|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
11-276 |
2.81e-51 |
|
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: 167.49 E-value: 2.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 11 TFSTRGTTIHYELYEHDnkteRPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLfKYSYHNLATIII 90
Cdd:COG0596 6 FVTVDGVRLHYREAGPD----GPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAG-GYTLDDLADDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 91 DLIEHLSLSNIVLVGHSMGGQISLYVNRIRPELISKTILLcsssylaratlpllyssylpffhlyvknwiirrgivhnlm 170
Cdd:COG0596 81 ALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 171 nvvhdhslidDEMKKGYSAPFYDDRIFP-ALTRMIRDREGDLSSTELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPNS 249
Cdd:COG0596 121 ----------DEVLAALAEPLRRPGLAPeALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNA 190
|
250 260
....*....|....*....|....*..
gi 446937948 250 KFISYENTGHLLPEEKPEHVYEEIIAF 276
Cdd:COG0596 191 ELVVLPGAGHFPPLEQPEAFAAALRDF 217
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
33-266 |
1.33e-32 |
|
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: 119.92 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPFGKSDK-SHLFKYSYHNLATIIIDLIEHLSLSNIVLVGHSMGG 110
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 111 QISLYVNRIRPELISKTILLCSSSY---------LARATLPLLYSSYLPFFHLYVKNwiIRRGIVHNLMNVVHDHSLIDD 181
Cdd:pfam00561 81 LIALAYAAKYPDRVKALVLLGALDPpheldeadrFILALFPGFFDGFVADFAPNPLG--RLVAKLLALLLLRLRLLKALP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 182 EMKKGYSAPFYDDRIFPALTR--MIRDREGDLSSTELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPNSKFISYENTGH 259
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGAllFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238
|
....*..
gi 446937948 260 LLPEEKP 266
Cdd:pfam00561 239 FAFLEGP 245
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
33-279 |
1.70e-22 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 95.29 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFKYSYHNLATIIIDLIEHLSLSNIVLVGHSMGGQI 112
Cdd:PLN02679 89 PPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSLA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 113 SLYV-NRIRPELISKTILL-CSSSYLARAT-----LPLLyssyLPFfhLYVKNWIIR-RGIVHNLMNVVHDHS------- 177
Cdd:PLN02679 169 CVIAaSESTRDLVRGLVLLnCAGGMNNKAVvddwrIKLL----LPL--LWLIDFLLKqRGIASALFNRVKQRDnlknill 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 178 -------LIDDEMKKGYSAPFYDDRIFPALTRMIRDREGDLSSTELQKIETPTLLIWGEKDRVVPVH--VGH---RLHKD 245
Cdd:PLN02679 243 svygnkeAVDDELVEIIRGPADDEGALDAFVSIVTGPPGPNPIKLIPRISLPILVLWGDQDPFTPLDgpVGKyfsSLPSQ 322
|
250 260 270
....*....|....*....|....*....|....
gi 446937948 246 LPNSKFISYENTGHLLPEEKPEHVYEEIIAFSAQ 279
Cdd:PLN02679 323 LPNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLAQ 356
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
31-276 |
1.21e-16 |
|
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: 77.26 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 31 ERPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFK-YSYHNLAT-IIIDLIEHLSLSNIVLVGHSM 108
Cdd:TIGR03695 1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIErYDFEEAAQlLLATLLDQLGIEPFFLVGYSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 109 GGQISLYVNRIRPELISKTILLCSSSYLARATLPLlySSYLPFFHLyvKNWIIRRGIVHNL--------------MNVVH 174
Cdd:TIGR03695 81 GGRIALYYALQYPERVQGLILESGSPGLQTEEERA--ARRQNDEQL--AQRFEQEGLEAFLddwyqqplfasqknLPPEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 175 DHSLIddEMKKGYSApfyddrifPALTRMIRDregdlSST--------ELQKIETPTLLIWGEKDRVVpVHVGHRLHKDL 246
Cdd:TIGR03695 157 RQALR--AERLANNP--------EGLAKMLRA-----TGLgkqpslwpKLQALKIPVLYLCGERDEKF-VQIAKEMQKLI 220
|
250 260 270
....*....|....*....|....*....|
gi 446937948 247 PNSKFISYENTGHLLPEEKPEHVYEEIIAF 276
Cdd:TIGR03695 221 PNLTLHIIPNAGHNIHLENPEAFAKILLAF 250
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
7-119 |
7.85e-07 |
|
Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain] Cd Length: 275 Bit Score: 49.16 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 7 CPYFTFSTRGTTIHYELYehdnKTERPTFVLVHGFLSSSF--SYRRLIP-LLSKAGT-VIALD---------------LP 67
Cdd:cd00707 15 CPQLLFADDPSSLKNSNF----NPSRPTRFIIHGWTSSGEesWISDLRKaYLSRGDYnVIVVDwgrganpnypqavnnTR 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446937948 68 PFGKsdkshlfkysyhNLATIIIDLIEH--LSLSNIVLVGHSMGGQISLY--------VNRI 119
Cdd:cd00707 91 VVGA------------ELAKFLDFLVDNtgLSLENVHLIGHSLGAHVAGFagkrlngkLGRI 140
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
11-276 |
2.81e-51 |
|
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: 167.49 E-value: 2.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 11 TFSTRGTTIHYELYEHDnkteRPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLfKYSYHNLATIII 90
Cdd:COG0596 6 FVTVDGVRLHYREAGPD----GPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAG-GYTLDDLADDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 91 DLIEHLSLSNIVLVGHSMGGQISLYVNRIRPELISKTILLcsssylaratlpllyssylpffhlyvknwiirrgivhnlm 170
Cdd:COG0596 81 ALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 171 nvvhdhslidDEMKKGYSAPFYDDRIFP-ALTRMIRDREGDLSSTELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPNS 249
Cdd:COG0596 121 ----------DEVLAALAEPLRRPGLAPeALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNA 190
|
250 260
....*....|....*....|....*..
gi 446937948 250 KFISYENTGHLLPEEKPEHVYEEIIAF 276
Cdd:COG0596 191 ELVVLPGAGHFPPLEQPEAFAAALRDF 217
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
33-266 |
1.33e-32 |
|
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: 119.92 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPFGKSDK-SHLFKYSYHNLATIIIDLIEHLSLSNIVLVGHSMGG 110
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 111 QISLYVNRIRPELISKTILLCSSSY---------LARATLPLLYSSYLPFFHLYVKNwiIRRGIVHNLMNVVHDHSLIDD 181
Cdd:pfam00561 81 LIALAYAAKYPDRVKALVLLGALDPpheldeadrFILALFPGFFDGFVADFAPNPLG--RLVAKLLALLLLRLRLLKALP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 182 EMKKGYSAPFYDDRIFPALTR--MIRDREGDLSSTELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPNSKFISYENTGH 259
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGAllFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238
|
....*..
gi 446937948 260 LLPEEKP 266
Cdd:pfam00561 239 FAFLEGP 245
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
10-276 |
5.40e-28 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 107.01 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 10 FTFSTR-GTTIHYELYEHDNKTeRPTFVLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPFGKSDKSHLFKYSYHNLAT 87
Cdd:COG2267 6 VTLPTRdGLRLRGRRWRPAGSP-RGTVVLVHGLGEHSGRYAELAEALAAAGyAVLAFDLRGHGRSDGPRGHVDSFDDYVD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 88 IIIDLIEHLSL---SNIVLVGHSMGGQISL-YVNRiRPELISKTIlLCSSSYLARatlPLLYSSYLPFFHLYVKNWiirr 163
Cdd:COG2267 85 DLRAALDALRArpgLPVVLLGHSMGGLIALlYAAR-YPDRVAGLV-LLAPAYRAD---PLLGPSARWLRALRLAEA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 164 givhnlmnvvhdhsliddemkkgysapfyddrifpaltrmirdregdlssteLQKIETPTLLIWGEKDRVVPVHVGHRLH 243
Cdd:COG2267 156 ----------------------------------------------------LARIDVPVLVLHGGADRVVPPEAARRLA 183
|
250 260 270
....*....|....*....|....*....|....*
gi 446937948 244 KDL-PNSKFISYENTGHLLPEEKP-EHVYEEIIAF 276
Cdd:COG2267 184 ARLsPDVELVLLPGARHELLNEPArEEVLAAILAW 218
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
32-276 |
2.54e-24 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 98.09 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 32 RPTFVLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPFGkSDKSHLFKYSYHNLATIIIDLIEHLSL--SNIVLVGHSM 108
Cdd:COG1647 15 RKGVLLLHGFTGSPAEMRPLAEALAKAGyTVYAPRLPGHG-TSPEDLLKTTWEDWLEDVEEAYEILKAgyDKVIVIGLSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 109 GGQISLYVNRIRPElISKTILLCSSSYLARATLPLLyssylPFFHlYVKNWIIRRGivhnlmnvvhdhsliDDEMKKGYS 188
Cdd:COG1647 94 GGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLL-----PLLK-YLARSLRGIG---------------SDIEDPEVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 189 APFYDDRIFPA---LTRMIRDREGDLSstelqKIETPTLLIWGEKDRVVPVHVGHRLHKDL--PNSKFISYENTGHL--L 261
Cdd:COG1647 152 EYAYDRTPLRAlaeLQRLIREVRRDLP-----KITAPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHVitL 226
|
250
....*....|....*
gi 446937948 262 PEEKPEhVYEEIIAF 276
Cdd:COG1647 227 DKDREE-VAEEILDF 240
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
33-279 |
1.70e-22 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 95.29 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFKYSYHNLATIIIDLIEHLSLSNIVLVGHSMGGQI 112
Cdd:PLN02679 89 PPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSLA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 113 SLYV-NRIRPELISKTILL-CSSSYLARAT-----LPLLyssyLPFfhLYVKNWIIR-RGIVHNLMNVVHDHS------- 177
Cdd:PLN02679 169 CVIAaSESTRDLVRGLVLLnCAGGMNNKAVvddwrIKLL----LPL--LWLIDFLLKqRGIASALFNRVKQRDnlknill 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 178 -------LIDDEMKKGYSAPFYDDRIFPALTRMIRDREGDLSSTELQKIETPTLLIWGEKDRVVPVH--VGH---RLHKD 245
Cdd:PLN02679 243 svygnkeAVDDELVEIIRGPADDEGALDAFVSIVTGPPGPNPIKLIPRISLPILVLWGDQDPFTPLDgpVGKyfsSLPSQ 322
|
250 260 270
....*....|....*....|....*....|....
gi 446937948 246 LPNSKFISYENTGHLLPEEKPEHVYEEIIAFSAQ 279
Cdd:PLN02679 323 LPNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLAQ 356
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
16-279 |
3.72e-21 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 91.54 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 16 GTTIHY-ELYEHDnkteRPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKShLFKYSYHNLATIIIDLIE 94
Cdd:PRK14875 118 GRTVRYlRLGEGD----GTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKA-VGAGSLDELAAAVLAFLD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 95 HLSLSNIVLVGHSMGGQISLYVNRIRPELISKTILLCS--------SSYL---ARAtlpllySSylpffhlyvknwiiRR 163
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPaglgpeinGDYIdgfVAA------ES--------------RR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 164 GIVHNLMNVVHDHSLIDDEMKKGYSAPFYDDRIFPALTRMIR-----DREGDLSSTELQKIETPTLLIWGEKDRVVPV-H 237
Cdd:PRK14875 253 ELKPVLELLFADPALVTRQMVEDLLKYKRLDGVDDALRALADalfagGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAaH 332
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446937948 238 VGHrlhkdLP-NSKFISYENTGHLLPEEKPEHVYEEIIAFSAQ 279
Cdd:PRK14875 333 AQG-----LPdGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
|
|
| PRK00870 |
PRK00870 |
haloalkane dehalogenase; Provisional |
33-279 |
1.72e-20 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179147 [Multi-domain] Cd Length: 302 Bit Score: 88.87 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPFGKSDK-SHLFKYSYHNLATIIIDLIEHLSLSNIVLVGHSMGG 110
Cdd:PRK00870 47 PPVLLLHGEPSWSYLYRKMIPILAAAGhRVIAPDLIGFGRSDKpTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 111 QISLYVNRIRPELISKTIllcsssyLARATLP-------------LLYSSYLPFFHLyvkNWIIRRGIVHNLmnvvhdhs 177
Cdd:PRK00870 127 LIGLRLAAEHPDRFARLV-------VANTGLPtgdgpmpdafwawRAFSQYSPVLPV---GRLVNGGTVRDL-------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 178 liDDEMKKGYSAPFYDD------RIFPALTRMIRD----REGDLSSTELQKIETPTLLIWGEKDrvvPVHVG--HRLHKD 245
Cdd:PRK00870 189 --SDAVRAAYDAPFPDEsykagaRAFPLLVPTSPDdpavAANRAAWAVLERWDKPFLTAFSDSD---PITGGgdAILQKR 263
|
250 260 270
....*....|....*....|....*....|....*..
gi 446937948 246 LPNSKFISY---ENTGHLLPEEKPEHVYEEIIAFSAQ 279
Cdd:PRK00870 264 IPGAAGQPHptiKGAGHFLQEDSGEELAEAVLEFIRA 300
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
13-276 |
1.73e-20 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 87.38 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 13 STRGTTIHYELYEHDNKTERPTFVLVHGFLSSSF-SYRRLIPLLSKAG-TVIALDLPPFGKSDKsHLFKYSYHNLATIII 90
Cdd:COG1506 4 SADGTTLPGWLYLPADGKKYPVVVYVHGGPGSRDdSFLPLAQALASRGyAVLAPDYRGYGESAG-DWGGDEVDDVLAAID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 91 DLIEH--LSLSNIVLVGHSMGGQISLYVNRIRPELISKTILLCSSSylaratlpllyssylpffhlyvkNWIIRRGIVHN 168
Cdd:COG1506 83 YLAARpyVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS-----------------------DLRSYYGTTRE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 169 LMNVVHDHSLIDDEMKKGYSAPFYddrifpaltrmirdregdlssteLQKIETPTLLIWGEKDRVVPVHVGHRLHKDL-- 246
Cdd:COG1506 140 YTERLMGGPWEDPEAYAARSPLAY-----------------------ADKLKTPLLLIHGEADDRVPPEQAERLYEALkk 196
|
250 260 270
....*....|....*....|....*....|..
gi 446937948 247 --PNSKFISYENTGHLLPEEKPEHVYEEIIAF 276
Cdd:COG1506 197 agKPVELLVYPGEGHGFSGAGAPDYLERILDF 228
|
|
| PLN02578 |
PLN02578 |
hydrolase |
15-278 |
6.85e-19 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 84.89 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 15 RGTTIHYELyehdnKTERPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKShLFKYSYHNLATIIIDLIE 94
Cdd:PLN02578 74 RGHKIHYVV-----QGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKA-LIEYDAMVWRDQVADFVK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 95 HLSLSNIVLVGHSMGGQISLYVNRIRPELISKTILLCSSSYLA-----RATLPLLYSSYLP-FFHLYVKNWIIR------ 162
Cdd:PLN02578 148 EVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGsesreKEEAIVVEETVLTrFVVKPLKEWFQRvvlgfl 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 163 -------RGIVHNLMNVVHDHSLIDDEMKKGYSAPFYDDRIFPALTRMIRD---REGDLS-STELQKIETPTLLIWGEKD 231
Cdd:PLN02578 228 fwqakqpSRIESVLKSVYKDKSNVDDYLVESITEPAADPNAGEVYYRLMSRflfNQSRYTlDSLLSKLSCPLLLLWGDLD 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446937948 232 RVVPVHVGHRLHKDLPNSKFISYEnTGHLLPEEKPEHVYEEIIAFSA 278
Cdd:PLN02578 308 PWVGPAKAEKIKAFYPDTTLVNLQ-AGHCPHDEVPEQVNKALLEWLS 353
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
35-272 |
2.25e-17 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 78.67 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 35 FVLVHGFlssSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHlfkYSYHNLATIIIDLIEHLSLSNIVLVGHSMGGQISL 114
Cdd:pfam12697 1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPP---LDLADLADLAALLDELGAARPVVLVGHSLGGAVAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 115 yvnRIRPELISKTILLCSSSYLARatlpllyssYLPFFHLYVKNWIIRRGIVHNLMNVVHDHSLIDDEmkkgysAPFYDD 194
Cdd:pfam12697 75 ---AAAAAALVVGVLVAPLAAPPG---------LLAALLALLARLGAALAAPAWLAAESLARGFLDDL------PADAEW 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446937948 195 RIFPALTRMIRDREGDLSSTELQKIETPTLLIWGEkDRVVPVHVgHRLHKDLPNSKFISYENTGHlLPEEKPEHVYEE 272
Cdd:pfam12697 137 AAALARLAALLAALALLPLAAWRDLPVPVLVLAEE-DRLVPELA-QRLLAALAGARLVVLPGAGH-LPLDDPEEVAEA 211
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
31-276 |
1.21e-16 |
|
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: 77.26 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 31 ERPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFK-YSYHNLAT-IIIDLIEHLSLSNIVLVGHSM 108
Cdd:TIGR03695 1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIErYDFEEAAQlLLATLLDQLGIEPFFLVGYSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 109 GGQISLYVNRIRPELISKTILLCSSSYLARATLPLlySSYLPFFHLyvKNWIIRRGIVHNL--------------MNVVH 174
Cdd:TIGR03695 81 GGRIALYYALQYPERVQGLILESGSPGLQTEEERA--ARRQNDEQL--AQRFEQEGLEAFLddwyqqplfasqknLPPEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 175 DHSLIddEMKKGYSApfyddrifPALTRMIRDregdlSST--------ELQKIETPTLLIWGEKDRVVpVHVGHRLHKDL 246
Cdd:TIGR03695 157 RQALR--AERLANNP--------EGLAKMLRA-----TGLgkqpslwpKLQALKIPVLYLCGERDEKF-VQIAKEMQKLI 220
|
250 260 270
....*....|....*....|....*....|
gi 446937948 247 PNSKFISYENTGHLLPEEKPEHVYEEIIAF 276
Cdd:TIGR03695 221 PNLTLHIIPNAGHNIHLENPEAFAKILLAF 250
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
33-278 |
4.73e-15 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 73.62 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFK------YSYHNLATIIIDLIEHLSLSNIVLVGH 106
Cdd:PLN02824 30 PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSappnsfYTFETWGEQLNDFCSDVVGDPAFVICN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 107 SMGGQISLYVNRIRPELISKTILLCSSsylaratLPLLYSSYLPFF------------------HLYVKNWIIRRGIVHN 168
Cdd:PLN02824 110 SVGGVVGLQAAVDAPELVRGVMLINIS-------LRGLHIKKQPWLgrpfikafqnllretavgKAFFKSVATPETVKNI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 169 LMNVVHDHSLIDDEMKKGYSAPFYDDRIFPALTRMIRDREGDLSSTELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPN 248
Cdd:PLN02824 183 LCQCYHDDSAVTDELVEAILRPGLEPGAVDVFLDFISYSGGPLPEELLPAVKCPVLIAWGEKDPWEPVELGRAYANFDAV 262
|
250 260 270
....*....|....*....|....*....|
gi 446937948 249 SKFISYENTGHLLPEEKPEHVYEEIIAFSA 278
Cdd:PLN02824 263 EDFIVLPGVGHCPQDEAPELVNPLIESFVA 292
|
|
| PRK03204 |
PRK03204 |
haloalkane dehalogenase; Provisional |
33-275 |
9.05e-14 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179554 [Multi-domain] Cd Length: 286 Bit Score: 69.89 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFKYSYHNLATIIIDLIEHLSLSNIVLVGHSMGGQI 112
Cdd:PRK03204 35 PPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGFGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 113 SLYVNRIRPELISKTIL----LCSSSYLARATLPLLYSSYLPFFHLYVKNWIIRR----GIVHNLMNVVHDHsliddemk 184
Cdd:PRK03204 115 SMAVAVERADRVRGVVLgntwFWPADTLAMKAFSRVMSSPPVQYAILRRNFFVERlipaGTEHRPSSAVMAH-------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 185 kgYSA--PFYDDR----IFPALTRMIRDREGDLSSTELQKIET-PTLLIWGEKDRVV-PVHVGHRLHKDLPNSKFISYEN 256
Cdd:PRK03204 187 --YRAvqPNAAARrgvaEMPKQILAARPLLARLAREVPATLGTkPTLLVWGMKDVAFrPKTILPRLRATFPDHVLVELPN 264
|
250
....*....|....*....
gi 446937948 257 TGHLLPEEKPEHVYEEIIA 275
Cdd:PRK03204 265 AKHFIQEDAPDRIAAAIIE 283
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
33-259 |
2.60e-13 |
|
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: 67.92 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFkysyhNLATIIIDLIEHLSlSNIVLVGHSMGGQI 112
Cdd:TIGR01738 5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPL-----SLADMAEAIAAQAP-DPAIWLGWSLGGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 113 SLYVNRIRPELISKTILLCSSS-YLARATLP--LLYSSYLPFFHLYVKNW--IIRRGIVHNLMNVVHDHSLIDDEMKKGY 187
Cdd:TIGR01738 79 ALHIAATHPDRVRALVTVASSPcFSAREDWPegIKPDVLTGFQQQLSDDYqrTIERFLALQTLGTPTARQDARALKQTLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446937948 188 SAPFYDDRIFPALTRMIrdREGDLSStELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPNSKFISYENTGH 259
Cdd:TIGR01738 159 ARPTPNVQVLQAGLEIL--ATVDLRQ-PLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAH 227
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
32-265 |
3.27e-13 |
|
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: 67.24 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 32 RPTFVLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPFGKSD--KSHL--FKYSYHNLATIIIDLIEHLSLSNIVLVGH 106
Cdd:pfam12146 4 RAVVVLVHGLGEHSGRYAHLADALAAQGfAVYAYDHRGHGRSDgkRGHVpsFDDYVDDLDTFVDKIREEHPGLPLFLLGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 107 SMGGQISLYVNRIRPELISKTILlcSSSYLARAtlPLLYSSYLPFFhLYVKNWIIRRGIVHNLMNVvhdHSLIDD--EMK 184
Cdd:pfam12146 84 SMGGLIAALYALRYPDKVDGLIL--SAPALKIK--PYLAPPILKLL-AKLLGKLFPRLRVPNNLLP---DSLSRDpeVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 185 KGYSAPFYDDRIFPALTRMIRDReGDLSSTELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPNS--KFISYENTGHLLP 262
Cdd:pfam12146 156 AYAADPLVHGGISARTLYELLDA-GERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPGLYHELL 234
|
...
gi 446937948 263 EEK 265
Cdd:pfam12146 235 NEP 237
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
10-275 |
1.04e-11 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 63.40 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 10 FTFSTR-GTTIHYELY-EHDNKTERPTFVLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPFGKSDKshlfKYSYHNLA 86
Cdd:COG1073 13 VTFKSRdGIKLAGDLYlPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGfNVLAFDYRGYGESEG----EPREEGSP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 87 TI--IIDLIEHLSL------SNIVLVGHSMGGQISLYVNRIRPElISKTILLCS-SSY--LARATLPLLYSSYLPFFhly 155
Cdd:COG1073 89 ERrdARAAVDYLRTlpgvdpERIGLLGISLGGGYALNAAATDPR-VKAVILDSPfTSLedLAAQRAKEARGAYLPGV--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 156 vknwiirrgivhNLMNVVHDHSLIDDEmkkgysapfyddriFPALTRmirdregdlssteLQKIETPTLLIWGEKDRVVP 235
Cdd:COG1073 165 ------------PYLPNVRLASLLNDE--------------FDPLAK-------------IEKISRPLLFIHGEKDEAVP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446937948 236 VHVGHRLHKDLPNSK-FISYENTGHLLPEEKPEHVYEEIIA 275
Cdd:COG1073 206 FYMSEDLYEAAAEPKeLLIVPGAGHVDLYDRPEEEYFDKLA 246
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
16-124 |
1.12e-11 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 63.86 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 16 GTTIHYElyEHDnktERPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFkYSYHNLATIIIDLIEH 95
Cdd:PRK03592 16 GSRMAYI--ETG---EGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDID-YTFADHARYLDAWFDA 89
|
90 100
....*....|....*....|....*....
gi 446937948 96 LSLSNIVLVGHSMGGQISLYVNRIRPELI 124
Cdd:PRK03592 90 LGLDDVVLVGHDWGSALGFDWAARHPDRV 118
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
33-267 |
1.15e-11 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 64.13 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 33 PTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDK---SHLFKYSYHNLATIIIDLIEHLSLSNIVLVGHSMG 109
Cdd:PLN03084 128 PPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKpqpGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQGYF 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 110 GQISLYVNRIRPELISKTILLCSSSYLARATLPLLYSSYLPFFHLYVKNWIIRRGIVHNLMNVVHDHSLIDDEM--KKGY 187
Cdd:PLN03084 208 SPPVVKYASAHPDKIKKLILLNPPLTKEHAKLPSTLSEFSNFLLGEIFSQDPLRASDKALTSCGPYAMKEDDAMvyRRPY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 188 ----SAPFYDDRIFPALTRMIRDREGDLSSTELQKI-ETPTLLIWGEKDRVVPVHVGHRLHKDLpNSKFISYENTGHLLP 262
Cdd:PLN03084 288 ltsgSSGFALNAISRSMKKELKKYIEEMRSILTDKNwKTPITVCWGLRDRWLNYDGVEDFCKSS-QHKLIELPMAGHHVQ 366
|
....*
gi 446937948 263 EEKPE 267
Cdd:PLN03084 367 EDCGE 371
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
36-132 |
3.51e-11 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 58.69 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 36 VLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPfgksdkshlFKYSYHNLATIIIDLIEHLS----LSNIVLVGHSMGG 110
Cdd:COG1075 9 VLVHGLGGSAASWAPLAPRLRAAGyPVYALNYPS---------TNGSIEDSAEQLAAFVDAVLaatgAEKVDLVGHSMGG 79
|
90 100
....*....|....*....|....
gi 446937948 111 QISLYV--NRIRPELISKTILLCS 132
Cdd:COG1075 80 LVARYYlkRLGGAAKVARVVTLGT 103
|
|
| PRK10673 |
PRK10673 |
esterase; |
28-130 |
4.75e-08 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 52.81 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 28 NKTERPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHlfKYSYHNLATIIIDLIEHLSLSNIVLVGHS 107
Cdd:PRK10673 12 NPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDP--VMNYPAMAQDLLDTLDALQIEKATFIGHS 89
|
90 100
....*....|....*....|...
gi 446937948 108 MGGQISLYVNRIRPELISKTILL 130
Cdd:PRK10673 90 MGGKAVMALTALAPDRIDKLVAI 112
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
23-133 |
6.50e-08 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 53.71 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 23 LYEHDNKTERPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKS-------DKSHLFKYSYHNLATIIIDLIEH 95
Cdd:PLN02980 1362 VHEVGQNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhakETQTEPTLSVELVADLLYKLIEH 1441
|
90 100 110
....*....|....*....|....*....|....*...
gi 446937948 96 LSLSNIVLVGHSMGGQISLYVNRIRPELISKTILLCSS 133
Cdd:PLN02980 1442 ITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIISGS 1479
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
7-119 |
7.85e-07 |
|
Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain] Cd Length: 275 Bit Score: 49.16 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 7 CPYFTFSTRGTTIHYELYehdnKTERPTFVLVHGFLSSSF--SYRRLIP-LLSKAGT-VIALD---------------LP 67
Cdd:cd00707 15 CPQLLFADDPSSLKNSNF----NPSRPTRFIIHGWTSSGEesWISDLRKaYLSRGDYnVIVVDwgrganpnypqavnnTR 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446937948 68 PFGKsdkshlfkysyhNLATIIIDLIEH--LSLSNIVLVGHSMGGQISLY--------VNRI 119
Cdd:cd00707 91 VVGA------------ELAKFLDFLVDNtgLSLENVHLIGHSLGAHVAGFagkrlngkLGRI 140
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
27-135 |
2.76e-06 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 47.98 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 27 DNKTERPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFKYSYHNLATIIIDLIEHL----SLSNIV 102
Cdd:PLN02894 100 DSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTEETEAWFIDSFEEWrkakNLSNFI 179
|
90 100 110
....*....|....*....|....*....|...
gi 446937948 103 LVGHSMGGQISLYVNRIRPELISKTILLCSSSY 135
Cdd:PLN02894 180 LLGHSFGGYVAAKYALKHPEHVQHLILVGPAGF 212
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
13-259 |
2.77e-06 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 47.27 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 13 STRGTTIHYELYEHDNKTERPTFVLVHGFLSSSFSYRRLIPLLSKAG-TVIALDLPPFGKSDKS------HLFKYSYHNL 85
Cdd:COG0412 10 TPDGVTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGyVVLAPDLYGRGGPGDDpdearaLMGALDPELL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 86 ATIIIDLIEHL------SLSNIVLVGHSMGGQISLYVNRIRPELisktillcsssylaRATlpllyssylpffhlyvknw 159
Cdd:COG0412 90 AADLRAALDWLkaqpevDAGRVGVVGFCFGGGLALLAAARGPDL--------------AAA------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 160 iirrgivhnlmnvvhdhsliddemkkgysAPFYddrifPALTRmirdregDLSSTELQKIETPTLLIWGEKDRVVPVHVG 239
Cdd:COG0412 137 -----------------------------VSFY-----GGLPA-------DDLLDLAARIKAPVLLLYGEKDPLVPPEQV 175
|
250 260
....*....|....*....|....
gi 446937948 240 HRLHKDL----PNSKFISYENTGH 259
Cdd:COG0412 176 AALEAALaaagVDVELHVYPGAGH 199
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
61-276 |
5.83e-06 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 47.05 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 61 VIALDLPPFGKSDKSHLFKYSYHNLATiiiDLIEHLS-------LSNI--VLVGHSMGGQISLYVNRIRPELISKTILLC 131
Cdd:PLN02385 118 VFAMDYPGFGLSEGLHGYIPSFDDLVD---DVIEHYSkikgnpeFRGLpsFLFGQSMGGAVALKVHLKQPNAWDGAILVA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 132 SSSYLARATLPllyssylPffhlyvknWIIRRGIVhNLMNVVHDHSLIDD---------EMKKGYSAPF----YDD--RI 196
Cdd:PLN02385 195 PMCKIADDVVP-------P--------PLVLQILI-LLANLLPKAKLVPQkdlaelafrDLKKRKMAEYnviaYKDkpRL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 197 FPALtRMIRDREgDLSStELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPNS--KFISYENTGHLLPEEKPE----HVY 270
Cdd:PLN02385 259 RTAV-ELLRTTQ-EIEM-QLEEVSLPLLILHGEADKVTDPSVSKFLYEKASSSdkKLKLYEDAYHSILEGEPDemifQVL 335
|
....*.
gi 446937948 271 EEIIAF 276
Cdd:PLN02385 336 DDIISW 341
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
32-115 |
8.57e-06 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 45.99 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 32 RPTFVLVHGFLSSSFSYRRLIPLLSKAgTVIALDLPPFGKSDKshlfkYSYHNLATI---IIDLIEHLSLSNIVLVGHSM 108
Cdd:PRK11126 2 LPWLVFLHGLLGSGQDWQPVGEALPDY-PRLYIDLPGHGGSAA-----ISVDGFADVsrlLSQTLQSYNILPYWLVGYSL 75
|
....*..
gi 446937948 109 GGQISLY 115
Cdd:PRK11126 76 GGRIAMY 82
|
|
| COG4757 |
COG4757 |
Predicted alpha/beta hydrolase [General function prediction only]; |
10-250 |
3.38e-04 |
|
Predicted alpha/beta hydrolase [General function prediction only];
Pssm-ID: 443790 [Multi-domain] Cd Length: 289 Bit Score: 41.41 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 10 FTFSTR-GTTIHYELYEHDNkTERPTfVLVHG--FLSSSFsYRRLIPLLSKAG-TVIALDLPPFGKSDKSHL--FKYSYH 83
Cdd:COG4757 10 VTITAAdGYPLAARLFPPAG-PPRAV-VLINPatGVPQRF-YRPFARYLAERGfAVLTYDYRGIGLSRPGSLrgFDAGYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 84 NLATI----IIDLIEHLSLSN-IVLVGHSMGGQ-ISLYVNrirPELISKTILLCSSS-YLARATLPLLYSSYLpFFHLYV 156
Cdd:COG4757 87 DWGELdlpaVLDALRARFPGLpLLLVGHSLGGQlLGLAPN---AERVDRLVTVASGSgYWRDYPPRRRLKVLL-FWHLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 157 KnWIIRR---------GIVHNL-MNVVHD--HSLiddeMKKGYSAPFYDDRIFPAltrmirdregdlssteLQKIETPTL 224
Cdd:COG4757 163 P-LLTRLlgyfpgrrlGFGEDLpAGVARQwrRWC----RRPRYFFDDDGEDLEAA----------------LAAVTAPVL 221
|
250 260
....*....|....*....|....*.
gi 446937948 225 LIWGEKDRVVPVHVGHRLHKDLPNSK 250
Cdd:COG4757 222 AISFTDDELAPPAAVDRLLAYYPNAP 247
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
32-112 |
7.75e-04 |
|
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: 40.84 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446937948 32 RPTFVLVHGFLSSSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLfkySYHNLATIIIDLIEHLSLS-NIVLVGHSMGG 110
Cdd:COG3319 601 GPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPPA---SVEEMAARYVEAIRAVQPEgPYHLLGWSFGG 677
|
..
gi 446937948 111 QI 112
Cdd:COG3319 678 LV 679
|
|
| Abhydrolase_4 |
pfam08386 |
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ... |
215-259 |
3.35e-03 |
|
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.
Pssm-ID: 429964 [Multi-domain] Cd Length: 98 Bit Score: 36.16 E-value: 3.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446937948 215 ELQKIETPTLLIWGEKDRVVPVHVGHRLHKDLPNSKFISYENTGH 259
Cdd:pfam08386 28 STAKGAPPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGH 72
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
44-116 |
4.85e-03 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 37.52 E-value: 4.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446937948 44 SSFSYRRLIPLLSKAGTVIALDLPPFGKSDKSHLFKySYHNLATIIIDLIEHLSLSNIVLVGHSMGGQISLYV 116
Cdd:COG3208 18 SASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLT-SLEELADDLAEELAPLLDRPFALFGHSMGALLAFEL 89
|
|
| |
