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         17 GALVGSPAKAPAPVIVIAQDIFGVNAFMRETVSWLVDQGYAAVCPDLYARQApgtalDPQDERQREQAY-KLWQAFDMEA 95
Cdd:pfam01738   1 DAYLATPKNPPWPVVVVFQEIFGVNDNIREIADRLADEGYVALAPDLYFRQG-----DPNDEADAARAMfELVSKRVMEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         96 GVGDLEAAIRYARHQPY-SNGKVGLVGYSLGGALAFLVAAKG-YVDRAVGYYGVGLEKQLNKVPEVKHPALFHMGGQDHF 173
Cdd:pfam01738  76 VLDDLEAAVNYLKSQPEvSPKKVGVVGYCMGGALAVLLAAKGpLVDAAVGFYGVGPEPPLIEAPDIKAPILFHFGEEDHF 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
1ZI9_A        174 VPAPSRQLITEGF-GANPLLQVHWYEEAGHSFARTSSSGYVASAAALANERTLDFLAP 230
Cdd:pfam01738 156 VPADSRELIEEALkAANVDHQIHSYPGAGHAFANDSRPSYNAAAAEDAWERTLEFFKQ 213
 
Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
17-230 2.71e-85

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 252.27  E-value: 2.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         17 GALVGSPAKAPAPVIVIAQDIFGVNAFMRETVSWLVDQGYAAVCPDLYARQApgtalDPQDERQREQAY-KLWQAFDMEA 95
Cdd:pfam01738   1 DAYLATPKNPPWPVVVVFQEIFGVNDNIREIADRLADEGYVALAPDLYFRQG-----DPNDEADAARAMfELVSKRVMEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         96 GVGDLEAAIRYARHQPY-SNGKVGLVGYSLGGALAFLVAAKG-YVDRAVGYYGVGLEKQLNKVPEVKHPALFHMGGQDHF 173
Cdd:pfam01738  76 VLDDLEAAVNYLKSQPEvSPKKVGVVGYCMGGALAVLLAAKGpLVDAAVGFYGVGPEPPLIEAPDIKAPILFHFGEEDHF 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
1ZI9_A        174 VPAPSRQLITEGF-GANPLLQVHWYEEAGHSFARTSSSGYVASAAALANERTLDFLAP 230
Cdd:pfam01738 156 VPADSRELIEEALkAANVDHQIHSYPGAGHAFANDSRPSYNAAAAEDAWERTLEFFKQ 213
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
1-229 1.83e-55

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 176.70  E-value: 1.83e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A        1 MLTEGISIQSYDGHTFGALVGSPA-KAPAPVIVIAQDIFGVNAFMRETVSWLVDQGYAAVCPDLYARQAPGTaldpqder 79
Cdd:COG0412   1 MTTETVTIPTPDGVTLPGYLARPAgGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGD-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A       80 QREQAYKLWQAFDMEAGVGDLEAAIRYARHQPY-SNGKVGLVGYSLGGALAFLVAAKGY-VDRAVGYYGVG-LEKQLNKV 156
Cdd:COG0412  73 DPDEARALMGALDPELLAADLRAALDWLKAQPEvDAGRVGVVGFCFGGGLALLAAARGPdLAAAVSFYGGLpADDLLDLA 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1ZI9_A      157 PEVKHPALFHMGGQDHFVPAPSRQLITEGF-GANPLLQVHWYEEAGHSFARTSSSGYVASAAALANERTLDFLA 229
Cdd:COG0412 153 ARIKAPVLLLYGEKDPLVPPEQVAALEAALaAAGVDVELHVYPGAGHGFTNPGRPRYDPAAAEDAWQRTLAFLA 226
/NonD TIGR00976
putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes ...
 24-134 2.11e-03

putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes the cocaine esterase CocE, several glutaryl-7-ACA acylases, and the putative diester hydrolase NonD of Streptomyces griseus (all hydrolases). This family shows extensive, low-level similarity to a family of xaa-pro dipeptidyl-peptidases, and local similarity by PSI-BLAST to many other hydrolases. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273375 [Multi-domain]  Cd Length: 550  Bit Score: 39.01  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         24 AKAPAPVIVIAQDIFGVNAFMRETVS----WLVDQGYAAVCPDLYARQAPGTALDPQDERQREqayklwqafdmeagvgD 99
Cdd:TIGR00976  18 GGGPVPVILSRTPYGKDAGLRWGLDKtepaWFVAQGYAVVIQDTRGRGASEGEFDLLGSDEAA----------------D 81

                          90       100       110
                  ....*....|....*....|....*....|....*
1ZI9_A        100 LEAAIRYARHQPYSNGKVGLVGYSLGGALAFLVAA 134
Cdd:TIGR00976  82 GYDLVDWIAKQPWCDGNVGMLGVSYLAVTQLLAAV 116
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 99-144 7.08e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 35.94  E-value: 7.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
1ZI9_A       99 DLEAAIRYARHQpYSNGKVGLVGYSLGGALAFLVAA------KGYVDRAVGY 144
Cdd:cd00741  13 LVLPLLKSALAQ-YPDYKIHVTGHSLGGALAGLAGLdlrgrgLGRLVRVYTF 63
 
Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
17-230 2.71e-85

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 252.27  E-value: 2.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         17 GALVGSPAKAPAPVIVIAQDIFGVNAFMRETVSWLVDQGYAAVCPDLYARQApgtalDPQDERQREQAY-KLWQAFDMEA 95
Cdd:pfam01738   1 DAYLATPKNPPWPVVVVFQEIFGVNDNIREIADRLADEGYVALAPDLYFRQG-----DPNDEADAARAMfELVSKRVMEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         96 GVGDLEAAIRYARHQPY-SNGKVGLVGYSLGGALAFLVAAKG-YVDRAVGYYGVGLEKQLNKVPEVKHPALFHMGGQDHF 173
Cdd:pfam01738  76 VLDDLEAAVNYLKSQPEvSPKKVGVVGYCMGGALAVLLAAKGpLVDAAVGFYGVGPEPPLIEAPDIKAPILFHFGEEDHF 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
1ZI9_A        174 VPAPSRQLITEGF-GANPLLQVHWYEEAGHSFARTSSSGYVASAAALANERTLDFLAP 230
Cdd:pfam01738 156 VPADSRELIEEALkAANVDHQIHSYPGAGHAFANDSRPSYNAAAAEDAWERTLEFFKQ 213
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
1-229 1.83e-55

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 176.70  E-value: 1.83e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A        1 MLTEGISIQSYDGHTFGALVGSPA-KAPAPVIVIAQDIFGVNAFMRETVSWLVDQGYAAVCPDLYARQAPGTaldpqder 79
Cdd:COG0412   1 MTTETVTIPTPDGVTLPGYLARPAgGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGD-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A       80 QREQAYKLWQAFDMEAGVGDLEAAIRYARHQPY-SNGKVGLVGYSLGGALAFLVAAKGY-VDRAVGYYGVG-LEKQLNKV 156
Cdd:COG0412  73 DPDEARALMGALDPELLAADLRAALDWLKAQPEvDAGRVGVVGFCFGGGLALLAAARGPdLAAAVSFYGGLpADDLLDLA 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1ZI9_A      157 PEVKHPALFHMGGQDHFVPAPSRQLITEGF-GANPLLQVHWYEEAGHSFARTSSSGYVASAAALANERTLDFLA 229
Cdd:COG0412 153 ARIKAPVLLLYGEKDPLVPPEQVAALEAALaAAGVDVELHVYPGAGHGFTNPGRPRYDPAAAEDAWQRTLAFLA 226
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
1-206 1.77e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 72.73  E-value: 1.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A        1 MLTEGISIQSYDGHTFGALVGSPAKAPAPVIVIAQDIFGVNAFMRETVSWLVDQGYAAVCPDLyarqaPGtaldpQDERQ 80
Cdd:COG2267   1 MTRRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDL-----RG-----HGRSD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A       81 REQAYklwqAFDMEAGVGDLEAAIRYARHQPysNGKVGLVGYSLGGALAFLVAAKG-------------YVDRAVGYYGV 147
Cdd:COG2267  71 GPRGH----VDSFDDYVDDLRAALDALRARP--GLPVVLLGHSMGGLIALLYAARYpdrvaglvllapaYRADPLLGPSA 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1ZI9_A      148 GLEKQL---NKVPEVKHPALFHMGGQDHFVPAPSRQLITEGFGANplLQVHWYEEAGHSFAR 206
Cdd:COG2267 145 RWLRALrlaEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPD--VELVLLPGARHELLN 204
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
7-229 1.33e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 67.73  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A        7 SIQSYDGHTFGALVGSPAKA-PAPVIVIAQDI-FGVNAFMRETVSWLVDQGYAAVCPDlyarqAPGTALDPQDERQREQA 84
Cdd:COG1506   1 TFKSADGTTLPGWLYLPADGkKYPVVVYVHGGpGSRDDSFLPLAQALASRGYAVLAPD-----YRGYGESAGDWGGDEVD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A       85 yklwqafdmeagvgDLEAAIRYARHQPYSNG-KVGLVGYSLGGALAFLVAAK--GYVDRAVGYYGV-------------- 147
Cdd:COG1506  76 --------------DVLAAIDYLAARPYVDPdRIGIYGHSYGGYMALLAAARhpDRFKAAVALAGVsdlrsyygttreyt 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A      148 ------------GLEKQ--LNKVPEVKHPALFHMGGQDHFVP-APSRQLITEGFGANPLLQVHWYEEAGHSFARTSSSGY 212
Cdd:COG1506 142 erlmggpwedpeAYAARspLAYADKLKTPLLLIHGEADDRVPpEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDY 221

                       250
                ....*....|....*..
1ZI9_A      213 VasaaalanERTLDFLA 229
Cdd:COG1506 222 L--------ERILDFLD 230
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
44-228 4.22e-07

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 49.17  E-value: 4.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A       44 MRETVSWLVDQGYAAVCPDLyarqaPGTALDPQDERQreqayklwqaFDMEAGVGDLEAAIRYARhQPYSngKVGLVGYS 123
Cdd:COG1647  31 MRPLAEALAKAGYTVYAPRL-----PGHGTSPEDLLK----------TTWEDWLEDVEEAYEILK-AGYD--KVIVIGLS 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A      124 LGGALAFLVAAK-GYVDRAV-----------------------------------------GYYGVGLE--KQLNK---- 155
Cdd:COG1647  93 MGGLLALLLAARyPDVAGLVllspalkiddpsapllpllkylarslrgigsdiedpevaeyAYDRTPLRalAELQRlire 172

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1ZI9_A      156 ----VPEVKHPALFHMGGQDHFVPAPSRQLITEGFGANPlLQVHWYEEAGHSFArtsssgyVASAAALANERTLDFL 228
Cdd:COG1647 173 vrrdLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPD-KELVWLEDSGHVIT-------LDKDREEVAEEILDFL 241
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 38-229 3.19e-06

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: 46.53  E-value: 3.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A       38 FGVNAFMRETVSWLVDQGYAAVCPDLyarqaPGTALDPQDERqreqayklwqAFDMEAGVGDLEAAIRYARHQPysngkV 117
Cdd:COG0596  32 LPGSSYEWRPLIPALAAGYRVIAPDL-----RGHGRSDKPAG----------GYTLDDLADDLAALLDALGLER-----V 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A      118 GLVGYSLGGALAFLVAAK--GYVDRAV----------------GYYGVGLEKQLN---------KVPEVKHPALFHMGGQ 170
Cdd:COG0596  92 VLVGHSMGGMVALELAARhpERVAGLVlvdevlaalaeplrrpGLAPEALAALLRalartdlreRLARITVPTLVIWGEK 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
1ZI9_A      171 DHFVPAPSRQLITEgfgANPLLQVHWYEEAGHSFArtsssgyvASAAALANERTLDFLA 229
Cdd:COG0596 172 DPIVPPALARRLAE---LLPNAELVVLPGAGHFPP--------LEQPEAFAAALRDFLA 219
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
23-136 5.80e-05

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 43.10  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         23 PAKAPAPVIVIAQ------DIFGVNAFMRETVSWlVDQGYAAVCPDlyarqAPGTAL---DPQDERQREQAyklwqafdm 93
Cdd:pfam02129  14 KTGGPVPALLTRSpygarrDGASDLALAHPEWEF-AARGYAVVYQD-----VRGTGGsegVFTVGGPQEAA--------- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
1ZI9_A         94 eagvgDLEAAIRYARHQPYSNGKVGLVGYSLGGALAFLVAAKG 136
Cdd:pfam02129  79 -----DGKDVIDWLAGQPWCNGKVGMTGISYLGTTQLAAAATG 116
COG2936 COG2936
Predicted acyl esterase [General function prediction only];
27-136 4.28e-04

Predicted acyl esterase [General function prediction only];


Pssm-ID: 442179 [Multi-domain]  Cd Length: 555  Bit Score: 41.06  E-value: 4.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A       27 PAPVIVIAQ----DIFGVNAFMReTVSWLVDQGYAAVcpdlyaRQ-APGT-----ALDP--QDERQreqayklwqafdme 94
Cdd:COG2936  38 PVPVILERTpygkRDGTAGRDLG-PHPYFAERGYAVV------VQdVRGTggsegEFDPyrVDEQT-------------- 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1ZI9_A       95 agvgDLEAAIRYARHQPYSNGKVGLVGYSLGGALAFLVAAKG 136
Cdd:COG2936  97 ----DGYDTIDWLAKQPWSNGKVGMIGISYGGFTQLAAAADR 134
/NonD TIGR00976
putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes ...
 24-134 2.11e-03

putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes the cocaine esterase CocE, several glutaryl-7-ACA acylases, and the putative diester hydrolase NonD of Streptomyces griseus (all hydrolases). This family shows extensive, low-level similarity to a family of xaa-pro dipeptidyl-peptidases, and local similarity by PSI-BLAST to many other hydrolases. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273375 [Multi-domain]  Cd Length: 550  Bit Score: 39.01  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A         24 AKAPAPVIVIAQDIFGVNAFMRETVS----WLVDQGYAAVCPDLYARQAPGTALDPQDERQREqayklwqafdmeagvgD 99
Cdd:TIGR00976  18 GGGPVPVILSRTPYGKDAGLRWGLDKtepaWFVAQGYAVVIQDTRGRGASEGEFDLLGSDEAA----------------D 81

                          90       100       110
                  ....*....|....*....|....*....|....*
1ZI9_A        100 LEAAIRYARHQPYSNGKVGLVGYSLGGALAFLVAA 134
Cdd:TIGR00976  82 GYDLVDWIAKQPWCDGNVGMLGVSYLAVTQLLAAV 116
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 99-144 7.08e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 35.94  E-value: 7.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
1ZI9_A       99 DLEAAIRYARHQpYSNGKVGLVGYSLGGALAFLVAA------KGYVDRAVGY 144
Cdd:cd00741  13 LVLPLLKSALAQ-YPDYKIHVTGHSLGGALAGLAGLdlrgrgLGRLVRVYTF 63
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 96-140 7.09e-03

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: 36.71  E-value: 7.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
1ZI9_A         96 GVGDLEAAIRYARhQPYSNGKVGLVGYSLGGALAFLVAAKgYVDR 140
Cdd:pfam00561  51 RTDDLAEDLEYIL-EALGLEKVNLVGHSMGGLIALAYAAK-YPDR 93
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
21-133 8.41e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 36.62  E-value: 8.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZI9_A       21 GSPAKAPAPVIVIAQDIFGVNAFMRETVSWLVDQGYAAVCPD---------LYARQAPGTALDPQD--ERQREQAYKLWQ 89
Cdd:COG4188  55 DAPAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDhpgsnaadlSAALDGLADALDPEElwERPLDLSFVLDQ 134

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
1ZI9_A       90 AFDMEAGVGDLEAAIRYARhqpysngkVGLVGYSLGGALAFLVA 133
Cdd:COG4188 135 LLALNKSDPPLAGRLDLDR--------IGVIGHSLGGYTALALA 170
 
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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