|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
54-387 |
3.05e-56 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 191.66 E-value: 3.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 54 LWKWLCNWTSSSPTMLRAVEKKILSYVKLPYRGFFVDIG------------PAVGEADKIWTISMNTESKEVPLVLLHGL 121
Cdd:PLN02894 35 LWPSPLRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGsgppgskvrwfrSASNEPRFINTVTFDSKEDAPTLVMVHGY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 122 GAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLF-AKDALVCEKQFVKSVEEWRREMNINDMILLGHSMGGFIASSYA 200
Cdd:PLN02894 115 GASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFtCKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 201 LSHPERVKHLILADPWGFPEKPSDSTNG--KTIPLWVRAIARVLTPLN--PLWALRAAGPFGQWVVQKTrpdIMRKFQST 276
Cdd:PLN02894 195 LKHPEHVQHLILVGPAGFSSESDDKSEWltKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRY---TTARFGAH 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 277 ------IEEDINLLPQYIHQCNAQNPSGESAFHTMMQSFGWAKHPMIHRIKDVRsdIPITFIYGSRSWIDsSSGEKIKSQ 350
Cdd:PLN02894 272 stgdilSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMN-YEGAVEARK 348
|
330 340 350
....*....|....*....|....*....|....*..
gi 24586385 351 RGSNMVDIKIVTGAGHHVYADKPDVFNRYVNETCDMY 387
Cdd:PLN02894 349 RMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYACRKY 385
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
114-382 |
5.55e-26 |
|
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: 105.08 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPlfakDALVCEKQFVKSVEEWRREMNINDMILLGHSMGG 193
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP----AGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 194 FIASSYALSHPERVKHLILADPwgfpekpsdstngktiplWVRAIARVLtplnplwalraagpfgqwvvqktrpdimrkf 273
Cdd:COG0596 101 MVALELAARHPERVAGLVLVDE------------------VLAALAEPL------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 274 qstieedinllpqyihqcnAQNPSGESAFHTMMQSF-GWAKHPMIHRIkdvrsDIPITFIYGSRS-WIDSSSGEKIKSQ- 350
Cdd:COG0596 132 -------------------RRPGLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELl 187
|
250 260 270
....*....|....*....|....*....|..
gi 24586385 351 RGSNMVDIKivtGAGHHVYADKPDVFNRYVNE 382
Cdd:COG0596 188 PNAELVVLP---GAGHFPPLEQPEAFAAALRD 216
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
114-373 |
5.85e-24 |
|
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: 100.27 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAKDalVCEKQFVKSVEEWRREMNINDMILLGHSMG 192
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKAQDD--YRTDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 193 GFIASSYALSHPERVKHLILADPWGFPEKPSD--STNGKTIPLWVRAIARVL--TPLNPLWALRAAGPFGQWVVQKTRPD 268
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEadRFILALFPGFFDGFVADFapNPLGRLVAKLLALLLLRLRLLKALPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 269 IMRKFQSTIEEDINLLPQYIHQCNAQnpsgesafhtmmqsfgWAKHPMIHRIkdVRSDIPITFIYGSRSWIDSSSGeKIK 348
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVTGALLFIET----------------WSTELRAKFL--GRLDEPTLIIWGDQDPLVPPQA-LEK 220
|
250 260
....*....|....*....|....*
gi 24586385 349 SQRGSNMVDIKIVTGAGHHVYADKP 373
Cdd:pfam00561 221 LAQLFPNARLVVIPDAGHFAFLEGP 245
|
|
| pro_imino_pep_2 |
TIGR01250 |
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ... |
100-247 |
3.67e-19 |
|
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase
Pssm-ID: 188121 [Multi-domain] Cd Length: 289 Bit Score: 87.44 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 100 KIWTISMNTESKeVPLVLLHGLGAGIALWVMNLDAFAK--GRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRR 177
Cdd:TIGR01250 14 HLFTKTGGEGEK-IKLLLLHGGPGMSHEYLENLRELLKeeGREVIMYDQLGCGYSDQPDDSDEELWTIDYFVDELEEVRE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 178 EMNINDMILLGHSMGGFIASSYALSHPERVKHLILADpwgfpekPSDStngktIPLWVRAIARVLTPLNP 247
Cdd:TIGR01250 93 KLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISS-------MLDS-----APEYVKELNRLRKELPP 150
|
|
| Esterase_713_like |
cd12806 |
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ... |
109-235 |
6.15e-04 |
|
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown. This enzyme is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.
Pssm-ID: 214005 Cd Length: 261 Bit Score: 41.36 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 109 ESKEVPLVLLHGLGAGIALWVMNLDA--------FAKGRPVYAMDILGFGRSSR----PLFAKDAlvcekQFVKSVEEWR 176
Cdd:cd12806 45 RAKRYPLLLIHGCGLTGMTWETTPDGrmgwdnyfLRKGYSVYVVDQPGRGRSGWdtqfPVQGQAE-----LWQQMVPDWL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586385 177 REMNINDM---------------ILLGHSMGGFIASSYALSHPERVKHLILADPWGFPeKPSDSTNGKTIPLWV 235
Cdd:cd12806 120 GAMPTPNPtvaalskladkldptVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCP-KPEDVKPLTSIPVLV 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
54-387 |
3.05e-56 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 191.66 E-value: 3.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 54 LWKWLCNWTSSSPTMLRAVEKKILSYVKLPYRGFFVDIG------------PAVGEADKIWTISMNTESKEVPLVLLHGL 121
Cdd:PLN02894 35 LWPSPLRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGsgppgskvrwfrSASNEPRFINTVTFDSKEDAPTLVMVHGY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 122 GAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLF-AKDALVCEKQFVKSVEEWRREMNINDMILLGHSMGGFIASSYA 200
Cdd:PLN02894 115 GASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFtCKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 201 LSHPERVKHLILADPWGFPEKPSDSTNG--KTIPLWVRAIARVLTPLN--PLWALRAAGPFGQWVVQKTrpdIMRKFQST 276
Cdd:PLN02894 195 LKHPEHVQHLILVGPAGFSSESDDKSEWltKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRY---TTARFGAH 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 277 ------IEEDINLLPQYIHQCNAQNPSGESAFHTMMQSFGWAKHPMIHRIKDVRsdIPITFIYGSRSWIDsSSGEKIKSQ 350
Cdd:PLN02894 272 stgdilSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMN-YEGAVEARK 348
|
330 340 350
....*....|....*....|....*....|....*..
gi 24586385 351 RGSNMVDIKIVTGAGHHVYADKPDVFNRYVNETCDMY 387
Cdd:PLN02894 349 RMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYACRKY 385
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
114-382 |
5.55e-26 |
|
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: 105.08 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPlfakDALVCEKQFVKSVEEWRREMNINDMILLGHSMGG 193
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP----AGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 194 FIASSYALSHPERVKHLILADPwgfpekpsdstngktiplWVRAIARVLtplnplwalraagpfgqwvvqktrpdimrkf 273
Cdd:COG0596 101 MVALELAARHPERVAGLVLVDE------------------VLAALAEPL------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 274 qstieedinllpqyihqcnAQNPSGESAFHTMMQSF-GWAKHPMIHRIkdvrsDIPITFIYGSRS-WIDSSSGEKIKSQ- 350
Cdd:COG0596 132 -------------------RRPGLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELl 187
|
250 260 270
....*....|....*....|....*....|..
gi 24586385 351 RGSNMVDIKivtGAGHHVYADKPDVFNRYVNE 382
Cdd:COG0596 188 PNAELVVLP---GAGHFPPLEQPEAFAAALRD 216
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
114-373 |
5.85e-24 |
|
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: 100.27 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAKDalVCEKQFVKSVEEWRREMNINDMILLGHSMG 192
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKAQDD--YRTDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 193 GFIASSYALSHPERVKHLILADPWGFPEKPSD--STNGKTIPLWVRAIARVL--TPLNPLWALRAAGPFGQWVVQKTRPD 268
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEadRFILALFPGFFDGFVADFapNPLGRLVAKLLALLLLRLRLLKALPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 269 IMRKFQSTIEEDINLLPQYIHQCNAQnpsgesafhtmmqsfgWAKHPMIHRIkdVRSDIPITFIYGSRSWIDSSSGeKIK 348
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVTGALLFIET----------------WSTELRAKFL--GRLDEPTLIIWGDQDPLVPPQA-LEK 220
|
250 260
....*....|....*....|....*
gi 24586385 349 SQRGSNMVDIKIVTGAGHHVYADKP 373
Cdd:pfam00561 221 LAQLFPNARLVVIPDAGHFAFLEGP 245
|
|
| pro_imino_pep_2 |
TIGR01250 |
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ... |
100-247 |
3.67e-19 |
|
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase
Pssm-ID: 188121 [Multi-domain] Cd Length: 289 Bit Score: 87.44 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 100 KIWTISMNTESKeVPLVLLHGLGAGIALWVMNLDAFAK--GRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRR 177
Cdd:TIGR01250 14 HLFTKTGGEGEK-IKLLLLHGGPGMSHEYLENLRELLKeeGREVIMYDQLGCGYSDQPDDSDEELWTIDYFVDELEEVRE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 178 EMNINDMILLGHSMGGFIASSYALSHPERVKHLILADpwgfpekPSDStngktIPLWVRAIARVLTPLNP 247
Cdd:TIGR01250 93 KLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISS-------MLDS-----APEYVKELNRLRKELPP 150
|
|
| PLN02578 |
PLN02578 |
hydrolase |
109-378 |
3.93e-18 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 85.28 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 109 ESKEVPLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLFAKDALVCEKQfvksVEEWRREMNINDMILLG 188
Cdd:PLN02578 83 QGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQ----VADFVKEVVKEPAVLVG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 189 HSMGGFIASSYALSHPERVKHLILADPWGFPEKPSDSTNGKTIPLWVRAIARVLTPLNPlWALRAAGPFGQWvvQKTRPD 268
Cdd:PLN02578 159 NSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAIVVEETVLTRFVVKPLKE-WFQRVVLGFLFW--QAKQPS 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 269 IMRKFQSTIEEDINLLPQYIHQC---NAQNPSGESAFHTMMQSFgwAKHPMIHRIKDVRSDI--PITFIYG-SRSWIDSS 342
Cdd:PLN02578 236 RIESVLKSVYKDKSNVDDYLVESitePAADPNAGEVYYRLMSRF--LFNQSRYTLDSLLSKLscPLLLLWGdLDPWVGPA 313
|
250 260 270
....*....|....*....|....*....|....*..
gi 24586385 343 SGEKIKS-QRGSNMVDIKivtgAGHHVYADKPDVFNR 378
Cdd:PLN02578 314 KAEKIKAfYPDTTLVNLQ----AGHCPHDEVPEQVNK 346
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
114-245 |
6.68e-18 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 82.36 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAKDALvceKQFVKSVEEWRREMNIN---DMILLGH 189
Cdd:COG2267 30 TVVLVHGLGEHSGRYAELAEALAAaGYAVLAFDLRGHGRSDGPRGHVDSF---DDYVDDLRAALDALRARpglPVVLLGH 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24586385 190 SMGGFIASSYALSHPERVKHLILADPWGFPEKPSDSTNGKTIPLWV-RAIARVLTPL 245
Cdd:COG2267 107 SMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRALRLaEALARIDVPV 163
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
109-228 |
1.99e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 80.37 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 109 ESKEVPLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLFAKDALvcekQFVKSVEEWRREMNINDMILLG 188
Cdd:PRK14875 128 EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLD----ELAAAVLAFLDALGIERAHLVG 203
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24586385 189 HSMGGFIASSYALSHPERVKHLILADPWGF-PEKPSDSTNG 228
Cdd:PRK14875 204 HSMGGAVALRLAARAPQRVASLTLIAPAGLgPEINGDYIDG 244
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
115-268 |
4.32e-15 |
|
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: 74.56 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 115 LVLLHGLG------AGIAlwvmnlDAFAK-GRPVYAMDILGFGRSSRP--------LFAKDAlvceKQFV-KSVEEWRRE 178
Cdd:pfam12146 7 VVLVHGLGehsgryAHLA------DALAAqGFAVYAYDHRGHGRSDGKrghvpsfdDYVDDL----DTFVdKIREEHPGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 179 mninDMILLGHSMGGFIASSYALSHPERVKHLILADPWGFPEKPSdstngktIPLWVRAIARVLTPLNPLWALRAAGPFG 258
Cdd:pfam12146 77 ----PLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYL-------APPILKLLAKLLGKLFPRLRVPNNLLPD 145
|
170
....*....|....*
gi 24586385 259 -----QWVVQKTRPD 268
Cdd:pfam12146 146 slsrdPEVVAAYAAD 160
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
115-378 |
3.30e-10 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 59.79 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 115 LVLLHGLGAGIALWvmnLDAFAKGRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRREmnindmILLGHSMGGF 194
Cdd:pfam12697 1 VVLVHGAGLSAAPL---AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV------VLVGHSLGGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 195 IASSYAlshPERVKHLILADPWGFPekpsdstngktiPLWVRAIARVLTPLNPLWALRAagpfgqWVVQKTRPDIMrkfq 274
Cdd:pfam12697 72 VALAAA---AAALVVGVLVAPLAAP------------PGLLAALLALLARLGAALAAPA------WLAAESLARGF---- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 275 stieedinllpqyiHQCNAQNPSGESAFHTMMQSFGWAKHPMIHRIKDVRSdiPITFIYGSRSWIDSSSGEKIKSQRGsn 354
Cdd:pfam12697 127 --------------LDDLPADAEWAAALARLAALLAALALLPLAAWRDLPV--PVLVLAEEDRLVPELAQRLLAALAG-- 188
|
250 260
....*....|....*....|....
gi 24586385 355 mVDIKIVTGAGHHVYaDKPDVFNR 378
Cdd:pfam12697 189 -ARLVVLPGAGHLPL-DDPEEVAE 210
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
114-211 |
6.16e-10 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 56.38 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAkdalvcekQFVKSVEEWRREMNINDMILLGHSMG 192
Cdd:COG1075 7 PVVLVHGLGGSAASWAPLAPRLRAaGYPVYALNYPSTNGSIEDSAE--------QLAAFVDAVLAATGAEKVDLVGHSMG 78
|
90 100
....*....|....*....|.
gi 24586385 193 GFIASSYA--LSHPERVKHLI 211
Cdd:COG1075 79 GLVARYYLkrLGGAAKVARVV 99
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
114-212 |
1.43e-08 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 56.39 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPlfakdalvceKQFVKSVEEWR-------REMNINDMIL 186
Cdd:PLN02679 90 PVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKP----------PGFSYTMETWAelildflEEVVQKPTVL 159
|
90 100
....*....|....*....|....*....
gi 24586385 187 LGHSMGGF---IASSYalSHPERVKHLIL 212
Cdd:PLN02679 160 IGNSVGSLacvIAASE--STRDLVRGLVL 186
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
116-378 |
1.91e-08 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 54.95 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 116 VLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAKDAlvceKQFVKSVEEwrrEMNI-----NDMILLGH 189
Cdd:COG1647 19 LLLHGFTGSPAEMRPLAEALAKaGYTVYAPRLPGHGTSPEDLLKTTW----EDWLEDVEE---AYEIlkagyDKVIVIGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 190 SMGGFIASSYALSHPErVKHLILADPwgfpekpsdstngktiPLWVRAIARVLTplnplwalraagPFGQWVVQKtrpdi 269
Cdd:COG1647 92 SMGGLLALLLAARYPD-VAGLVLLSP----------------ALKIDDPSAPLL------------PLLKYLARS----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 270 MRKFQSTIEEdinllPQYIHQCNAQNPSgeSAFHTMMQSFGWAKHPmIHRIKdvrsdIPITFIYGSR-SWIDSSSGEKIK 348
Cdd:COG1647 138 LRGIGSDIED-----PEVAEYAYDRTPL--RALAELQRLIREVRRD-LPKIT-----APTLIIQSRKdEVVPPESARYIY 204
|
250 260 270
....*....|....*....|....*....|..
gi 24586385 349 SQRGSNMVDIKIVTGAGH--HVYADKPDVFNR 378
Cdd:COG1647 205 ERLGSPDKELVWLEDSGHviTLDKDREEVAEE 236
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
114-215 |
8.57e-08 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 53.59 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPlfakDALVCEKQFVKSVEEWRREMN--INDMI-----L 186
Cdd:PLN02824 31 ALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP----NPRSAPPNSFYTFETWGEQLNdfCSDVVgdpafV 106
|
90 100
....*....|....*....|....*....
gi 24586385 187 LGHSMGGFIASSYALSHPERVKHLILADP 215
Cdd:PLN02824 107 ICNSVGGVVGLQAAVDAPELVRGVMLINI 135
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
114-260 |
8.79e-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: 54.71 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGaGIALWVMNL-DAFAKGRPVYAMDILGFGRSSRPLfakdalvcekqfvKSVEEWRREMnINDM-------- 184
Cdd:COG3319 603 PLFCVHPAG-GNVLCYRPLaRALGPDRPVYGLQAPGLDGGEPPP-------------ASVEEMAARY-VEAIravqpegp 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 185 -ILLGHSMGGFIAssYALSH-----PERVKHLILADPWGfPEKPSDSTNGKTIPLWVRAIARVLTPLNPLWALRAAGPFG 258
Cdd:COG3319 668 yHLLGWSFGGLVA--YEMARqleaqGEEVALLVLLDSYA-PGALARLDEAELLAALLRDLARGVDLPLDAEELRALDPEE 744
|
..
gi 24586385 259 QW 260
Cdd:COG3319 745 RL 746
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
115-212 |
9.18e-08 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 52.22 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 115 LVLLHGLGA------GIALWVMNLDAF-----AKGRPVYAM----DILGFGRSSRPLFAKDALvceKQFVKSVEEWRREM 179
Cdd:COG0400 8 VVLLHGYGGdeedllPLAPELALPGAAvlaprAPVPEGPGGrawfDLSFLEGREDEEGLAAAA---EALAAFIDELEARY 84
|
90 100 110
....*....|....*....|....*....|....*
gi 24586385 180 NIND--MILLGHSMGGFIASSYALSHPERVKHLIL 212
Cdd:COG0400 85 GIDPerIVLAGFSQGAAMALSLALRRPELLAGVVA 119
|
|
| PRK10673 |
PRK10673 |
esterase; |
114-382 |
1.04e-07 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 52.81 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGL-GAGIALWVMNLDaFAKGRPVYAMDILGFGRSSR------PLFAKDALvcekqfvksveEWRREMNINDMIL 186
Cdd:PRK10673 18 PIVLVHGLfGSLDNLGVLARD-LVNDHDIIQVDMRNHGLSPRdpvmnyPAMAQDLL-----------DTLDALQIEKATF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 187 LGHSMGGFIASSYALSHPERVKHLILADPwgfpeKPSDSTngktiplwVRAIARVLTPLNplwALRAAGpfgqwVVQKTR 266
Cdd:PRK10673 86 IGHSMGGKAVMALTALAPDRIDKLVAIDI-----APVDYH--------VRRHDEIFAAIN---AVSEAG-----ATTRQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 267 P-DIMRKfqsTIEED--INLLPQYIHQcnaqnpsGESAFH--TMMQSF----GWAKHPMIHRikdvrsdiPITFIYGSRS 337
Cdd:PRK10673 145 AaAIMRQ---HLNEEgvIQFLLKSFVD-------GEWRFNvpVLWDQYphivGWEKIPAWPH--------PALFIRGGNS 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 24586385 338 -WIDSSSGEKIKSQ----RGsnmvdiKIVTGAGHHVYADKPD----VFNRYVNE 382
Cdd:PRK10673 207 pYVTEAYRDDLLAQfpqaRA------HVIAGAGHWVHAEKPDavlrAIRRYLND 254
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
113-211 |
5.52e-07 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 50.79 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 113 VPLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSrplfAKDALVCEKQFVKSVEEwrremNINDMILLGHSMG 192
Cdd:PRK10349 14 VHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR----GFGALSLADMAEAVLQQ-----APDKAIWLGWSLG 84
|
90
....*....|....*....
gi 24586385 193 GFIASSYALSHPERVKHLI 211
Cdd:PRK10349 85 GLVASQIALTHPERVQALV 103
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
114-371 |
2.01e-06 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 49.88 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRREMNINDMILLGHSMGG 193
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQGYFS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 194 FIASSYALSHPERVKHLILADPwgfPEKPSDSTNGKTIPLWVRAIARVLTPLNPLWA----LRAAGPFgqwvvQKTRPDI 269
Cdd:PLN03084 209 PPVVKYASAHPDKIKKLILLNP---PLTKEHAKLPSTLSEFSNFLLGEIFSQDPLRAsdkaLTSCGPY-----AMKEDDA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 270 M--RKfqstieedinllpQYIhqcnaqnPSGESAF--HTMMQSFgwaKHPMIHRIKDVRS-------DIPITFIYGSRS- 337
Cdd:PLN03084 281 MvyRR-------------PYL-------TSGSSGFalNAISRSM---KKELKKYIEEMRSiltdknwKTPITVCWGLRDr 337
|
250 260 270
....*....|....*....|....*....|....
gi 24586385 338 WIDSSSGEKIKSQRGSNMVDIKIvtgAGHHVYAD 371
Cdd:PLN03084 338 WLNYDGVEDFCKSSQHKLIELPM---AGHHVQED 368
|
|
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
116-219 |
1.43e-05 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 47.11 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 116 VLLHGLGAGIALWVM----NLDAFAKGR-PVYAMDILGFGRSSRPlfaKDALVCEKQFVKSVEEWRRE-MNINDMILLGH 189
Cdd:PLN03087 205 LFIHGFISSSAFWTEtlfpNFSDAAKSTyRLFAVDLLGFGRSPKP---ADSLYTLREHLEMIERSVLErYKVKSFHIVAH 281
|
90 100 110
....*....|....*....|....*....|
gi 24586385 190 SMGGFIASSYALSHPERVKHLILADPWGFP 219
Cdd:PLN03087 282 SLGCILALALAVKHPGAVKSLTLLAPPYYP 311
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
109-212 |
1.93e-05 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 45.78 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 109 ESKEVPLVLL-HGLGAGIAL-WVMNLDAFA-KGRPVYAMDILGFGRSSRPLFAKDALVCEK--QFVKSveewRREMNIND 183
Cdd:COG1506 19 DGKKYPVVVYvHGGPGSRDDsFLPLAQALAsRGYAVLAPDYRGYGESAGDWGGDEVDDVLAaiDYLAA----RPYVDPDR 94
|
90 100
....*....|....*....|....*....
gi 24586385 184 MILLGHSMGGFIASSYALSHPERVKHLIL 212
Cdd:COG1506 95 IGIYGHSYGGYMALLAAARHPDRFKAAVA 123
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
114-208 |
3.16e-04 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 42.67 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 114 PLVLLHGLGAGIALW--VMNLDAfAKGRPVyAMDILGFGRSSRP----LFAKDAlvcekqfvKSVEEWRREMNINDMILL 187
Cdd:PRK03592 29 PIVFLHGNPTSSYLWrnIIPHLA-GLGRCL-APDLIGMGASDKPdidyTFADHA--------RYLDAWFDALGLDDVVLV 98
|
90 100
....*....|....*....|.
gi 24586385 188 GHSMGGFIASSYALSHPERVK 208
Cdd:PRK03592 99 GHDWGSALGFDWAARHPDRVR 119
|
|
| PRK00870 |
PRK00870 |
haloalkane dehalogenase; Provisional |
88-213 |
4.88e-04 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179147 [Multi-domain] Cd Length: 302 Bit Score: 41.88 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 88 FVDIGPAVGEadkiwtismnteskevPLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPlfAKDALVCEK 166
Cdd:PRK00870 38 YVDEGPADGP----------------PVLLLHGEPSWSYLYRKMIPILAAaGHRVIAPDLIGFGRSDKP--TRREDYTYA 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 24586385 167 QFVKSVEEWRREMNINDMILLGHSMGGFIASSYALSHPERVKHLILA 213
Cdd:PRK00870 100 RHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVA 146
|
|
| Esterase_713_like |
cd12806 |
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ... |
109-235 |
6.15e-04 |
|
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown. This enzyme is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.
Pssm-ID: 214005 Cd Length: 261 Bit Score: 41.36 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 109 ESKEVPLVLLHGLGAGIALWVMNLDA--------FAKGRPVYAMDILGFGRSSR----PLFAKDAlvcekQFVKSVEEWR 176
Cdd:cd12806 45 RAKRYPLLLIHGCGLTGMTWETTPDGrmgwdnyfLRKGYSVYVVDQPGRGRSGWdtqfPVQGQAE-----LWQQMVPDWL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586385 177 REMNINDM---------------ILLGHSMGGFIASSYALSHPERVKHLILADPWGFPeKPSDSTNGKTIPLWV 235
Cdd:cd12806 120 GAMPTPNPtvaalskladkldptVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCP-KPEDVKPLTSIPVLV 192
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
186-228 |
1.46e-03 |
|
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: 40.14 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24586385 186 LLGHSMGGFIASSYALSHPERVKHLIL--------ADPWGFPEKPSDSTNG 228
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSfspilnpsNSMWGPEDDPAWQEGD 164
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
185-255 |
2.00e-03 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214007 Cd Length: 309 Bit Score: 39.92 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 185 ILLGHSMGGFIASSYALSHPERVKHLILADPWGFPEkPSDSTNGKTIPL-------------WVRAIARVltpLNPLWAL 251
Cdd:cd12808 191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPD-PAEAAPLADVPHllvwgdyidadprWPRYRATV---DAYAAAL 266
|
....
gi 24586385 252 RAAG 255
Cdd:cd12808 267 RAAG 270
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
115-212 |
2.06e-03 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 39.82 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586385 115 LVLLHGLGAGIALWVMNLDAFAkGRPVYAMDILGFGRSsRPLFAKDALVCEKQFVKSVEEWrremNINDMILLGHSMGGF 194
Cdd:PRK11126 5 LVFLHGLLGSGQDWQPVGEALP-DYPRLYIDLPGHGGS-AAISVDGFADVSRLLSQTLQSY----NILPYWLVGYSLGGR 78
|
90
....*....|....*....
gi 24586385 195 IASSYAL-SHPERVKHLIL 212
Cdd:PRK11126 79 IAMYYACqGLAGGLCGLIV 97
|
|
| MET2 |
COG2021 |
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ... |
186-217 |
9.70e-03 |
|
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 441624 [Multi-domain] Cd Length: 355 Bit Score: 38.15 E-value: 9.70e-03
10 20 30
....*....|....*....|....*....|....*...
gi 24586385 186 LLGHSMGGFIASSYALSHPERVKHLIL------ADPWG 217
Cdd:COG2021 132 VIGGSMGGMQALEWAVSYPDRVRRAIViataarLSAQN 169
|
|
| |
