|
Name |
Accession |
Description |
Interval |
E-value |
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
13-252 |
3.56e-87 |
|
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: 258.98 E-value: 3.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 13 PALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIEPLSLDGMVQAITAQVPERAIWLGWSLGGLVAKYAAI 92
Cdd:TIGR01738 5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVALHIAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 93 HQPQQVTGLITVASSAHFIAKSEWP-GIQGKVLDGFASGLQQDFKKTLQQFLAIQAMGSDQAKQDIKQLRELLASRPLPQ 171
Cdd:TIGR01738 85 THPDRVRALVTVASSPCFSAREDWPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTLLARPTPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 172 LSALEQGLGLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQYLFASSSHAPFISEKQLFAEKVLGF 251
Cdd:TIGR01738 165 VQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAFCALLVAF 244
|
.
gi 2666255427 252 A 252
Cdd:TIGR01738 245 K 245
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
1-255 |
9.20e-80 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 240.69 E-value: 9.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 1 MSKLHFERHGSGPA-LILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIEPLSLDGMVQAITAQVPERAIWLG 79
Cdd:PRK10349 1 MNNIWWQTKGQGNVhLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 80 WSLGGLVAKYAAIHQPQQVTGLITVASSAHFIAKSEWPGIQGKVLDGFASGLQQDFKKTLQQFLAIQAMGSDQAKQDIKQ 159
Cdd:PRK10349 81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 160 LRELLASRPLPQLSALEQGLGLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQYLFASSSHAPFIS 239
Cdd:PRK10349 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240
|
250
....*....|....*.
gi 2666255427 240 EKQLFAEKVLGFARSI 255
Cdd:PRK10349 241 HPAEFCHLLVALKQRV 256
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
3-254 |
8.92e-38 |
|
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: 132.05 E-value: 8.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 3 KLHFERHG-SGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIE-PLSLDGMVQAITAQV----PERAI 76
Cdd:COG0596 13 RLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLdalgLERVV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 77 WLGWSLGGLVAKYAAIHQPQQVTGLITVAssahfiaksewpgiqgkvldgfasglqqdfkktlqqflaiqamgsdqakQD 156
Cdd:COG0596 93 LVGHSMGGMVALELAARHPERVAGLVLVD-------------------------------------------------EV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 157 IKQLRELLAsRPLPQLSALEQGLGLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQYLFASSSHAP 236
Cdd:COG0596 124 LAALAEPLR-RPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202
|
250
....*....|....*...
gi 2666255427 237 FISEKQLFAEKVLGFARS 254
Cdd:COG0596 203 PLEQPEAFAAALRDFLAR 220
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
13-240 |
1.97e-22 |
|
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: 92.57 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 13 PALILIHGWGLNGAVWQPVTELLAE-HFSVYLVDLPGFGHSPAIEPL------SLDGMVQAITAQVP-ERAIWLGWSLGG 84
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKAQddyrtdDLAEDLEYILEALGlEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 85 LVAKYAAIHQPQQVTGLITVASSAHFIAKSEWPGIQGKVLDGFASGLQQDFKKTLQ-QFLAIQAMGSDQAKQDIKQLREL 163
Cdd:pfam00561 81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLgRLVAKLLALLLLRLRLLKALPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 164 LASRP-----LPQLSALEQGLGLLQSQ--DLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQYLFASSSHAP 236
Cdd:pfam00561 161 NKRFPsgdyaLAKSLVTGALLFIETWSteLRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240
|
....
gi 2666255427 237 FISE 240
Cdd:pfam00561 241 FLEG 244
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
15-75 |
3.39e-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: 214008 Cd Length: 280 Bit Score: 37.98 E-value: 3.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2666255427 15 LILIHGWGLNGAVW------QP--VTELLAEHFSVYLVDLPGFGHSPAIEPlsLDGMVQAITAQVPERA 75
Cdd:cd12809 42 IVLIHGGGQTGTNWlntpdgRPgwASYFLEKGYEVYIVDQPGRGRSPWNPE--VGGPLAASTAETVEQR 108
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
13-252 |
3.56e-87 |
|
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: 258.98 E-value: 3.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 13 PALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIEPLSLDGMVQAITAQVPERAIWLGWSLGGLVAKYAAI 92
Cdd:TIGR01738 5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVALHIAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 93 HQPQQVTGLITVASSAHFIAKSEWP-GIQGKVLDGFASGLQQDFKKTLQQFLAIQAMGSDQAKQDIKQLRELLASRPLPQ 171
Cdd:TIGR01738 85 THPDRVRALVTVASSPCFSAREDWPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTLLARPTPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 172 LSALEQGLGLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQYLFASSSHAPFISEKQLFAEKVLGF 251
Cdd:TIGR01738 165 VQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAFCALLVAF 244
|
.
gi 2666255427 252 A 252
Cdd:TIGR01738 245 K 245
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
1-255 |
9.20e-80 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 240.69 E-value: 9.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 1 MSKLHFERHGSGPA-LILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIEPLSLDGMVQAITAQVPERAIWLG 79
Cdd:PRK10349 1 MNNIWWQTKGQGNVhLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 80 WSLGGLVAKYAAIHQPQQVTGLITVASSAHFIAKSEWPGIQGKVLDGFASGLQQDFKKTLQQFLAIQAMGSDQAKQDIKQ 159
Cdd:PRK10349 81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 160 LRELLASRPLPQLSALEQGLGLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQYLFASSSHAPFIS 239
Cdd:PRK10349 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240
|
250
....*....|....*.
gi 2666255427 240 EKQLFAEKVLGFARSI 255
Cdd:PRK10349 241 HPAEFCHLLVALKQRV 256
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
3-254 |
8.92e-38 |
|
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: 132.05 E-value: 8.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 3 KLHFERHG-SGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIE-PLSLDGMVQAITAQV----PERAI 76
Cdd:COG0596 13 RLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLdalgLERVV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 77 WLGWSLGGLVAKYAAIHQPQQVTGLITVAssahfiaksewpgiqgkvldgfasglqqdfkktlqqflaiqamgsdqakQD 156
Cdd:COG0596 93 LVGHSMGGMVALELAARHPERVAGLVLVD-------------------------------------------------EV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 157 IKQLRELLAsRPLPQLSALEQGLGLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQYLFASSSHAP 236
Cdd:COG0596 124 LAALAEPLR-RPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202
|
250
....*....|....*...
gi 2666255427 237 FISEKQLFAEKVLGFARS 254
Cdd:COG0596 203 PLEQPEAFAAALRDFLAR 220
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
9-236 |
1.18e-25 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 103.49 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 9 HGSGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHS-PAIEPLSLDGMVQAITAQV----PERAIWLGWSLG 83
Cdd:PRK14875 128 EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLdalgIERAHLVGHSMG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 84 GLVAKYAAIHQPQQVTGLITVASSAHfiakseWPGIQGKVLDGFASG-LQQDFKKTLQQFLAIQAMGSDQAKQDIKQLRE 162
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAGL------GPEINGDYIDGFVAAeSRRELKPVLELLFADPALVTRQMVEDLLKYKR 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2666255427 163 LLASRplPQLSALEQGL--GLLQSQDLRGELAQISMPWLQLYGRSDALVPKAamqqHAE-LHPAATQYLFASSSHAP 236
Cdd:PRK14875 282 LDGVD--DALRALADALfaGGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAA----HAQgLPDGVAVHVLPGAGHMP 352
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
11-251 |
3.39e-23 |
|
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: 94.59 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 11 SGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIEPLSLDGMVQA-------ITAQVP-ERAIWLGWSL 82
Cdd:TIGR03695 1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAaqlllatLLDQLGiEPFFLVGYSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 83 GGLVAKYAAIHQPQQVTGLITVASSahfiaksewPGIQGKvlDGFASGLQQDFK-------KTLQQFLAI---QAMGSDQ 152
Cdd:TIGR03695 81 GGRIALYYALQYPERVQGLILESGS---------PGLQTE--EERAARRQNDEQlaqrfeqEGLEAFLDDwyqQPLFASQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 153 AKQDIKQLRELLASRpLPQLS-----ALEqGLGLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAmQQHAELHPAATQY 227
Cdd:TIGR03695 150 KNLPPEQRQALRAER-LANNPeglakMLR-ATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIA-KEMQKLIPNLTLH 226
|
250 260
....*....|....*....|....
gi 2666255427 228 LFASSSHAPFISEKQLFAEKVLGF 251
Cdd:TIGR03695 227 IIPNAGHNIHLENPEAFAKILLAF 250
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
13-240 |
1.97e-22 |
|
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: 92.57 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 13 PALILIHGWGLNGAVWQPVTELLAE-HFSVYLVDLPGFGHSPAIEPL------SLDGMVQAITAQVP-ERAIWLGWSLGG 84
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKAQddyrtdDLAEDLEYILEALGlEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 85 LVAKYAAIHQPQQVTGLITVASSAHFIAKSEWPGIQGKVLDGFASGLQQDFKKTLQ-QFLAIQAMGSDQAKQDIKQLREL 163
Cdd:pfam00561 81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLgRLVAKLLALLLLRLRLLKALPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 164 LASRP-----LPQLSALEQGLGLLQSQ--DLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQYLFASSSHAP 236
Cdd:pfam00561 161 NKRFPsgdyaLAKSLVTGALLFIETWSteLRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFA 240
|
....
gi 2666255427 237 FISE 240
Cdd:pfam00561 241 FLEG 244
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
10-251 |
9.96e-16 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 73.88 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 10 GSGPALILIHGWGLNGAVWQPVTELLAEH-FSVYLVDLPGFGHSPAIEPLS---------LDGMVQAITAQVPERAIWLG 79
Cdd:COG2267 26 SPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVdsfddyvddLRAALDALRARPGLPVVLLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 80 WSLGGLVAKYAAIHQPQQVTGLITVASSahfiaksewpgiqgkvldgfasglqqdfkktlqqflaiqamgsdqakqdikq 159
Cdd:COG2267 106 HSMGGLIALLYAARYPDRVAGLVLLAPA---------------------------------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 160 lrelLASRPLPQLSAleqglGLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAMQQHAE-LHPAATQYLFASSSHAPFI 238
Cdd:COG2267 134 ----YRADPLLGPSA-----RWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAArLSPDVELVLLPGARHELLN 204
|
250
....*....|....
gi 2666255427 239 S-EKQLFAEKVLGF 251
Cdd:COG2267 205 EpAREEVLAAILAW 218
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
6-256 |
2.74e-14 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 70.36 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 6 FERHGSGPALILIHGWGLNGAVWQPVTELLAEH-FSVYLVDLPGFGHSP-AIEPLSLDGMVQAITAQVPE-RAIW----- 77
Cdd:COG1647 9 FFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPeDLLKTTWEDWLEDVEEAYEIlKAGYdkviv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 78 LGWSLGGLVAKYAAIHQPqQVTGLITVASSAHFIAKSEWpgiqgkvldgfasglqqdFKKTLQQFLA-IQAMGSDQAKQD 156
Cdd:COG1647 89 IGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSAP------------------LLPLLKYLARsLRGIGSDIEDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 157 IKQLRelLASRPLPQLSALEQGLgllqsQDLRGELAQISMPWLQLYGRSDALVPKAAMQQ-HAEL-HPAATQYLFASSSH 234
Cdd:COG1647 150 VAEYA--YDRTPLRALAELQRLI-----REVRRDLPKITAPTLIIQSRKDEVVPPESARYiYERLgSPDKELVWLEDSGH 222
|
250 260
....*....|....*....|...
gi 2666255427 235 APFIS-EKQLFAEKVLGFARSIV 256
Cdd:COG1647 223 VITLDkDREEVAEEILDFLERLA 245
|
|
| PLN02578 |
PLN02578 |
hydrolase |
3-225 |
7.73e-13 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 67.17 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 3 KLHFERHGSGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPA--IE---PLSLDGMVQAITAQVPERAIW 77
Cdd:PLN02578 77 KIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKalIEydaMVWRDQVADFVKEVVKEPAVL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 78 LGWSLGGLVAKYAAIHQPQQVTGLITVASSAHFIAKSEwPGIQGKVLDgfASGLQQDFKKTLQQFLAIQAMGSD--QAKQ 155
Cdd:PLN02578 157 VGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESR-EKEEAIVVE--ETVLTRFVVKPLKEWFQRVVLGFLfwQAKQ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 156 -------------DIKQLRELLA---SRPLPQLSALEQGLGLL------QS-QDLRGELAQISMPWLQLYGRSDALVPKA 212
Cdd:PLN02578 234 psriesvlksvykDKSNVDDYLVesiTEPAADPNAGEVYYRLMsrflfnQSrYTLDSLLSKLSCPLLLLWGDLDPWVGPA 313
|
250
....*....|...
gi 2666255427 213 AMQQHAELHPAAT 225
Cdd:PLN02578 314 KAEKIKAFYPDTT 326
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
12-102 |
1.30e-12 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 65.25 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 12 GPALILIHGWGLNGAVWQPVTELLAeHFSVYLVDLPGFGHSPAIEPLSLDGMVQAITAQVPERAI---WL-GWSLGGLVA 87
Cdd:PRK11126 2 LPWLVFLHGLLGSGQDWQPVGEALP-DYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNIlpyWLvGYSLGGRIA 80
|
90
....*....|....*.
gi 2666255427 88 KYAAIH-QPQQVTGLI 102
Cdd:PRK11126 81 MYYACQgLAGGLCGLI 96
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
15-109 |
4.38e-11 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 58.30 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 15 LILIHGWGLNGAVWQPVTELLAEH-FSVYLVDLPGFGHSpaIEPLS--LDGMVQAITAQVPERAIWL-GWSLGGLVAKYA 90
Cdd:COG1075 8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGS--IEDSAeqLAAFVDAVLAATGAEKVDLvGHSMGGLVARYY 85
|
90 100
....*....|....*....|.
gi 2666255427 91 AIHQ--PQQVTGLITVASSAH 109
Cdd:COG1075 86 LKRLggAAKVARVVTLGTPHH 106
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
10-149 |
6.51e-11 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 61.29 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 10 GSGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIEPLSL------------DGMVQAITAQVPERAIW 77
Cdd:PLN02824 27 TSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSAppnsfytfetwgEQLNDFCSDVVGDPAFV 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2666255427 78 LGWSLGGLVAKYAAIHQPQQVTG--LITVASSAHFIAKSEWpgiqgkvldgfasgLQQDFKKTLQQFLAIQAMG 149
Cdd:PLN02824 107 ICNSVGGVVGLQAAVDAPELVRGvmLINISLRGLHIKKQPW--------------LGRPFIKAFQNLLRETAVG 166
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
14-216 |
1.78e-10 |
|
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: 59.15 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 14 ALILIHGWGLNGAVWQPVTELLAEH-FSVYLVDLPGFGHSPA----IEPLS-----LDGMVQAITAQVPER-AIWLGWSL 82
Cdd:pfam12146 6 VVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDGkrghVPSFDdyvddLDTFVDKIREEHPGLpLFLLGHSM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 83 GGLVAKYAAIHQPQQVTGLItVASSAHFIAKSEWPGIQ---GKVLDGFASGLQqdfkktLQQFLAIQAMGSDQAKQDIKQ 159
Cdd:pfam12146 86 GGLIAALYALRYPDKVDGLI-LSAPALKIKPYLAPPILkllAKLLGKLFPRLR------VPNNLLPDSLSRDPEVVAAYA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2666255427 160 LRELLASRPLPQLsaleqGLGLLQ-SQDLRGELAQISMPWLQLYGRSDALVPKAAMQQ 216
Cdd:pfam12146 159 ADPLVHGGISART-----LYELLDaGERLLRRAAAITVPLLLLHGGADRVVDPAGSRE 211
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
15-246 |
9.57e-08 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 51.32 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 15 LILIHGWGLngaVWQPVTELLAEHFSVYLVDLPGFGHSPAiEPLSLDGMVQAITA----QVPERAIWLGWSLGGLVAKYA 90
Cdd:pfam12697 1 VVLVHGAGL---SAAPLAALLAAGVAVLAPDLPGHGSSSP-PPLDLADLADLAALldelGAARPVVLVGHSLGGAVALAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 91 AIHQPqqVTGLITVASSAHFIAKSEWPGIQGKVLDGFASGLQQDFKKTLQQFLAIQAMGSDQAkQDIKQLRELLASRPLP 170
Cdd:pfam12697 77 AAAAL--VVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWA-AALARLAALLAALALL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2666255427 171 QLSALEQGLgllqsqdlrgelaqismPWLQLYGRSDALVPkAAMQQHAELHPAATQYLFASSSHAPFISEKQLFAE 246
Cdd:pfam12697 154 PLAAWRDLP-----------------VPVLVLAEEDRLVP-ELAQRLLAALAGARLVVLPGAGHLPLDDPEEVAEA 211
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
7-251 |
1.25e-06 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 48.37 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 7 ERHGSGPALILIHGWGLNGAVWQPVTELLAEH-FSVYLVDLPGFGHSP-----AIEPLSLD--GMVQAITAQV---PERA 75
Cdd:COG1073 32 GASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESEgepreEGSPERRDarAAVDYLRTLPgvdPERI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 76 IWLGWSLGGLVAKYAAIHQPqQVTGLITVAssahfiaksewpgiqgkvldGFASglqqdfkktlqqflaIQAMGSDQAKQ 155
Cdd:COG1073 112 GLLGISLGGGYALNAAATDP-RVKAVILDS--------------------PFTS---------------LEDLAAQRAKE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 156 DIKQLRELLASRPLPQLSALeqglgLLQSQDLRGELAQISMPWLQLYGRSDALVPKAAMQQHAELHPAATQ-YLFASSSH 234
Cdd:COG1073 156 ARGAYLPGVPYLPNVRLASL-----LNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKElLIVPGAGH 230
|
250
....*....|....*...
gi 2666255427 235 A-PFISEKQLFAEKVLGF 251
Cdd:COG1073 231 VdLYDRPEEEYFDKLAEF 248
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
13-112 |
3.50e-06 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 46.93 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 13 PALILIHGWGLNGAV-WQPVTELLAEH-FSVYLVDLPGFGHSP-AIEPLSLDGMVQAI-----TAQV-PERAIWLGWSLG 83
Cdd:COG1506 24 PVVVYVHGGPGSRDDsFLPLAQALASRgYAVLAPDYRGYGESAgDWGGDEVDDVLAAIdylaaRPYVdPDRIGIYGHSYG 103
|
90 100
....*....|....*....|....*....
gi 2666255427 84 GLVAKYAAIHQPQQVTGLITVASSAHFIA 112
Cdd:COG1506 104 GYMALLAAARHPDRFKAAVALAGVSDLRS 132
|
|
| PRK05855 |
PRK05855 |
SDR family oxidoreductase; |
11-59 |
5.43e-06 |
|
SDR family oxidoreductase;
Pssm-ID: 235628 [Multi-domain] Cd Length: 582 Bit Score: 46.90 E-value: 5.43e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2666255427 11 SGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAIEPLS 59
Cdd:PRK05855 24 DRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTA 72
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
8-87 |
1.24e-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: 43.15 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 8 RHGSGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSPAiEPLSLDGM----VQAITAQVPERAIWL-GWSL 82
Cdd:COG3319 597 AGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEP-PPASVEEMaaryVEAIRAVQPEGPYHLlGWSF 675
|
....*
gi 2666255427 83 GGLVA 87
Cdd:COG3319 676 GGLVA 680
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
7-52 |
1.31e-04 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 42.52 E-value: 1.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2666255427 7 ERHGSGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHS 52
Cdd:PLN02679 83 EVTSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGAS 128
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
39-206 |
1.37e-04 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 42.43 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 39 FSVYLVDLPGFGHSPAIEPL--SLDGMVQAITAQ---VPER-------AIWLGWSLGGLVAKYAAIHQPQQVTGLITVAS 106
Cdd:PLN02385 116 YGVFAMDYPGFGLSEGLHGYipSFDDLVDDVIEHyskIKGNpefrglpSFLFGQSMGGAVALKVHLKQPNAWDGAILVAP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 107 SAHFIAKSEWPGIQGKVLDGFASGLQQDfKKTLQQFLAiqamgsDQAKQDIKQlREL-----LASRPLPQL-SALEQglg 180
Cdd:PLN02385 196 MCKIADDVVPPPLVLQILILLANLLPKA-KLVPQKDLA------ELAFRDLKK-RKMaeynvIAYKDKPRLrTAVEL--- 264
|
170 180
....*....|....*....|....*.
gi 2666255427 181 LLQSQDLRGELAQISMPWLQLYGRSD 206
Cdd:PLN02385 265 LRTTQEIEMQLEEVSLPLLILHGEAD 290
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
8-87 |
2.35e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.34 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 8 RHGSGPALILIHGWGlnGAVWQ--PVTELLAEHFSVYLVDLPGFgHSPAIEPLSLDGM----VQAITAQVPERAIWL-GW 80
Cdd:PRK10252 1064 REGDGPTLFCFHPAS--GFAWQfsVLSRYLDPQWSIYGIQSPRP-DGPMQTATSLDEVceahLATLLEQQPHGPYHLlGY 1140
|
....*..
gi 2666255427 81 SLGGLVA 87
Cdd:PRK10252 1141 SLGGTLA 1147
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
7-96 |
3.67e-04 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 40.72 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 7 ERHGSGPALILIHGW-GLNGAVWQpVTELLAEH-FSVYLVDLPGFGHSPAIEPLSLDGMVQAITAQVPERAI----WL-- 78
Cdd:COG0412 24 AGGGPRPGVVVLHEIfGLNPHIRD-VARRLAAAgYVVLAPDLYGRGGPGDDPDEARALMGALDPELLAADLRaaldWLka 102
|
90 100 110
....*....|....*....|....*....|
gi 2666255427 79 ------------GWSLGGLVAKYAAIHQPQ 96
Cdd:COG0412 103 qpevdagrvgvvGFCFGGGLALLAAARGPD 132
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
6-116 |
6.54e-04 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 40.66 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666255427 6 FERHGSGPALILIHGWGLNGAVWQPVTELLAEHFSVYLVDLPGFGHSP----------AIEPLSLDGMVQAITAQVPERA 75
Cdd:PLN02894 99 FDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSrpdftcksteETEAWFIDSFEEWRKAKNLSNF 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2666255427 76 IWLGWSLGGLVAKYAAIHQPQQVTGLITVAS---SAHFIAKSEW 116
Cdd:PLN02894 179 ILLGHSFGGYVAAKYALKHPEHVQHLILVGPagfSSESDDKSEW 222
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
15-75 |
3.39e-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: 214008 Cd Length: 280 Bit Score: 37.98 E-value: 3.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2666255427 15 LILIHGWGLNGAVW------QP--VTELLAEHFSVYLVDLPGFGHSPAIEPlsLDGMVQAITAQVPERA 75
Cdd:cd12809 42 IVLIHGGGQTGTNWlntpdgRPgwASYFLEKGYEVYIVDQPGRGRSPWNPE--VGGPLAASTAETVEQR 108
|
|
|