|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
4-320 |
9.80e-56 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 188.20 E-value: 9.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 4 AVEKKILSYVKLPYRGFFVDIG------------PAVGEADKIWTISMNTESKEVPLVLLHGLGAGIALWVMNLDAFAKG 71
Cdd:PLN02894 52 AAEKRLLSLVKTPYVQEQVNIGsgppgskvrwfrSASNEPRFINTVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 72 RPVYAMDILGFGRSSRPLF-AKDALVCEKQFVKSVEEWRREMNINDMILLGHSMGGFIASSYALSHPERVKHLILADPWG 150
Cdd:PLN02894 132 FRVIAIDQLGWGGSSRPDFtCKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 151 FPEKPSDSTNG--KTIPLWVRAIARVLTPLN--PLWALRAAGPFGQWVVQKTrpdIMRKFQST------IEEDINLLPQY 220
Cdd:PLN02894 212 FSSESDDKSEWltKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRY---TTARFGAHstgdilSEEESKLLTDY 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 221 IHQCNAQNPSGESAFHTMMQSFGWAKHPMIHRIKDVRsdIPITFIYGSRSWIDsSSGEKIKSQRGSNMVDIKIVTGAGHH 300
Cdd:PLN02894 289 VYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMN-YEGAVEARKRMKVPCEIIRVPQGGHF 365
|
330 340
....*....|....*....|
gi 665399345 301 VYADKPDVFNRYVNETCDMY 320
Cdd:PLN02894 366 VFLDNPSGFHSAVLYACRKY 385
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
47-315 |
7.58e-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: 103.54 E-value: 7.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPlfakDALVCEKQFVKSVEEWRREMNINDMILLGHSMGG 126
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP----AGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 127 FIASSYALSHPERVKHLILADPwgfpekpsdstngktiplWVRAIARVLtplnplwalraagpfgqwvvqktrpdimrkf 206
Cdd:COG0596 101 MVALELAARHPERVAGLVLVDE------------------VLAALAEPL------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 207 qstieedinllpqyihqcnAQNPSGESAFHTMMQSF-GWAKHPMIHRIkdvrsDIPITFIYGSRS-WIDSSSGEKIKSQ- 283
Cdd:COG0596 132 -------------------RRPGLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELl 187
|
250 260 270
....*....|....*....|....*....|..
gi 665399345 284 RGSNMVDIKivtGAGHHVYADKPDVFNRYVNE 315
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. |
47-306 |
4.49e-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: 99.50 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAKDalVCEKQFVKSVEEWRREMNINDMILLGHSMG 125
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKAQDD--YRTDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 126 GFIASSYALSHPERVKHLILADPWGFPEKPSD--STNGKTIPLWVRAIARVL--TPLNPLWALRAAGPFGQWVVQKTRPD 201
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEadRFILALFPGFFDGFVADFapNPLGRLVAKLLALLLLRLRLLKALPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 202 IMRKFQSTIEEDINLLPQYIHQCNAQnpsgesafhtmmqsfgWAKHPMIHRIkdVRSDIPITFIYGSRSWIDSSSGeKIK 281
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVTGALLFIET----------------WSTELRAKFL--GRLDEPTLIIWGDQDPLVPPQA-LEK 220
|
250 260
....*....|....*....|....*
gi 665399345 282 SQRGSNMVDIKIVTGAGHHVYADKP 306
Cdd:pfam00561 221 LAQLFPNARLVVIPDAGHFAFLEGP 245
|
|
| pro_imino_pep_2 |
TIGR01250 |
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ... |
33-180 |
2.15e-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: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 33 KIWTISMNTESKeVPLVLLHGLGAGIALWVMNLDAFAK--GRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRR 110
Cdd:TIGR01250 14 HLFTKTGGEGEK-IKLLLLHGGPGMSHEYLENLRELLKeeGREVIMYDQLGCGYSDQPDDSDEELWTIDYFVDELEEVRE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 111 EMNINDMILLGHSMGGFIASSYALSHPERVKHLILADpwgfpekPSDStngktIPLWVRAIARVLTPLNP 180
Cdd:TIGR01250 93 KLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISS-------MLDS-----APEYVKELNRLRKELPP 150
|
|
| Esterase_713_like |
cd12806 |
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ... |
42-168 |
4.80e-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: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 42 ESKEVPLVLLHGLGAGIALWVMNLDA--------FAKGRPVYAMDILGFGRSSR----PLFAKDAlvcekQFVKSVEEWR 109
Cdd:cd12806 45 RAKRYPLLLIHGCGLTGMTWETTPDGrmgwdnyfLRKGYSVYVVDQPGRGRSGWdtqfPVQGQAE-----LWQQMVPDWL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399345 110 REMNINDM---------------ILLGHSMGGFIASSYALSHPERVKHLILADPWGFPeKPSDSTNGKTIPLWV 168
Cdd:cd12806 120 GAMPTPNPtvaalskladkldptVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCP-KPEDVKPLTSIPVLV 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
4-320 |
9.80e-56 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 188.20 E-value: 9.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 4 AVEKKILSYVKLPYRGFFVDIG------------PAVGEADKIWTISMNTESKEVPLVLLHGLGAGIALWVMNLDAFAKG 71
Cdd:PLN02894 52 AAEKRLLSLVKTPYVQEQVNIGsgppgskvrwfrSASNEPRFINTVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 72 RPVYAMDILGFGRSSRPLF-AKDALVCEKQFVKSVEEWRREMNINDMILLGHSMGGFIASSYALSHPERVKHLILADPWG 150
Cdd:PLN02894 132 FRVIAIDQLGWGGSSRPDFtCKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 151 FPEKPSDSTNG--KTIPLWVRAIARVLTPLN--PLWALRAAGPFGQWVVQKTrpdIMRKFQST------IEEDINLLPQY 220
Cdd:PLN02894 212 FSSESDDKSEWltKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRY---TTARFGAHstgdilSEEESKLLTDY 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 221 IHQCNAQNPSGESAFHTMMQSFGWAKHPMIHRIKDVRsdIPITFIYGSRSWIDsSSGEKIKSQRGSNMVDIKIVTGAGHH 300
Cdd:PLN02894 289 VYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMN-YEGAVEARKRMKVPCEIIRVPQGGHF 365
|
330 340
....*....|....*....|
gi 665399345 301 VYADKPDVFNRYVNETCDMY 320
Cdd:PLN02894 366 VFLDNPSGFHSAVLYACRKY 385
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
47-315 |
7.58e-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: 103.54 E-value: 7.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPlfakDALVCEKQFVKSVEEWRREMNINDMILLGHSMGG 126
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP----AGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 127 FIASSYALSHPERVKHLILADPwgfpekpsdstngktiplWVRAIARVLtplnplwalraagpfgqwvvqktrpdimrkf 206
Cdd:COG0596 101 MVALELAARHPERVAGLVLVDE------------------VLAALAEPL------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 207 qstieedinllpqyihqcnAQNPSGESAFHTMMQSF-GWAKHPMIHRIkdvrsDIPITFIYGSRS-WIDSSSGEKIKSQ- 283
Cdd:COG0596 132 -------------------RRPGLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELl 187
|
250 260 270
....*....|....*....|....*....|..
gi 665399345 284 RGSNMVDIKivtGAGHHVYADKPDVFNRYVNE 315
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. |
47-306 |
4.49e-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: 99.50 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAKDalVCEKQFVKSVEEWRREMNINDMILLGHSMG 125
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKAQDD--YRTDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 126 GFIASSYALSHPERVKHLILADPWGFPEKPSD--STNGKTIPLWVRAIARVL--TPLNPLWALRAAGPFGQWVVQKTRPD 201
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLLGALDPPHELDEadRFILALFPGFFDGFVADFapNPLGRLVAKLLALLLLRLRLLKALPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 202 IMRKFQSTIEEDINLLPQYIHQCNAQnpsgesafhtmmqsfgWAKHPMIHRIkdVRSDIPITFIYGSRSWIDSSSGeKIK 281
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVTGALLFIET----------------WSTELRAKFL--GRLDEPTLIIWGDQDPLVPPQA-LEK 220
|
250 260
....*....|....*....|....*
gi 665399345 282 SQRGSNMVDIKIVTGAGHHVYADKP 306
Cdd:pfam00561 221 LAQLFPNARLVVIPDAGHFAFLEGP 245
|
|
| pro_imino_pep_2 |
TIGR01250 |
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ... |
33-180 |
2.15e-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: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 33 KIWTISMNTESKeVPLVLLHGLGAGIALWVMNLDAFAK--GRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRR 110
Cdd:TIGR01250 14 HLFTKTGGEGEK-IKLLLLHGGPGMSHEYLENLRELLKeeGREVIMYDQLGCGYSDQPDDSDEELWTIDYFVDELEEVRE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 111 EMNINDMILLGHSMGGFIASSYALSHPERVKHLILADpwgfpekPSDStngktIPLWVRAIARVLTPLNP 180
Cdd:TIGR01250 93 KLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISS-------MLDS-----APEYVKELNRLRKELPP 150
|
|
| PLN02578 |
PLN02578 |
hydrolase |
42-311 |
1.55e-18 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 86.05 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 42 ESKEVPLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLFAKDALVCEKQfvksVEEWRREMNINDMILLG 121
Cdd:PLN02578 83 QGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQ----VADFVKEVVKEPAVLVG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 122 HSMGGFIASSYALSHPERVKHLILADPWGFPEKPSDSTNGKTIPLWVRAIARVLTPLNPlWALRAAGPFGQWvvQKTRPd 201
Cdd:PLN02578 159 NSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAIVVEETVLTRFVVKPLKE-WFQRVVLGFLFW--QAKQP- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 202 imrkfqSTIEEDINLLpqYIHQCN------------AQNPSGESAFHTMMQSFgwAKHPMIHRIKDVRSDI--PITFIYG 267
Cdd:PLN02578 235 ------SRIESVLKSV--YKDKSNvddylvesitepAADPNAGEVYYRLMSRF--LFNQSRYTLDSLLSKLscPLLLLWG 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 665399345 268 -SRSWIDSSSGEKIKS-QRGSNMVDIKivtgAGHHVYADKPDVFNR 311
Cdd:PLN02578 305 dLDPWVGPAKAEKIKAfYPDTTLVNLQ----AGHCPHDEVPEQVNK 346
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
47-178 |
9.80e-18 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 81.20 E-value: 9.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAKDALvceKQFVKSVEEWRREMNIN---DMILLGH 122
Cdd:COG2267 30 TVVLVHGLGEHSGRYAELAEALAAaGYAVLAFDLRGHGRSDGPRGHVDSF---DDYVDDLRAALDALRARpglPVVLLGH 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 665399345 123 SMGGFIASSYALSHPERVKHLILADPWGFPEKPSDSTNGKTIPLWV-RAIARVLTPL 178
Cdd:COG2267 107 SMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRALRLaEALARIDVPV 163
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
42-161 |
1.74e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 79.99 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 42 ESKEVPLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLFAKDALvcekQFVKSVEEWRREMNINDMILLG 121
Cdd:PRK14875 128 EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLD----ELAAAVLAFLDALGIERAHLVG 203
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 665399345 122 HSMGGFIASSYALSHPERVKHLILADPWGF-PEKPSDSTNG 161
Cdd:PRK14875 204 HSMGGAVALRLAARAPQRVASLTLIAPAGLgPEINGDYIDG 244
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
48-201 |
3.01e-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: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 48 LVLLHGLG------AGIAlwvmnlDAFAK-GRPVYAMDILGFGRSSRP--------LFAKDAlvceKQFV-KSVEEWRRE 111
Cdd:pfam12146 7 VVLVHGLGehsgryAHLA------DALAAqGFAVYAYDHRGHGRSDGKrghvpsfdDYVDDL----DTFVdKIREEHPGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 112 mninDMILLGHSMGGFIASSYALSHPERVKHLILADPWGFPEKPSdstngktIPLWVRAIARVLTPLNPLWALRAAGPFG 191
Cdd:pfam12146 77 ----PLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYL-------APPILKLLAKLLGKLFPRLRVPNNLLPD 145
|
170
....*....|....*
gi 665399345 192 -----QWVVQKTRPD 201
Cdd:pfam12146 146 slsrdPEVVAAYAAD 160
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
48-311 |
4.53e-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: 59.02 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 48 LVLLHGLGAGIALWvmnLDAFAKGRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRREmnindmILLGHSMGGF 127
Cdd:pfam12697 1 VVLVHGAGLSAAPL---AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV------VLVGHSLGGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 128 IASSYAlshPERVKHLILADPWGFPekpsdstngktiPLWVRAIARVLTPLNPLWALRAagpfgqWVVQKTRPDIMrkfq 207
Cdd:pfam12697 72 VALAAA---AAALVVGVLVAPLAAP------------PGLLAALLALLARLGAALAAPA------WLAAESLARGF---- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 208 stieedinllpqyiHQCNAQNPSGESAFHTMMQSFGWAKHPMIHRIKDVRSdiPITFIYGSRSWIDSSSGEKIKSQRGsn 287
Cdd:pfam12697 127 --------------LDDLPADAEWAAALARLAALLAALALLPLAAWRDLPV--PVLVLAEEDRLVPELAQRLLAALAG-- 188
|
250 260
....*....|....*....|....
gi 665399345 288 mVDIKIVTGAGHHVYaDKPDVFNR 311
Cdd:pfam12697 189 -ARLVVLPGAGHLPL-DDPEEVAE 210
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
47-144 |
6.63e-10 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 55.99 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAkdalvcekQFVKSVEEWRREMNINDMILLGHSMG 125
Cdd:COG1075 7 PVVLVHGLGGSAASWAPLAPRLRAaGYPVYALNYPSTNGSIEDSAE--------QLAAFVDAVLAATGAEKVDLVGHSMG 78
|
90 100
....*....|....*....|.
gi 665399345 126 GFIASSYA--LSHPERVKHLI 144
Cdd:COG1075 79 GLVARYYLkrLGGAAKVARVV 99
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
47-145 |
5.92e-09 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 57.16 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPlfakdalvceKQFVKSVEEWR-------REMNINDMIL 119
Cdd:PLN02679 90 PVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKP----------PGFSYTMETWAelildflEEVVQKPTVL 159
|
90 100
....*....|....*....|....*....
gi 665399345 120 LGHSMGGF---IASSYalSHPERVKHLIL 145
Cdd:PLN02679 160 IGNSVGSLacvIAASE--STRDLVRGLVL 186
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
49-311 |
2.95e-08 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 54.18 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 49 VLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPLFAKDAlvceKQFVKSVEEwrrEMNI-----NDMILLGH 122
Cdd:COG1647 19 LLLHGFTGSPAEMRPLAEALAKaGYTVYAPRLPGHGTSPEDLLKTTW----EDWLEDVEE---AYEIlkagyDKVIVIGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 123 SMGGFIASSYALSHPErVKHLILADPwgfpekpsdstngktiPLWVRAIARVLTplnplwalraagPFGQWVVQKtrpdi 202
Cdd:COG1647 92 SMGGLLALLLAARYPD-VAGLVLLSP----------------ALKIDDPSAPLL------------PLLKYLARS----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 203 MRKFQSTIEEdinllPQYIHQCNAQNPSgeSAFHTMMQSFGWAKHPmIHRIKdvrsdIPITFIYGSR-SWIDSSSGEKIK 281
Cdd:COG1647 138 LRGIGSDIED-----PEVAEYAYDRTPL--RALAELQRLIREVRRD-LPKIT-----APTLIIQSRKdEVVPPESARYIY 204
|
250 260 270
....*....|....*....|....*....|..
gi 665399345 282 SQRGSNMVDIKIVTGAGH--HVYADKPDVFNR 311
Cdd:COG1647 205 ERLGSPDKELVWLEDSGHviTLDKDREEVAEE 236
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
47-148 |
6.56e-08 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 53.59 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPlfakDALVCEKQFVKSVEEWRREMN--INDMI-----L 119
Cdd:PLN02824 31 ALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP----NPRSAPPNSFYTFETWGEQLNdfCSDVVgdpafV 106
|
90 100
....*....|....*....|....*....
gi 665399345 120 LGHSMGGFIASSYALSHPERVKHLILADP 148
Cdd:PLN02824 107 ICNSVGGVVGLQAAVDAPELVRGVMLINI 135
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
47-193 |
7.12e-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: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGaGIALWVMNL-DAFAKGRPVYAMDILGFGRSSRPLfakdalvcekqfvKSVEEWRREMnINDM-------- 117
Cdd:COG3319 603 PLFCVHPAG-GNVLCYRPLaRALGPDRPVYGLQAPGLDGGEPPP-------------ASVEEMAARY-VEAIravqpegp 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 118 -ILLGHSMGGFIAssYALSH-----PERVKHLILADPWGfPEKPSDSTNGKTIPLWVRAIARVLTPLNPLWALRAAGPFG 191
Cdd:COG3319 668 yHLLGWSFGGLVA--YEMARqleaqGEEVALLVLLDSYA-PGALARLDEAELLAALLRDLARGVDLPLDAEELRALDPEE 744
|
..
gi 665399345 192 QW 193
Cdd:COG3319 745 RL 746
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
48-145 |
9.90e-08 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 51.83 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 48 LVLLHGLGA------GIALWVMNLDAF-----AKGRPVYAM----DILGFGRSSRPLFAKDALvceKQFVKSVEEWRREM 112
Cdd:COG0400 8 VVLLHGYGGdeedllPLAPELALPGAAvlaprAPVPEGPGGrawfDLSFLEGREDEEGLAAAA---EALAAFIDELEARY 84
|
90 100 110
....*....|....*....|....*....|....*
gi 665399345 113 NIND--MILLGHSMGGFIASSYALSHPERVKHLIL 145
Cdd:COG0400 85 GIDPerIVLAGFSQGAAMALSLALRRPELLAGVVA 119
|
|
| PRK10673 |
PRK10673 |
esterase; |
47-315 |
1.87e-07 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 51.65 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGL-GAGIALWVMNLDaFAKGRPVYAMDILGFGRSSR------PLFAKDALvcekqfvksveEWRREMNINDMIL 119
Cdd:PRK10673 18 PIVLVHGLfGSLDNLGVLARD-LVNDHDIIQVDMRNHGLSPRdpvmnyPAMAQDLL-----------DTLDALQIEKATF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 120 LGHSMGGFIASSYALSHPERVKHLILADPwgfpeKPSDSTngktiplwVRAIARVLTPLNplwALRAAGpfgqwVVQKTR 199
Cdd:PRK10673 86 IGHSMGGKAVMALTALAPDRIDKLVAIDI-----APVDYH--------VRRHDEIFAAIN---AVSEAG-----ATTRQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 200 P-DIMRKfqsTIEED--INLLPQYIHQcnaqnpsGESAFH--TMMQSF----GWAKHPMIHRikdvrsdiPITFIYGSRS 270
Cdd:PRK10673 145 AaAIMRQ---HLNEEgvIQFLLKSFVD-------GEWRFNvpVLWDQYphivGWEKIPAWPH--------PALFIRGGNS 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 665399345 271 -WIDSSSGEKIKSQrgSNMVDIKIVTGAGHHVYADKPD----VFNRYVNE 315
Cdd:PRK10673 207 pYVTEAYRDDLLAQ--FPQARAHVIAGAGHWVHAEKPDavlrAIRRYLND 254
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
46-144 |
3.22e-07 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 51.17 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 46 VPLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSrplfAKDALVCEKQFVKSVEEwrremNINDMILLGHSMG 125
Cdd:PRK10349 14 VHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR----GFGALSLADMAEAVLQQ-----APDKAIWLGWSLG 84
|
90
....*....|....*....
gi 665399345 126 GFIASSYALSHPERVKHLI 144
Cdd:PRK10349 85 GLVASQIALTHPERVQALV 103
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
47-304 |
1.16e-06 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 50.26 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALWVMNLDAFAKGRPVYAMDILGFGRSSRPLFAKDALVCEKQFVKSVEEWRREMNINDMILLGHSMGG 126
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQGYFS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 127 FIASSYALSHPERVKHLILADPwgfPEKPSDSTNGKTIPLWVRAIARVLTPLNPLWA----LRAAGPFgqwvvQKTRPDI 202
Cdd:PLN03084 209 PPVVKYASAHPDKIKKLILLNP---PLTKEHAKLPSTLSEFSNFLLGEIFSQDPLRAsdkaLTSCGPY-----AMKEDDA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 203 M--RKfqstieedinllpQYIhqcnaqnPSGESAF--HTMMQSFgwaKHPMIHRIKDVRS-------DIPITFIYGSRS- 270
Cdd:PLN03084 281 MvyRR-------------PYL-------TSGSSGFalNAISRSM---KKELKKYIEEMRSiltdknwKTPITVCWGLRDr 337
|
250 260 270
....*....|....*....|....*....|....
gi 665399345 271 WIDSSSGEKIKSQRGSNMVDIKIvtgAGHHVYAD 304
Cdd:PLN03084 338 WLNYDGVEDFCKSSQHKLIELPM---AGHHVQED 368
|
|
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
49-152 |
1.02e-05 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 47.50 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 49 VLLHGLGAGIALWVM----NLDAFAKGR-PVYAMDILGFGRSSRPlfaKDALVCEKQFVKSVEEWRRE-MNINDMILLGH 122
Cdd:PLN03087 205 LFIHGFISSSAFWTEtlfpNFSDAAKSTyRLFAVDLLGFGRSPKP---ADSLYTLREHLEMIERSVLErYKVKSFHIVAH 281
|
90 100 110
....*....|....*....|....*....|
gi 665399345 123 SMGGFIASSYALSHPERVKHLILADPWGFP 152
Cdd:PLN03087 282 SLGCILALALAVKHPGAVKSLTLLAPPYYP 311
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
42-145 |
2.27e-05 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 45.39 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 42 ESKEVPLVLL-HGLGAGIAL-WVMNLDAFA-KGRPVYAMDILGFGRSSRPLFAKDALVCEK--QFVKSveewRREMNIND 116
Cdd:COG1506 19 DGKKYPVVVYvHGGPGSRDDsFLPLAQALAsRGYAVLAPDYRGYGESAGDWGGDEVDDVLAaiDYLAA----RPYVDPDR 94
|
90 100
....*....|....*....|....*....
gi 665399345 117 MILLGHSMGGFIASSYALSHPERVKHLIL 145
Cdd:COG1506 95 IGIYGHSYGGYMALLAAARHPDRFKAAVA 123
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
47-141 |
2.53e-04 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 42.67 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 47 PLVLLHGLGAGIALW--VMNLDAfAKGRPVyAMDILGFGRSSRP----LFAKDAlvcekqfvKSVEEWRREMNINDMILL 120
Cdd:PRK03592 29 PIVFLHGNPTSSYLWrnIIPHLA-GLGRCL-APDLIGMGASDKPdidyTFADHA--------RYLDAWFDALGLDDVVLV 98
|
90 100
....*....|....*....|.
gi 665399345 121 GHSMGGFIASSYALSHPERVK 141
Cdd:PRK03592 99 GHDWGSALGFDWAARHPDRVR 119
|
|
| PRK00870 |
PRK00870 |
haloalkane dehalogenase; Provisional |
21-146 |
4.09e-04 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179147 [Multi-domain] Cd Length: 302 Bit Score: 41.88 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 21 FVDIGPAVGEadkiwtismnteskevPLVLLHGLGAGIALWVMNLDAFAK-GRPVYAMDILGFGRSSRPlfAKDALVCEK 99
Cdd:PRK00870 38 YVDEGPADGP----------------PVLLLHGEPSWSYLYRKMIPILAAaGHRVIAPDLIGFGRSDKP--TRREDYTYA 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 665399345 100 QFVKSVEEWRREMNINDMILLGHSMGGFIASSYALSHPERVKHLILA 146
Cdd:PRK00870 100 RHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVA 146
|
|
| Esterase_713_like |
cd12806 |
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ... |
42-168 |
4.80e-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: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 42 ESKEVPLVLLHGLGAGIALWVMNLDA--------FAKGRPVYAMDILGFGRSSR----PLFAKDAlvcekQFVKSVEEWR 109
Cdd:cd12806 45 RAKRYPLLLIHGCGLTGMTWETTPDGrmgwdnyfLRKGYSVYVVDQPGRGRSGWdtqfPVQGQAE-----LWQQMVPDWL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399345 110 REMNINDM---------------ILLGHSMGGFIASSYALSHPERVKHLILADPWGFPeKPSDSTNGKTIPLWV 168
Cdd:cd12806 120 GAMPTPNPtvaalskladkldptVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCP-KPEDVKPLTSIPVLV 192
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
119-161 |
1.01e-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: 40.52 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 665399345 119 LLGHSMGGFIASSYALSHPERVKHLIL--------ADPWGFPEKPSDSTNG 161
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSfspilnpsNSMWGPEDDPAWQEGD 164
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
118-188 |
1.59e-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: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 118 ILLGHSMGGFIASSYALSHPERVKHLILADPWGFPEkPSDSTNGKTIPL-------------WVRAIARVltpLNPLWAL 184
Cdd:cd12808 191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPD-PAEAAPLADVPHllvwgdyidadprWPRYRATV---DAYAAAL 266
|
....
gi 665399345 185 RAAG 188
Cdd:cd12808 267 RAAG 270
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
48-145 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399345 48 LVLLHGLGAGIALWVMNLDAFAkGRPVYAMDILGFGRSsRPLFAKDALVCEKQFVKSVEEWrremNINDMILLGHSMGGF 127
Cdd:PRK11126 5 LVFLHGLLGSGQDWQPVGEALP-DYPRLYIDLPGHGGS-AAISVDGFADVSRLLSQTLQSY----NILPYWLVGYSLGGR 78
|
90
....*....|....*....
gi 665399345 128 IASSYAL-SHPERVKHLIL 145
Cdd:PRK11126 79 IAMYYACqGLAGGLCGLIV 97
|
|
| MET2 |
COG2021 |
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ... |
119-150 |
7.70e-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: 7.70e-03
10 20 30
....*....|....*....|....*....|....*...
gi 665399345 119 LLGHSMGGFIASSYALSHPERVKHLIL------ADPWG 150
Cdd:COG2021 132 VIGGSMGGMQALEWAVSYPDRVRRAIViataarLSAQN 169
|
|
| |
