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Conserved domains on  [gi|742403343|ref|WP_038882468|]
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carboxylesterase/lipase family protein, partial [Cronobacter malonaticus]

Protein Classification

carboxylesterase/lipase family protein( domain architecture ID 10006294)

carboxylesterase/lipase family protein similar to carboxylesterase, which catalyzes the hydrolysis of a carboxylic ester to form an alcohol and a carboxylate, and lipase, which hydrolyzes triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0052689|GO:0016298
SCOP:  3000102

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
1-404 7.84e-153

Carboxylesterase type B [Lipid transport and metabolism];


:

Pssm-ID: 441873  Cd Length: 500  Bit Score: 441.63  E-value: 7.84e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   1 APATRET-PLPVMVWLHGGGFTLGAGSLPPYDGQALARRGVVLVTINYRLGHLGFFAHPALEGEDPAGPVyNFALLDQIA 79
Cdd:COG2272   96 TPALAAGaKLPVMVWIHGGGFVSGSGSEPLYDGAALARRGVVVVTINYRLGALGFLALPALSGESYGASG-NYGLLDQIA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  80 ALRWVQDNIAAFGGDRDNVTLFGESAGARSVLSLMASPLAKGLFHKAIVQSGYTLPDIPRRKALLNGAALTRHLGLDNPT 159
Cdd:COG2272  175 ALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTLAEAEAVGAAFAAALGVAPAT 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 160 AADLRALPADTFWPLTA------PYVTGPAPIAGDIVLPEPMLETFFAARQHPMPVMVGSNSDEASVLAYFG-----VNL 228
Cdd:COG2272  255 LAALRALPAEELLAAQAalaaegPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEGRLFAALLgdlgpLTA 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 229 EEQIRKLRRERRFGLGLIRMLYPGvRGDRELGRQVCRDMAFTTLGFVVMQAQSRRGVPCWRYWFDYVAEGEReTFANGAW 308
Cdd:COG2272  335 ADYRAALRRRFGDDADEVLAAYPA-ASPAEALAALATDRVFRCPARRLAEAHAAAGAPVYLYRFDWRSPPLR-GFGLGAF 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 309 HGNEVPYVFDNLDQVEPLKNyaTAADRAFAGQVADYWVNFARHASAQSqalDGPVRWLACVRGRDRLLRIGLHKKAGwrl 388
Cdd:COG2272  413 HGAELPFVFGNLDAPALTGL--TPADRALSDQMQAYWVNFARTGDPNG---PGLPEWPAYDPEDRAVMVFDAEPRVV--- 484
                        410
                 ....*....|....*.
gi 742403343 389 ENRFMRARLALFKRVM 404
Cdd:COG2272  485 NDPDAEERLDLWDGVV 500
 
Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
1-404 7.84e-153

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 441.63  E-value: 7.84e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   1 APATRET-PLPVMVWLHGGGFTLGAGSLPPYDGQALARRGVVLVTINYRLGHLGFFAHPALEGEDPAGPVyNFALLDQIA 79
Cdd:COG2272   96 TPALAAGaKLPVMVWIHGGGFVSGSGSEPLYDGAALARRGVVVVTINYRLGALGFLALPALSGESYGASG-NYGLLDQIA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  80 ALRWVQDNIAAFGGDRDNVTLFGESAGARSVLSLMASPLAKGLFHKAIVQSGYTLPDIPRRKALLNGAALTRHLGLDNPT 159
Cdd:COG2272  175 ALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTLAEAEAVGAAFAAALGVAPAT 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 160 AADLRALPADTFWPLTA------PYVTGPAPIAGDIVLPEPMLETFFAARQHPMPVMVGSNSDEASVLAYFG-----VNL 228
Cdd:COG2272  255 LAALRALPAEELLAAQAalaaegPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEGRLFAALLgdlgpLTA 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 229 EEQIRKLRRERRFGLGLIRMLYPGvRGDRELGRQVCRDMAFTTLGFVVMQAQSRRGVPCWRYWFDYVAEGEReTFANGAW 308
Cdd:COG2272  335 ADYRAALRRRFGDDADEVLAAYPA-ASPAEALAALATDRVFRCPARRLAEAHAAAGAPVYLYRFDWRSPPLR-GFGLGAF 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 309 HGNEVPYVFDNLDQVEPLKNyaTAADRAFAGQVADYWVNFARHASAQSqalDGPVRWLACVRGRDRLLRIGLHKKAGwrl 388
Cdd:COG2272  413 HGAELPFVFGNLDAPALTGL--TPADRALSDQMQAYWVNFARTGDPNG---PGLPEWPAYDPEDRAVMVFDAEPRVV--- 484
                        410
                 ....*....|....*.
gi 742403343 389 ENRFMRARLALFKRVM 404
Cdd:COG2272  485 NDPDAEERLDLWDGVV 500
COesterase pfam00135
Carboxylesterase family;
6-390 6.50e-89

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 278.42  E-value: 6.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343    6 ETPLPVMVWLHGGGFTLGAGSLppYDGQALARRG-VVLVTINYRLGHLGFFAhpaLEGEDPAGpvyNFALLDQIAALRWV 84
Cdd:pfam00135 100 KNKLPVMVWIHGGGFMFGSGSL--YDGSYLAAEGdVIVVTINYRLGPLGFLS---TGDDEAPG---NYGLLDQVLALRWV 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   85 QDNIAAFGGDRDNVTLFGESAGARSVLSLMASPLAKGLFHKAIVQSG-----YTLPDIPRRKAllngAALTRHLGLDNPT 159
Cdd:pfam00135 172 QENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGsalspWAIQSNARQRA----KELAKLVGCPTSD 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  160 AAD----LRALPAD-------TFWPLTAPYVTGPAPIAGDIVLPEPMLETFFAARQHPMPVMVGSNSDEASVLAYFGVNl 228
Cdd:pfam00135 248 SAElvecLRSKPAEelldaqlKLLVYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLIGVTKDEGLLFAAYILD- 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  229 EEQIRKLRRERRFGLGLIRMLYPGVRGDRELGRQVCRDM-------------------AFTTLGFVV-----MQAQSRRG 284
Cdd:pfam00135 327 NVDILKALEEKLLRSLLIDLLYLLLVDLPEEISAALREEyldwgdrddpetsrralveLLTDYLFNCpvirfADLHASRG 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  285 VPCWRYWFDYVAEGERETFANGAWHGNEVPYVFDNLdqVEPLKNYaTAADRAFAGQVADYWVNFARHASAQSQAldGPVR 364
Cdd:pfam00135 407 TPVYMYSFDYRGSSLRYPKWVGVDHGDELPYVFGTP--FVGALLF-TEEDEKLSRKMMTYWTNFAKTGNPNGPE--GLPK 481
                         410       420
                  ....*....|....*....|....*.
gi 742403343  365 WLACVRGRDRLLRIGLHKKAGWRLEN 390
Cdd:pfam00135 482 WPPYTDENGQYLSIDLEPRVKQGLKA 507
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
2-351 8.92e-79

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 251.48  E-value: 8.92e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   2 PATRETP--LPVMVWLHGGGFTLGAGSLPPYDGqaLARRG--VVLVTINYRLGHLGFFAHPALEGEDpagpvyNFALLDQ 77
Cdd:cd00312   86 PKNTKPGnsLPVMVWIHGGGFMFGSGSLYPGDG--LAREGdnVIVVSINYRLGVLGFLSTGDIELPG------NYGLKDQ 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  78 IAALRWVQDNIAAFGGDRDNVTLFGESAGARSVLSLMASPLAKGLFHKAIVQSG-YTLPDIPRRKALLNGAALTRHLGLD 156
Cdd:cd00312  158 RLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGsALSPWAIQENARGRAKRLARLLGCN 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 157 NPTAAD----LRALPADTFW-----PLTAPYVtGPAP----IAGDIvLPEPMLETFFAARQHPMPVMVGSNSDEASVLAY 223
Cdd:cd00312  238 DTSSAElldcLRSKSAEELLdatrkLLLFSYS-PFLPfgpvVDGDF-IPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAA 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 224 FGVNLEEQIRKLRRERRF-------------GLGLIRMLYPGVRGDRELGRQVCRDMaFTTLGF----VVMQAQSRR--G 284
Cdd:cd00312  316 MLLNFDAKLIIETNDRWLellpyllfyaddaLADKVLEKYPGDVDDSVESRKNLSDM-LTDLLFkcpaRYFLAQHRKagG 394
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742403343 285 VPCWRYWFDYVAEG--ERETFANGAWHGNEVPYVFDNLDqvepLKNYATAADRAFAGQVADYWVNFARH 351
Cdd:cd00312  395 SPVYAYVFDHRSSLsvGRWPPWLGTVHGDEIFFVFGNPL----LKEGLREEEEKLSRTMMKYWANFAKT 459
 
Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
1-404 7.84e-153

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 441.63  E-value: 7.84e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   1 APATRET-PLPVMVWLHGGGFTLGAGSLPPYDGQALARRGVVLVTINYRLGHLGFFAHPALEGEDPAGPVyNFALLDQIA 79
Cdd:COG2272   96 TPALAAGaKLPVMVWIHGGGFVSGSGSEPLYDGAALARRGVVVVTINYRLGALGFLALPALSGESYGASG-NYGLLDQIA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  80 ALRWVQDNIAAFGGDRDNVTLFGESAGARSVLSLMASPLAKGLFHKAIVQSGYTLPDIPRRKALLNGAALTRHLGLDNPT 159
Cdd:COG2272  175 ALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTLAEAEAVGAAFAAALGVAPAT 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 160 AADLRALPADTFWPLTA------PYVTGPAPIAGDIVLPEPMLETFFAARQHPMPVMVGSNSDEASVLAYFG-----VNL 228
Cdd:COG2272  255 LAALRALPAEELLAAQAalaaegPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEGRLFAALLgdlgpLTA 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 229 EEQIRKLRRERRFGLGLIRMLYPGvRGDRELGRQVCRDMAFTTLGFVVMQAQSRRGVPCWRYWFDYVAEGEReTFANGAW 308
Cdd:COG2272  335 ADYRAALRRRFGDDADEVLAAYPA-ASPAEALAALATDRVFRCPARRLAEAHAAAGAPVYLYRFDWRSPPLR-GFGLGAF 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 309 HGNEVPYVFDNLDQVEPLKNyaTAADRAFAGQVADYWVNFARHASAQSqalDGPVRWLACVRGRDRLLRIGLHKKAGwrl 388
Cdd:COG2272  413 HGAELPFVFGNLDAPALTGL--TPADRALSDQMQAYWVNFARTGDPNG---PGLPEWPAYDPEDRAVMVFDAEPRVV--- 484
                        410
                 ....*....|....*.
gi 742403343 389 ENRFMRARLALFKRVM 404
Cdd:COG2272  485 NDPDAEERLDLWDGVV 500
COesterase pfam00135
Carboxylesterase family;
6-390 6.50e-89

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 278.42  E-value: 6.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343    6 ETPLPVMVWLHGGGFTLGAGSLppYDGQALARRG-VVLVTINYRLGHLGFFAhpaLEGEDPAGpvyNFALLDQIAALRWV 84
Cdd:pfam00135 100 KNKLPVMVWIHGGGFMFGSGSL--YDGSYLAAEGdVIVVTINYRLGPLGFLS---TGDDEAPG---NYGLLDQVLALRWV 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   85 QDNIAAFGGDRDNVTLFGESAGARSVLSLMASPLAKGLFHKAIVQSG-----YTLPDIPRRKAllngAALTRHLGLDNPT 159
Cdd:pfam00135 172 QENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGsalspWAIQSNARQRA----KELAKLVGCPTSD 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  160 AAD----LRALPAD-------TFWPLTAPYVTGPAPIAGDIVLPEPMLETFFAARQHPMPVMVGSNSDEASVLAYFGVNl 228
Cdd:pfam00135 248 SAElvecLRSKPAEelldaqlKLLVYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLIGVTKDEGLLFAAYILD- 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  229 EEQIRKLRRERRFGLGLIRMLYPGVRGDRELGRQVCRDM-------------------AFTTLGFVV-----MQAQSRRG 284
Cdd:pfam00135 327 NVDILKALEEKLLRSLLIDLLYLLLVDLPEEISAALREEyldwgdrddpetsrralveLLTDYLFNCpvirfADLHASRG 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  285 VPCWRYWFDYVAEGERETFANGAWHGNEVPYVFDNLdqVEPLKNYaTAADRAFAGQVADYWVNFARHASAQSQAldGPVR 364
Cdd:pfam00135 407 TPVYMYSFDYRGSSLRYPKWVGVDHGDELPYVFGTP--FVGALLF-TEEDEKLSRKMMTYWTNFAKTGNPNGPE--GLPK 481
                         410       420
                  ....*....|....*....|....*.
gi 742403343  365 WLACVRGRDRLLRIGLHKKAGWRLEN 390
Cdd:pfam00135 482 WPPYTDENGQYLSIDLEPRVKQGLKA 507
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
2-351 8.92e-79

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 251.48  E-value: 8.92e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   2 PATRETP--LPVMVWLHGGGFTLGAGSLPPYDGqaLARRG--VVLVTINYRLGHLGFFAHPALEGEDpagpvyNFALLDQ 77
Cdd:cd00312   86 PKNTKPGnsLPVMVWIHGGGFMFGSGSLYPGDG--LAREGdnVIVVSINYRLGVLGFLSTGDIELPG------NYGLKDQ 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  78 IAALRWVQDNIAAFGGDRDNVTLFGESAGARSVLSLMASPLAKGLFHKAIVQSG-YTLPDIPRRKALLNGAALTRHLGLD 156
Cdd:cd00312  158 RLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGsALSPWAIQENARGRAKRLARLLGCN 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 157 NPTAAD----LRALPADTFW-----PLTAPYVtGPAP----IAGDIvLPEPMLETFFAARQHPMPVMVGSNSDEASVLAY 223
Cdd:cd00312  238 DTSSAElldcLRSKSAEELLdatrkLLLFSYS-PFLPfgpvVDGDF-IPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAA 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343 224 FGVNLEEQIRKLRRERRF-------------GLGLIRMLYPGVRGDRELGRQVCRDMaFTTLGF----VVMQAQSRR--G 284
Cdd:cd00312  316 MLLNFDAKLIIETNDRWLellpyllfyaddaLADKVLEKYPGDVDDSVESRKNLSDM-LTDLLFkcpaRYFLAQHRKagG 394
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742403343 285 VPCWRYWFDYVAEG--ERETFANGAWHGNEVPYVFDNLDqvepLKNYATAADRAFAGQVADYWVNFARH 351
Cdd:cd00312  395 SPVYAYVFDHRSSLsvGRWPPWLGTVHGDEIFFVFGNPL----LKEGLREEEEKLSRTMMKYWANFAKT 459
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
2-107 1.23e-15

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 75.29  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   2 PATRETPLPVMVWLHGGGFTLGagSLPPYDGQA---LARRGVVLVTINYRLghlgffahpALEGEDPAgpvynfALLDQI 78
Cdd:COG0657    6 PAGAKGPLPVVVYFHGGGWVSG--SKDTHDPLArrlAARAGAAVVSVDYRL---------APEHPFPA------ALEDAY 68
                         90       100
                 ....*....|....*....|....*....
gi 742403343  79 AALRWVQDNIAAFGGDRDNVTLFGESAGA 107
Cdd:COG0657   69 AALRWLRANAAELGIDPDRIAVAGDSAGG 97
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
2-115 8.10e-15

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: 72.98  E-value: 8.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343    2 PATRETPLPVMVWLHGGGFTLG----AGSLPPYDGQALARRGVVLVTINYRL-GHLGFfahpalegedPAgpvynfALLD 76
Cdd:pfam20434   6 PKNAKGPYPVVIWIHGGGWNSGdkeaDMGFMTNTVKALLKAGYAVASINYRLsTDAKF----------PA------QIQD 69
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 742403343   77 QIAALRWVQDNIAAFGGDRDNVTLFGESAGARsvLSLMA 115
Cdd:pfam20434  70 VKAAIRFLRANAAKYGIDTNKIALMGFSAGGH--LALLA 106
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
12-107 3.55e-11

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: 62.23  E-value: 3.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   12 MVWLHGGGFTLGagSLPPYDGQA--LARR-GVVLVTINYRLghlgffA--HPAlegedPAgpvynfALLDQIAALRWVQD 86
Cdd:pfam07859   1 LVYFHGGGFVLG--SADTHDRLCrrLAAEaGAVVVSVDYRL------ApeHPF-----PA------AYDDAYAALRWLAE 61
                          90       100
                  ....*....|....*....|.
gi 742403343   87 NIAAFGGDRDNVTLFGESAGA 107
Cdd:pfam07859  62 QAAELGADPSRIAVAGDSAGG 82
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
8-133 1.31e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 55.02  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   8 PLPVMVWLHGGGFTLGAGSLPpyDGQALARRGVVLVTINYRlGHlgffahpaleGEDpAGPVYNFALLDQIAALRWVqdn 87
Cdd:COG1506   22 KYPVVVYVHGGPGSRDDSFLP--LAQALASRGYAVLAPDYR-GY----------GES-AGDWGGDEVDDVLAAIDYL--- 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 742403343  88 IAAFGGDRDNVTLFGESAGARSVLSLMAspLAKGLFHKAIVQSGYT 133
Cdd:COG1506   85 AARPYVDPDRIGIYGHSYGGYMALLAAA--RHPDRFKAAVALAGVS 128
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
2-171 1.03e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 46.45  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   2 PATRETPLPVMVWLHGGGFTLGAGSLppYdGQALARRGVVLVTINYRlghlgffAHPALEGEdpagPVY--NFALLDQIA 79
Cdd:COG1073   30 PAGASKKYPAVVVAHGNGGVKEQRAL--Y-AQRLAELGFNVLAFDYR-------GYGESEGE----PREegSPERRDARA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343  80 ALRWVQDNIaafGGDRDNVTLFGESAGARSVLSLMAS-PLAKGLfhkaIVQSGYT-LPDIPR-RKALLNGAALTRHLGLD 156
Cdd:COG1073   96 AVDYLRTLP---GVDPERIGLLGISLGGGYALNAAATdPRVKAV----ILDSPFTsLEDLAAqRAKEARGAYLPGVPYLP 168
                        170
                 ....*....|....*
gi 742403343 157 NPTAADLRALPADTF 171
Cdd:COG1073  169 NVRLASLLNDEFDPL 183
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
3-114 7.22e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 41.25  E-value: 7.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   3 ATRETPLPVMVWLHG-GGFTLGAGSLppydGQALARRGVVLVTINYrLGHLGFFAHPALEGEDPAGPVYNF--------A 73
Cdd:COG4188   56 APAGGPFPLVVLSHGlGGSREGYAYL----AEHLASHGYVVAAPDH-PGSNAADLSAALDGLADALDPEELwerpldlsF 130
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 742403343  74 LLDQIAALrwvQDNIAAFGG--DRDNVTLFGESAGARSVLSLM 114
Cdd:COG4188  131 VLDQLLAL---NKSDPPLAGrlDLDRIGVIGHSLGGYTALALA 170
YpfH COG0400
Predicted esterase [General function prediction only];
6-137 4.48e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.96  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   6 ETPLPVMVWLHGGGFTlgAGSLPPYdGQALARRGVVLVTIN--YRLGHLGF--FAHPALEG-EDPAGPVynfALLDQIAA 80
Cdd:COG0400    2 GPAAPLVVLLHGYGGD--EEDLLPL-APELALPGAAVLAPRapVPEGPGGRawFDLSFLEGrEDEEGLA---AAAEALAA 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 742403343  81 lrWVQDNIAAFGGDRDNVTLFGESAGARSVLSLMASplAKGLFHKAIVQSGYTLPDI 137
Cdd:COG0400   76 --FIDELEARYGIDPERIVLAGFSQGAAMALSLALR--RPELLAGVVALSGYLPGEE 128
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
5-142 6.41e-03

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 38.30  E-value: 6.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742403343   5 RETPLPVMVWLHGGGFT----LGAGSLPP-YDgqALARRG----VVLVTINYRLGhlgffahPALEGEDPAGPVYNFALL 75
Cdd:COG2382  108 PGKKYPVLYLLDGGGGDeqdwFDQGRLPTiLD--NLIAAGkippMIVVMPDGGDG-------GDRGTEGPGNDAFERFLA 178
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742403343  76 DQIaaLRWVQDNiAAFGGDRDNVTLFGESAGARSvlSLMASPLAKGLFHKAIVQSGYTLPDIPRRKA 142
Cdd:COG2382  179 EEL--IPFVEKN-YRVSADPEHRAIAGLSMGGLA--ALYAALRHPDLFGYVGSFSGSFWWPPGDADR 240
 
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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