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Conserved domains on  [gi|2666255427|ref|WP_329775601|]
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pimeloyl-ACP methyl ester esterase BioH [Agarivorans aestuarii]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
13-252 3.56e-87

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member TIGR01738:

Pssm-ID: 473884 [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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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