|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
69-329 |
7.03e-30 |
|
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: 113.94 E-value: 7.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 69 FHVYMAGNEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSvSENELELSLETMSNDVLAVIKELyGDSPP 148
Cdd:COG0596 14 LHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRS-DKPAGGYTLDDLADDLAALLDAL-GLERV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 149 aiVLVGHSMGGSVAVQVAAnkTLPS-LAGLVVVD-VVEgtaissliHMQKILSNRMQHFPSIEKAIEySVRGGSLRNiDS 226
Cdd:COG0596 92 --VLVGHSMGGMVALELAA--RHPErVAGLVLVDeVLA--------ALAEPLRRPGLAPEALAALLR-ALARTDLRE-RL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 227 ARVSIPTtlkyddskhcyvyrtrleeteqywkgwydglsekflsspvpklLLLAGTDrlDRTLTIGQMQ------GKFQM 300
Cdd:COG0596 158 ARITVPT-------------------------------------------LVIWGEK--DPIVPPALARrlaellPNAEL 192
|
250 260
....*....|....*....|....*....
gi 18413291 301 IVVKHTGHAIQEDVPEEFANLVLNFISRN 329
Cdd:COG0596 193 VVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
81-321 |
5.24e-21 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 89.84 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 81 VFCLHGGGYSglsFSIVASKIKEKARVVAMDLRGHGKSVSENeleLSLETMSnDVLAVIKELYGDSPpaIVLVGHSMGGS 160
Cdd:pfam12697 1 VVLVHGAGLS---AAPLAALLAAGVAVLAPDLPGHGSSSPPP---LDLADLA-DLAALLDELGAARP--VVLVGHSLGGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 161 VAVQVAAnktLPSLAGLVVVDVVEGTAisslihMQKILSNRMQHFPSIEKAIEYSVRGGSLRNIdsarvsipttlkYDDS 240
Cdd:pfam12697 72 VALAAAA---AALVVGVLVAPLAAPPG------LLAALLALLARLGAALAAPAWLAAESLARGF------------LDDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 241 KHCYVYRTRLEETEQYWKGWYDGLSEKFLSSPVPkLLLLAGTDRLDRTLT--IGQMQGKFQMIVVKHTGHAIQEDvPEEF 318
Cdd:pfam12697 131 PADAEWAAALARLAALLAALALLPLAAWRDLPVP-VLVLAEEDRLVPELAqrLLAALAGARLVVLPGAGHLPLDD-PEEV 208
|
...
gi 18413291 319 ANL 321
Cdd:pfam12697 209 AEA 211
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
77-168 |
1.46e-11 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 274729 [Multi-domain] Cd Length: 252 Bit Score: 63.77 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 77 EGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENELEL-SLETMSNDVLAVIKELYGDSPpaIVLVGH 155
Cdd:TIGR03695 1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERyDFEEAAQLLLATLLDQLGIEP--FFLVGY 78
|
90
....*....|...
gi 18413291 156 SMGGSVAVQVAAN 168
Cdd:TIGR03695 79 SMGGRIALYYALQ 91
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
75-177 |
3.42e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 63.81 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 75 GNEGPVVFcLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENELElSLETMSNDVLAVIKELygDSPPAIvLVG 154
Cdd:PRK14875 129 GDGTPVVL-IHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAG-SLDELAAAVLAFLDAL--GIERAH-LVG 203
|
90 100 110
....*....|....*....|....*....|
gi 18413291 155 HSMGGSVAVQVAANK-------TLPSLAGL 177
Cdd:PRK14875 204 HSMGGAVALRLAARApqrvaslTLIAPAGL 233
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
127-168 |
5.91e-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: 37.09 E-value: 5.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 18413291 127 SLETMSNDVLAVIKELYGDSPPA-IVLVGHSMGGSVAVQVAAN 168
Cdd:cd00741 6 AARSLANLVLPLLKSALAQYPDYkIHVTGHSLGGALAGLAGLD 48
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
69-329 |
7.03e-30 |
|
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: 113.94 E-value: 7.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 69 FHVYMAGNEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSvSENELELSLETMSNDVLAVIKELyGDSPP 148
Cdd:COG0596 14 LHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRS-DKPAGGYTLDDLADDLAALLDAL-GLERV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 149 aiVLVGHSMGGSVAVQVAAnkTLPS-LAGLVVVD-VVEgtaissliHMQKILSNRMQHFPSIEKAIEySVRGGSLRNiDS 226
Cdd:COG0596 92 --VLVGHSMGGMVALELAA--RHPErVAGLVLVDeVLA--------ALAEPLRRPGLAPEALAALLR-ALARTDLRE-RL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 227 ARVSIPTtlkyddskhcyvyrtrleeteqywkgwydglsekflsspvpklLLLAGTDrlDRTLTIGQMQ------GKFQM 300
Cdd:COG0596 158 ARITVPT-------------------------------------------LVIWGEK--DPIVPPALARrlaellPNAEL 192
|
250 260
....*....|....*....|....*....
gi 18413291 301 IVVKHTGHAIQEDVPEEFANLVLNFISRN 329
Cdd:COG0596 193 VVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
81-321 |
5.24e-21 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 89.84 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 81 VFCLHGGGYSglsFSIVASKIKEKARVVAMDLRGHGKSVSENeleLSLETMSnDVLAVIKELYGDSPpaIVLVGHSMGGS 160
Cdd:pfam12697 1 VVLVHGAGLS---AAPLAALLAAGVAVLAPDLPGHGSSSPPP---LDLADLA-DLAALLDELGAARP--VVLVGHSLGGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 161 VAVQVAAnktLPSLAGLVVVDVVEGTAisslihMQKILSNRMQHFPSIEKAIEYSVRGGSLRNIdsarvsipttlkYDDS 240
Cdd:pfam12697 72 VALAAAA---AALVVGVLVAPLAAPPG------LLAALLALLARLGAALAAPAWLAAESLARGF------------LDDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 241 KHCYVYRTRLEETEQYWKGWYDGLSEKFLSSPVPkLLLLAGTDRLDRTLT--IGQMQGKFQMIVVKHTGHAIQEDvPEEF 318
Cdd:pfam12697 131 PADAEWAAALARLAALLAALALLPLAAWRDLPVP-VLVLAEEDRLVPELAqrLLAALAGARLVVLPGAGHLPLDD-PEEV 208
|
...
gi 18413291 319 ANL 321
Cdd:pfam12697 209 AEA 211
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
49-180 |
1.29e-17 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 80.43 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 49 EWKSYFDKEDDISITGSddvfHVYMAGNEGPVVFCLHGGGYSGLSFSIVASKIKEK-ARVVAMDLRGHGKSVSENELELS 127
Cdd:COG2267 3 RRLVTLPTRDGLRLRGR----RWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 18413291 128 LETMSNDVLAVIKELYGDSPPAIVLVGHSMGGSVAVQVAAnKTLPSLAGLVVV 180
Cdd:COG2267 79 FDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIALLYAA-RYPDRVAGLVLL 130
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
79-313 |
3.53e-17 |
|
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: 79.86 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 79 PVVFCLHGGGYSGLSFSIVASKI-KEKARVVAMDLRGHGKS-VSENELELSLETMSNDVLAvIKELYGDSPpaIVLVGHS 156
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSsRPKAQDDYRTDDLAEDLEY-ILEALGLEK--VNLVGHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 157 MGGSVAVQVAANKTlPSLAGLVVVDVVEGTAisSLIHMQKILSNRMQHFPSIEKAIEYSVRGGSLRNIDSARVSIPTTLK 236
Cdd:pfam00561 78 MGGLIALAYAAKYP-DRVKALVLLGALDPPH--ELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 237 Y---DDSKHCYVYRTRLEETE-----QYWKGWYDGLSEKFLSSP-VPKLLLLAGTDRLDRTLTIGQMQGKF---QMIVVK 304
Cdd:pfam00561 155 KalpLLNKRFPSGDYALAKSLvtgalLFIETWSTELRAKFLGRLdEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIP 234
|
....*....
gi 18413291 305 HTGHAIQED 313
Cdd:pfam00561 235 DAGHFAFLE 243
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
77-168 |
1.46e-11 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 274729 [Multi-domain] Cd Length: 252 Bit Score: 63.77 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 77 EGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENELEL-SLETMSNDVLAVIKELYGDSPpaIVLVGH 155
Cdd:TIGR03695 1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERyDFEEAAQLLLATLLDQLGIEP--FFLVGY 78
|
90
....*....|...
gi 18413291 156 SMGGSVAVQVAAN 168
Cdd:TIGR03695 79 SMGGRIALYYALQ 91
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
75-177 |
3.42e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 63.81 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 75 GNEGPVVFcLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENELElSLETMSNDVLAVIKELygDSPPAIvLVG 154
Cdd:PRK14875 129 GDGTPVVL-IHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAG-SLDELAAAVLAFLDAL--GIERAH-LVG 203
|
90 100 110
....*....|....*....|....*....|
gi 18413291 155 HSMGGSVAVQVAANK-------TLPSLAGL 177
Cdd:PRK14875 204 HSMGGAVALRLAARApqrvaslTLIAPAGL 233
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
80-202 |
2.49e-09 |
|
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: 56.84 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 80 VVFCLHGGG-----YSGLSFSIVASKIKekarVVAMDLRGHGKSVSENELELSLETMSNDVLAV---IKELYGDSPpaIV 151
Cdd:pfam12146 6 VVVLVHGLGehsgrYAHLADALAAQGFA----VYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFvdkIREEHPGLP--LF 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18413291 152 LVGHSMGGSVAVQVAAnKTLPSLAGLVV----VDVVEGTAISSLIHMQKILSNRM 202
Cdd:pfam12146 80 LLGHSMGGLIAALYAL-RYPDKVDGLILsapaLKIKPYLAPPILKLLAKLLGKLF 133
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
74-179 |
5.40e-09 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 56.01 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 74 AGNEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSEnELELSLETMSNDVLAVIKElYGDSPpaIVLV 153
Cdd:COG3208 2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGE-PPLTSLEELADDLAEELAP-LLDRP--FALF 77
|
90 100
....*....|....*....|....*....
gi 18413291 154 GHSMGGSVAVQVAA---NKTLPSLAGLVV 179
Cdd:COG3208 78 GHSMGALLAFELARrleRRGRPLPAHLFV 106
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
72-180 |
1.41e-08 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 54.95 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 72 YMAGNEgPVVFCLHGggYSGLSFSI--VASKIKEK-ARVVAMDLRGHGKSVsENELELSLETMSNDVLAVIKELYGDSPP 148
Cdd:COG1647 10 FLEGGR-KGVLLLHG--FTGSPAEMrpLAEALAKAgYTVYAPRLPGHGTSP-EDLLKTTWEDWLEDVEEAYEILKAGYDK 85
|
90 100 110
....*....|....*....|....*....|..
gi 18413291 149 aIVLVGHSMGGSVAVQVAANktLPSLAGLVVV 180
Cdd:COG1647 86 -VIVIGLSMGGLLALLLAAR--YPDVAGLVLL 114
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
79-170 |
1.43e-08 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 54.64 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 79 PVVFCLHGGGYS-GLSFSIVASKIkekAR----VVAMDLRGHGKSVSENELElsletMSNDVLAVIKEL----YGDsPPA 149
Cdd:COG1506 24 PVVVYVHGGPGSrDDSFLPLAQAL---ASrgyaVLAPDYRGYGESAGDWGGD-----EVDDVLAAIDYLaarpYVD-PDR 94
|
90 100
....*....|....*....|.
gi 18413291 150 IVLVGHSMGGSVAVQVAANKT 170
Cdd:COG1506 95 IGIYGHSYGGYMALLAAARHP 115
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
74-167 |
7.21e-08 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 54.32 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 74 AGNEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGksvSENELELSLETMSNDVLAVIKELYGDSPpaIVLV 153
Cdd:COG3319 597 AGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLD---GGEPPPASVEEMAARYVEAIRAVQPEGP--YHLL 671
|
90
....*....|....
gi 18413291 154 GHSMGGSVAVQVAA 167
Cdd:COG3319 672 GWSFGGLVAYEMAR 685
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
54-180 |
8.15e-08 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 52.61 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 54 FDKEDDISITGsddvfHVYMAGNEG---PVVFCLHGGGYSGLSFSIVASKIkekAR----VVAMDLRGHGKSVSENELEL 126
Cdd:COG1073 15 FKSRDGIKLAG-----DLYLPAGASkkyPAVVVAHGNGGVKEQRALYAQRL---AElgfnVLAFDYRGYGESEGEPREEG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 18413291 127 SLETmsNDVLAVIKEL--YGDSPPA-IVLVGHSMGGSVAVQVAAnkTLPSLAGLVVV 180
Cdd:COG1073 87 SPER--RDARAAVDYLrtLPGVDPErIGLLGISLGGGYALNAAA--TDPRVKAVILD 139
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
56-178 |
1.58e-07 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 51.51 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 56 KEDDISITGSDDVF---HVYMAGNEGP---VVFcLHGGGysGLSfsivaSKIKEKAR--------VVAMDLRGHGKSVSE 121
Cdd:COG0412 2 TTETVTIPTPDGVTlpgYLARPAGGGPrpgVVV-LHEIF--GLN-----PHIRDVARrlaaagyvVLAPDLYGRGGPGDD 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18413291 122 NE------LELSLETMSNDVLAVI---KELYGDSPPAIVLVGHSMGGSVAVQVAAnkTLPSLAGLV 178
Cdd:COG0412 74 PDearalmGALDPELLAADLRAALdwlKAQPEVDAGRVGVVGFCFGGGLALLAAA--RGPDLAAAV 137
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
79-167 |
3.76e-07 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 50.46 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 79 PVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENElelSLETMSNDVLAVIKELYGDSPpaIVLVGHSMG 158
Cdd:pfam00975 1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLN---SIEALADEYAEALRQIQPEGP--YALFGHSMG 75
|
....*....
gi 18413291 159 GSVAVQVAA 167
Cdd:pfam00975 76 GMLAFEVAR 84
|
|
| PRK05855 |
PRK05855 |
SDR family oxidoreductase; |
61-178 |
4.44e-07 |
|
SDR family oxidoreductase;
Pssm-ID: 235628 [Multi-domain] Cd Length: 582 Bit Score: 51.52 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 61 SITGSDDV-FHVYMAGN-EGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENELE-LSLETMSNDVLA 137
Cdd:PRK05855 6 TVVSSDGVrLAVYEWGDpDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAaYTLARLADDFAA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 18413291 138 VIKELygdSPPAIV-LVGHSMGgsvAVQVAANKTLPSLAGLV 178
Cdd:PRK05855 86 VIDAV---SPDRPVhLLAHDWG---SIQGWEAVTRPRAAGRI 121
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
74-179 |
4.67e-07 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 49.52 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 74 AGNEGPVVFCLHGGGYSGLSF-SIVASKIKEKARVVA--------------MDLRGHGKSVSENELELSLETMsNDVLAV 138
Cdd:COG0400 1 GGPAAPLVVLLHGYGGDEEDLlPLAPELALPGAAVLAprapvpegpggrawFDLSFLEGREDEEGLAAAAEAL-AAFIDE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 18413291 139 IKELYGDSPPAIVLVGHSMGGSVAVQVAAnkTLP-SLAGLVV 179
Cdd:COG0400 80 LEARYGIDPERIVLAGFSQGAAMALSLAL--RRPeLLAGVVA 119
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
76-168 |
9.95e-07 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 50.63 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 76 NEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKS-----VSENELE--LSLETMSNDVLAVIKELygdSPP 148
Cdd:PLN02980 1369 AEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhAKETQTEptLSVELVADLLYKLIEHI---TPG 1445
|
90 100
....*....|....*....|
gi 18413291 149 AIVLVGHSMGGSVAVQVAAN 168
Cdd:PLN02980 1446 KVTLVGYSMGARIALYMALR 1465
|
|
| PRK10673 |
PRK10673 |
esterase; |
76-182 |
7.99e-06 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 46.65 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 76 NEGPVVFcLHG--GGYSGLSfsIVASKIKEKARVVAMDLRGHGKSVSENELELSleTMSNDVLAVIKELygdSPPAIVLV 153
Cdd:PRK10673 15 NNSPIVL-VHGlfGSLDNLG--VLARDLVNDHDIIQVDMRNHGLSPRDPVMNYP--AMAQDLLDTLDAL---QIEKATFI 86
|
90 100 110
....*....|....*....|....*....|
gi 18413291 154 GHSMGGSVAVQVAAnkTLPS-LAGLVVVDV 182
Cdd:PRK10673 87 GHSMGGKAVMALTA--LAPDrIDKLVAIDI 114
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
78-178 |
1.73e-05 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 78 GPVVFCLHGGGYSGLSFSI---VASKIKEK--ARVVAMDLRghgksvseneleLSLE----TMSNDVLAVIKEL------ 142
Cdd:COG0657 13 LPVVVYFHGGGWVSGSKDThdpLARRLAARagAAVVSVDYR------------LAPEhpfpAALEDAYAALRWLranaae 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 18413291 143 YGDSPPAIVLVGHSMGGSVAVQVAA---NKTLPSLAGLV 178
Cdd:COG0657 81 LGIDPDRIAVAGDSAGGHLAAALALrarDRGGPRPAAQV 119
|
|
| YheT |
COG0429 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
106-180 |
2.06e-05 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 440198 [Multi-domain] Cd Length: 323 Bit Score: 45.90 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 106 RVVAMDLRGHGKsvsenELELSLETM----SNDVLAVI---KELYGDSPpaIVLVGHSMGGSVAVQVAA--NKTLPSLAG 176
Cdd:COG0429 92 DVVRLNFRGCGG-----EPNLLPRLYhsgdTEDLVWVLahlRARYPYAP--LYAVGFSLGGNLLLKYLGeqGDDAPPLKA 164
|
....
gi 18413291 177 LVVV 180
Cdd:COG0429 165 AVAV 168
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
78-185 |
3.64e-05 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 44.44 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 78 GPVVFCLHGGGYSGLSFSIVASKIKEKARVVaMDLRGHGKSVSeneLELS-LETMSNDVLAVIKElYGDSPpaIVLVGHS 156
Cdd:PRK11126 2 LPWLVFLHGLLGSGQDWQPVGEALPDYPRLY-IDLPGHGGSAA---ISVDgFADVSRLLSQTLQS-YNILP--YWLVGYS 74
|
90 100
....*....|....*....|....*....
gi 18413291 157 MGGSVAVQVAANKTLPSLAGLvvvdVVEG 185
Cdd:PRK11126 75 LGGRIAMYYACQGLAGGLCGL----IVEG 99
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
79-168 |
5.84e-05 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 41.74 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 79 PVVFcLHG-GGySGLSFSIVASKIKEK-ARVVAMDLRGHGKSVSENELELSletmsnDVLAVIKELYGDSPpaIVLVGHS 156
Cdd:COG1075 7 PVVL-VHGlGG-SAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDSAEQLA------AFVDAVLAATGAEK--VDLVGHS 76
|
90
....*....|..
gi 18413291 157 MGGSVAVQVAAN 168
Cdd:COG1075 77 MGGLVARYYLKR 88
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
75-203 |
1.96e-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: 42.50 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 75 GNEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENelELSLETMSNDVLAVIKElygdspPAIVLvG 154
Cdd:TIGR01738 1 GQGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFG--PLSLADMAEAIAAQAPD------PAIWL-G 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 155 HSMGGSVAVQVAAnkTLPS-LAGLVVV----------DVVEGTAISSLIHMQKILSNRMQ 203
Cdd:TIGR01738 72 WSLGGLVALHIAA--THPDrVRALVTVasspcfsareDWPEGIKPDVLTGFQQQLSDDYQ 129
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
72-167 |
2.21e-04 |
|
Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
Pssm-ID: 395613 [Multi-domain] Cd Length: 246 Bit Score: 42.06 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 72 YMAGNEGPVVFCLHGGGY-------SGLSFSIVASKIkEKARVVAMDLRGHGKSVSENELEL---SLETMSNDVLAVIKE 141
Cdd:pfam00756 18 YPPGRKYPVLYLLDGTGWfqngpakEGLDRLAASGEI-PPVIIVGSPRGGEVSFYSDWDRGLnatEGPGAYAYETFLTQE 96
|
90 100 110
....*....|....*....|....*....|...
gi 18413291 142 L-------YGDSPPAIVLVGHSMGGSVAVQVAA 167
Cdd:pfam00756 97 LpplldanFPTAPDGRALAGQSMGGLGALYLAL 129
|
|
| PLN02578 |
PLN02578 |
hydrolase |
72-181 |
2.33e-04 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 42.52 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 72 YMAGNEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHG---KSVSENELELSLETMSNDVLAVIKElygdspP 148
Cdd:PLN02578 80 YVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGwsdKALIEYDAMVWRDQVADFVKEVVKE------P 153
|
90 100 110
....*....|....*....|....*....|....
gi 18413291 149 AiVLVGHSMGGSVAVQVAAnkTLPSL-AGLVVVD 181
Cdd:PLN02578 154 A-VLVGNSLGGFTALSTAV--GYPELvAGVALLN 184
|
|
| COG2945 |
COG2945 |
Alpha/beta superfamily hydrolase [General function prediction only]; |
107-180 |
2.52e-04 |
|
Alpha/beta superfamily hydrolase [General function prediction only];
Pssm-ID: 442188 [Multi-domain] Cd Length: 201 Bit Score: 41.69 E-value: 2.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18413291 107 VVAMDLRGHGKS---VSENELELSletmsnDVLAVIKELYGDSPPAIVLVGHSMGGSVAVQVAAnkTLPSLAGLVVV 180
Cdd:COG2945 58 VLRFNFRGVGRSegeFDEGRGELD------DAAAALDWLRAQNPLPLWLAGFSFGAYVALQLAM--RLPEVEGLILV 126
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
74-182 |
2.74e-04 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 42.03 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 74 AGNEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENELEL------SLETMSNDVLAVIKELYGDsp 147
Cdd:PLN02824 25 AGTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSAppnsfyTFETWGEQLNDFCSDVVGD-- 102
|
90 100 110
....*....|....*....|....*....|....*
gi 18413291 148 PAIVlVGHSMGGSVAVQVAANKTlPSLAGLVVVDV 182
Cdd:PLN02824 103 PAFV-ICNSVGGVVGLQAAVDAP-ELVRGVMLINI 135
|
|
| COG4757 |
COG4757 |
Predicted alpha/beta hydrolase [General function prediction only]; |
106-180 |
1.05e-03 |
|
Predicted alpha/beta hydrolase [General function prediction only];
Pssm-ID: 443790 [Multi-domain] Cd Length: 289 Bit Score: 40.25 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 106 RVVAMDLRGHGKSVSEN--ELELSL-ETMSND---VLAVIKELYGDSPpaIVLVGHSMGGsvaVQVAANKTLPSLAGLVV 179
Cdd:COG4757 61 AVLTYDYRGIGLSRPGSlrGFDAGYrDWGELDlpaVLDALRARFPGLP--LLLVGHSLGG---QLLGLAPNAERVDRLVT 135
|
.
gi 18413291 180 V 180
Cdd:COG4757 136 V 136
|
|
| PLN02408 |
PLN02408 |
phospholipase A1 |
120-180 |
1.16e-03 |
|
phospholipase A1
Pssm-ID: 215228 Cd Length: 365 Bit Score: 40.59 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18413291 120 SENELELSLETMSNDVLAVIKELYGDSPPAIVLVGHSMGGSVAVQVAAN-KTLPSLAGLVVV 180
Cdd:PLN02408 172 SGTAMGPSLQEMVREEIARLLQSYGDEPLSLTITGHSLGAALATLTAYDiKTTFKRAPMVTV 233
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
80-167 |
1.20e-03 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 40.25 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 80 VVFCLHGGGYSGLSFSIVASKI-KEKARVVAMDLRGHGKSVSENELELSLETMSNDVL---AVIKELYGDSPpaIVLVGH 155
Cdd:PHA02857 27 LVFISHGAGEHSGRYEELAENIsSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVqhvVTIKSTYPGVP--VFLLGH 104
|
90
....*....|..
gi 18413291 156 SMGGSVAVQVAA 167
Cdd:PHA02857 105 SMGATISILAAY 116
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
79-162 |
2.62e-03 |
|
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: 38.88 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413291 79 PVVFcLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGK------SVSENElELSL---ETMS------NDVLAVIKELY 143
Cdd:pfam07819 6 PVLF-IPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNGfhldffSVDFNE-ELSAfhgRTLLdqaeylNDAIRYILSLY 83
|
90 100
....*....|....*....|..
gi 18413291 144 GDS---PPAIVLVGHSMGGSVA 162
Cdd:pfam07819 84 ASGrpgPTSVILIGHSMGGIVA 105
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
127-168 |
5.91e-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: 37.09 E-value: 5.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 18413291 127 SLETMSNDVLAVIKELYGDSPPA-IVLVGHSMGGSVAVQVAAN 168
Cdd:cd00741 6 AARSLANLVLPLLKSALAQYPDYkIHVTGHSLGGALAGLAGLD 48
|
|
| PRK00870 |
PRK00870 |
haloalkane dehalogenase; Provisional |
302-330 |
6.13e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179147 [Multi-domain] Cd Length: 302 Bit Score: 38.03 E-value: 6.13e-03
10 20
....*....|....*....|....*....
gi 18413291 302 VVKHTGHAIQEDVPEEFANLVLNFISRNR 330
Cdd:PRK00870 274 TIKGAGHFLQEDSGEELAEAVLEFIRATP 302
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
127-163 |
8.10e-03 |
|
Lipase (class 3). 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: 238287 [Multi-domain] Cd Length: 229 Bit Score: 37.46 E-value: 8.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 18413291 127 SLETMSNDVLAVIKELYGDSPPA-IVLVGHSMGGSVAV 163
Cdd:cd00519 106 AYKSLYNQVLPELKSALKQYPDYkIIVTGHSLGGALAS 143
|
|
| |
