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Conserved domains on  [gi|1447699767|ref|NP_312282|]
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pimeloyl-ACP methyl ester carboxylesterase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

pimeloyl-ACP methyl ester esterase BioH( domain architecture ID 10793379)

pimeloyl-ACP methyl ester esterase BioH removes the methyl group introduced by BioC when the pimeloyl moiety is complete

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
1-256 0e+00

pimeloyl-ACP methyl ester esterase BioH;


:

Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 541.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLAEMAEAVLRQAPDKAIWLG 80
Cdd:PRK10349    1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160
Cdd:PRK10349   81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240
Cdd:PRK10349  161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240

                         250
                  ....*....|....*.
gi 1447699767 241 HPVEFRHVLVALKQRV 256
Cdd:PRK10349  241 HPAEFCHLLVALKQRV 256
 
Name Accession Description Interval E-value
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
1-256 0e+00

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 541.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLAEMAEAVLRQAPDKAIWLG 80
Cdd:PRK10349    1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160
Cdd:PRK10349   81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240
Cdd:PRK10349  161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240

                         250
                  ....*....|....*.
gi 1447699767 241 HPVEFRHVLVALKQRV 256
Cdd:PRK10349  241 HPAEFCHLLVALKQRV 256
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 10-253 1.24e-142

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: 399.58  E-value: 1.24e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  10 GQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLAEMAEAVLRQAPDKAIWLGWSLGGLVAS 89
Cdd:TIGR01738   1 GQGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  90 QIALTHPERVQALVTVASSPCFSARDEWP-GIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLAL 168
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSAREDWPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTLLAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 169 PMPEVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPVEFRHV 248
Cdd:TIGR01738 161 PTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAFCAL 240


                  ....*
gi 1447699767 249 LVALK 253
Cdd:TIGR01738 241 LVAFK 245
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 15-242 1.32e-38

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: 134.94  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  15 HLVLLHGWGLNAEVWRCIDEELS-SHFTLHLVDLPGFGRSR------GFGALSLAEMAEAVLRQAP-DKAIWLGWSLGGL 86
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSrpkaqdDYRTDDLAEDLEYILEALGlEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  87 VASQIALTHPERVQALVTVAS-SPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTV 165
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGAlDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 166 L-------ALPMPEVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPF 238
Cdd:pfam00561 162 KrfpsgdyALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 1447699767 239 ISHP 242
Cdd:pfam00561 242 LEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-251 1.26e-33

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: 121.26  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   3 NIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS----RGFGALSLAEMAEAVLRQAP-DKAI 77
Cdd:COG0596    13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSdkpaGGYTLDDLADDLAALLDALGlERVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  78 WLGWSLGGLVASQIALTHPERVQALVTVAsspcfsardewpgikpDVLAGFQQQLSDDFQRtverflalqtmgtetarqd 157
Cdd:COG0596    93 LVGHSMGGMVALELAARHPERVAGLVLVD----------------EVLAALAEPLRRPGLA------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 158 aralkktvlalpmpeVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAP 237
Cdd:COG0596   138 ---------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                         250
                  ....*....|....
gi 1447699767 238 FISHPVEFRHVLVA 251
Cdd:COG0596   203 PLEQPEAFAAALRD 216
 
Name Accession Description Interval E-value
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
1-256 0e+00

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 541.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLAEMAEAVLRQAPDKAIWLG 80
Cdd:PRK10349    1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160
Cdd:PRK10349   81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240
Cdd:PRK10349  161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240

                         250
                  ....*....|....*.
gi 1447699767 241 HPVEFRHVLVALKQRV 256
Cdd:PRK10349  241 HPAEFCHLLVALKQRV 256
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 10-253 1.24e-142

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: 399.58  E-value: 1.24e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  10 GQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLAEMAEAVLRQAPDKAIWLGWSLGGLVAS 89
Cdd:TIGR01738   1 GQGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  90 QIALTHPERVQALVTVASSPCFSARDEWP-GIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLAL 168
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSAREDWPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTLLAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 169 PMPEVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPVEFRHV 248
Cdd:TIGR01738 161 PTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAFCAL 240


                  ....*
gi 1447699767 249 LVALK 253
Cdd:TIGR01738 241 LVAFK 245
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 15-242 1.32e-38

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: 134.94  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  15 HLVLLHGWGLNAEVWRCIDEELS-SHFTLHLVDLPGFGRSR------GFGALSLAEMAEAVLRQAP-DKAIWLGWSLGGL 86
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSrpkaqdDYRTDDLAEDLEYILEALGlEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  87 VASQIALTHPERVQALVTVAS-SPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTV 165
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGAlDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 166 L-------ALPMPEVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPF 238
Cdd:pfam00561 162 KrfpsgdyALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 1447699767 239 ISHP 242
Cdd:pfam00561 242 LEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-251 1.26e-33

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: 121.26  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   3 NIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS----RGFGALSLAEMAEAVLRQAP-DKAI 77
Cdd:COG0596    13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSdkpaGGYTLDDLADDLAALLDALGlERVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  78 WLGWSLGGLVASQIALTHPERVQALVTVAsspcfsardewpgikpDVLAGFQQQLSDDFQRtverflalqtmgtetarqd 157
Cdd:COG0596    93 LVGHSMGGMVALELAARHPERVAGLVLVD----------------EVLAALAEPLRRPGLA------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 158 aralkktvlalpmpeVDVLNGGLEILKTVDLRLPLQNVPMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAP 237
Cdd:COG0596   138 ---------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                         250
                  ....*....|....
gi 1447699767 238 FISHPVEFRHVLVA 251
Cdd:COG0596   203 PLEQPEAFAAALRD 216
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 16-109 1.16e-14

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: 71.48  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLAEMAEAV-------LRQAPDKAIWL-GWSLGGLV 87
Cdd:TIGR03695   5 LVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAqlllatlLDQLGIEPFFLvGYSMGGRI 84

                          90       100
                  ....*....|....*....|..
gi 1447699767  88 ASQIALTHPERVQALVTVASSP 109
Cdd:TIGR03695  85 ALYYALQYPERVQGLILESGSP 106
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 16-237 3.84e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 71.13  E-value: 3.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS-RGFGALSLAEMAEAVLR----QAPDKAIWLGWSLGGLVASQ 90
Cdd:PRK14875  134 VVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAfldaLGIERAHLVGHSMGGAVALR 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  91 IALTHPERVQALVTVASSPCfsardeWPGIKPDVLAGF-------------------QQQLSDDFQRTVERFLALqtmgt 151
Cdd:PRK14875  214 LAARAPQRVASLTLIAPAGL------GPEINGDYIDGFvaaesrrelkpvlellfadPALVTRQMVEDLLKYKRL----- 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 152 ETARQDARALKKTVLAlpmpevdvlnGGLEilkTVDLRLPLQNVPMPFLRLYGYLDGLVPrkvvpmldklWPHSES---- 227
Cdd:PRK14875  283 DGVDDALRALADALFA----------GGRQ---RVDLRDRLASLAIPVLVIWGEQDRIIP----------AAHAQGlpdg 339

                         250
                  ....*....|...
gi 1447699767 228 ---YIFAKAAHAP 237
Cdd:PRK14875  340 vavHVLPGAGHMP 352
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
5-129 7.42e-14

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 68.49  E-value: 7.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   5 WWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSH-FTLHLVDLPGFGRSRGFGALS---------LAEMAEAVLRQAPD 74
Cdd:COG2267    20 RWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVdsfddyvddLRAALDALRARPGL 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1447699767  75 KAIWLGWSLGGLVASQIALTHPERVQALvtVASSPCFsARDEWPGIKPDVLAGFQ 129
Cdd:COG2267   100 PVVLLGHSMGGLIALLYAARYPDRVAGL--VLLAPAY-RADPLLGPSARWLRALR 151
PLN02578 PLN02578
hydrolase
 3-250 2.83e-10

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 59.47  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   3 NIW-WQT-------KGQGnVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRG----FGALSLAEMAEAVLR 70
Cdd:PLN02578   69 NFWtWRGhkihyvvQGEG-LPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKalieYDAMVWRDQVADFVK 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  71 Q-APDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSA----RDEWPGIKPDVLAGFQ-QQLSDDFQRTVERFL 144
Cdd:PLN02578  148 EvVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSesreKEEAIVVEETVLTRFVvKPLKEWFQRVVLGFL 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767 145 ALQtmgtetARQDAR---ALKKT-----------VLALPMPEVDVlNGGlEI---------LKTVDLRLP--LQNVPMPF 199
Cdd:PLN02578  228 FWQ------AKQPSRiesVLKSVykdksnvddylVESITEPAADP-NAG-EVyyrlmsrflFNQSRYTLDslLSKLSCPL 299

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1447699767 200 LRLYGYLDGLVPRKVVPMLDKLWPHSeSYIFAKAAHAPFISHPVEFRHVLV 250
Cdd:PLN02578  300 LLLWGDLDPWVGPAKAEKIKAFYPDT-TLVNLQAGHCPHDEVPEQVNKALL 349
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 16-107 1.22e-08

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 51.37  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAEVWRCIDEELSSH-FTLHLVDLPGFGRSRGFGALSLAEMAEAVLRQAPDKAIWL-GWSLGGLVASQIA- 92
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLvGHSMGGLVARYYLk 87

                          90
                  ....*....|....*.
gi 1447699767  93 -LTHPERVQALVTVAS 107
Cdd:COG1075    88 rLGGAAKVARVVTLGT 103
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 16-122 4.11e-07

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 49.39  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAEVWRcidEELSSHFTLHLVDLPGFGRSRG--FGALSLAEMAEAVLR-QAPDKAIWLGWSLGGLVASQiA 92
Cdd:pfam12697   1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSPppLDLADLADLAALLDElGAARPVVLVGHSLGGAVALA-A 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1447699767  93 LTHPERVQALVTVASSPCFSARDEWPGIKP 122
Cdd:pfam12697  77 AAAALVVGVLVAPLAAPPGLLAALLALLAR 106
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 16-118 4.33e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 50.29  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAEVW-RCIDEeLSSHFTLHLVDLPGFGRSR--GFGALSlAEMAEAVL-------RQAP--DKAIWLGWSL 83
Cdd:PLN02894  108 LVMVHGYGASQGFFfRNFDA-LASRFRVIAIDQLGWGGSSrpDFTCKS-TEETEAWFidsfeewRKAKnlSNFILLGHSF 185

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1447699767  84 GGLVASQIALTHPERVQALVTVASSPCFSARDEWP 118
Cdd:PLN02894  186 GGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKS 220
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
16-138 5.47e-07

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 49.24  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAE-VWRCIDEELSSH-FTLHLVDLPGFGRSRGFGALSLAEMAEAVLRQA-------PDKAIWLGWSLGGL 86
Cdd:COG1506    26 VVYVHGGPGSRDdSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLaarpyvdPDRIGIYGHSYGGY 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1447699767  87 VASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQR 138
Cdd:COG1506   106 MALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYAA 157
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 16-103 1.75e-06

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 47.53  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAEVWRCIDEELSSHFTLhLVDLPGFGRSRGFGALSLAEMAE---AVLRQAPDKAIWL-GWSLGGLVASQI 91
Cdd:PRK11126    5 LVFLHGLLGSGQDWQPVGEALPDYPRL-YIDLPGHGGSAAISVDGFADVSRllsQTLQSYNILPYWLvGYSLGGRIAMYY 83

                          90
                  ....*....|...
gi 1447699767  92 AL-THPERVQALV 103
Cdd:PRK11126   84 ACqGLAGGLCGLI 96
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 15-191 4.27e-06

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 46.23  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  15 HLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS----RGFGALsLAEMAEAVLRQAPDKAIWL-GWSLGGLVAS 89
Cdd:pfam00975   2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGepplNSIEAL-ADEYAEALRQIQPEGPYALfGHSMGGMLAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  90 QIALTHPER---VQALVTVASSPCFSARDeWPGIKPDvLAGFQQQLsDDFQRTVERFLALQ---TMGTETARQDARALKK 163
Cdd:pfam00975  81 EVARRLERQgeaVRSLFLSDASAPHTVRY-EASRAPD-DDEVVAEF-TDEGGTPEELLEDEellSMLLPALRADYRALES 157

                         170       180
                  ....*....|....*....|....*....
gi 1447699767 164 TVL-ALPMPEVDVLNGGLEILKTVDLRLP 191
Cdd:pfam00975 158 YSCpPLDAQSATLFYGSDDPLHDADDLAE 186
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
12-122 4.28e-06

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 46.47  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  12 GNVHLVLLHGWGLNAEVWRCIDEELSSH-FTLHLVDLPGFGRSRG-FGALSLAEMAEAV------LRQAPDKAIWLGWSL 83
Cdd:COG1647    14 GRKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEdLLKTTWEDWLEDVeeayeiLKAGYDKVIVIGLSM 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1447699767  84 GGLVASQIALTHPErVQALVTVasSPCFSARDEWPGIKP 122
Cdd:COG1647    94 GGLLALLLAARYPD-VAGLVLL--SPALKIDDPSAPLLP 129
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 9-109 3.49e-05

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 44.85  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767    9 KGQGNVhLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFG---------ALSLAEMAEAVLRQ----APDK 75
Cdd:PLN02980  1368 NAEGSV-VLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQNhaketqtepTLSVELVADLLYKLiehiTPGK 1446

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1447699767   76 AIWLGWSLGGLVASQIALTHPERVQALVTVASSP 109
Cdd:PLN02980  1447 VTLVGYSMGARIALYMALRFSDKIEGAVIISGSP 1480
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 16-118 6.31e-05

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: 42.97  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGwgLNAEVWRCID--EELSSH-FTLHLVDLPGFGRSRG-------FGAL--SLAEMAEAVLRQAPD-KAIWLGWS 82
Cdd:pfam12146   7 VVLVHG--LGEHSGRYAHlaDALAAQgFAVYAYDHRGHGRSDGkrghvpsFDDYvdDLDTFVDKIREEHPGlPLFLLGHS 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1447699767  83 LGGLVASQIALTHPERVQALvtVASSPCFSARDEWP 118
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDGL--ILSAPALKIKPYLA 118
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 3-103 9.71e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 42.80  E-value: 9.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   3 NIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS-----RGFGALSL------AEMAEAVLRQ 71
Cdd:PLN02824   19 NIRYQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSdkpnpRSAPPNSFytfetwGEQLNDFCSD 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1447699767  72 -APDKAIWLGWSLGGLVASQIALTHPERVQALV 103
Cdd:PLN02824   99 vVGDPAFVICNSVGGVVGLQAAVDAPELVRGVM 131
PRK05855 PRK05855
SDR family oxidoreductase;
16-110 9.24e-04

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 40.35  E-value: 9.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS---RGFGALSLAEMAE---AVLRQ-APDKAIWL---GWslgG 85
Cdd:PRK05855   28 VVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSsapKRTAAYTLARLADdfaAVIDAvSPDRPVHLlahDW---G 104

                          90       100
                  ....*....|....*....|....*...
gi 1447699767  86 LVASQIALTHPE---RVQALVTVaSSPC 110
Cdd:PRK05855  105 SIQGWEAVTRPRaagRIASFTSV-SGPS 131
metX PRK00175
homoserine O-acetyltransferase; Provisional
 79-113 1.09e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 39.79  E-value: 1.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1447699767  79 LGWSLGGLVASQIALTHPERVQALVTVASSPCFSA 113
Cdd:PRK00175  152 VGGSMGGMQALEWAIDYPDRVRSALVIASSARLSA 186
MET2 COG2021
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ...
 79-113 1.96e-03

Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 441624 [Multi-domain]  Cd Length: 355  Bit Score: 38.92  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1447699767  79 LGWSLGGLVASQIALTHPERVQALVTVASSPCFSA 113
Cdd:COG2021   133 IGGSMGGMQALEWAVSYPDRVRRAIVIATAARLSA 167
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
60-147 2.73e-03

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 38.87  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767   60 SLAEMAEA----VLRQAPDKAIWL-GWSLGGLVASQIALTHPER---VQALVTVASSP--CFSARDEWP-GIKPDVLAgf 128
Cdd:PRK10252  1114 SLDEVCEAhlatLLEQQPHGPYHLlGYSLGGTLAQGIAARLRARgeeVAFLGLLDTWPpeTQNWREKEAnGLDPEVLA-- 1191

                           90
                   ....*....|....*....
gi 1447699767  129 qqqlsdDFQRTVERFLALQ 147
Cdd:PRK10252  1192 ------EIDREREAFLAAQ 1204
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
16-179 3.92e-03

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 37.91  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  16 LVLLHGWGLNAEVW-------RCIDEELSSH-------FTLHLVDLPGFGRSRGFGALSLAEMAEAVL-------RQAPD 74
Cdd:COG2382   115 LYLLDGGGGDEQDWfdqgrlpTILDNLIAAGkippmivVMPDGGDGGDRGTEGPGNDAFERFLAEELIpfveknyRVSAD 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  75 KAIW--LGWSLGGLVASQIALTHPERVQALVTVASSPcfsardeWPGIKPDVLAGFQQQLSDDFQRTVERFlaLQTMGT- 151
Cdd:COG2382   195 PEHRaiAGLSMGGLAALYAALRHPDLFGYVGSFSGSF-------WWPPGDADRGGWAELLAAGAPKKPLRF--YLDVGTe 265

                         170       180
                  ....*....|....*....|....*....
gi 1447699767 152 ETARQDARALKKTVLALPMP-EVDVLNGG 179
Cdd:COG2382   266 DDLLEANRALAAALKAKGYDvEYREFPGG 294
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
 15-108 9.61e-03

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 36.79  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699767  15 HLVLLHGWGLNAEVW---RCIDEelSSHFTLHLVDLPGFG--RSRGFGALSLAEMAEAV---LRQAPD--KAIWLGWSLG 84
Cdd:PLN02211   20 HFVLIHGISGGSWCWykiRCLME--NSGYKVTCIDLKSAGidQSDADSVTTFDEYNKPLidfLSSLPEneKVILVGHSAG 97

                          90       100
                  ....*....|....*....|....
gi 1447699767  85 GLVASQIALTHPERVQALVTVASS 108
Cdd:PLN02211   98 GLSVTQAIHRFPKKICLAVYVAAT 121
 
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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