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Conserved domains on  [gi|1694914174|ref|WP_140604774|]
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pimeloyl-ACP methyl ester esterase BioH [Litorilituus lipolyticus]

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, ...
 24-270 6.28e-78

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: 236.64  E-value: 6.28e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  24 IVFLHGWGLNSAIWQPLLDEitplLADEFEFITVDLPGFGqnNHIDLNAYSLDSICQLISENIAQPAIYLGWSLGGLVAT 103
Cdd:TIGR01738   7 LVLIHGWGMNAEVFRCLDEE----LSAHFTLHLVDLPGHG--RSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 104 KMALDFNQQVLGLISVASTPLFVEQQDaltdeiiWP-GIKPAILSSFHQQLSQDSAKTIKGFLKIQAMGSPHIRQDLKQI 182
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSARED-------WPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARAL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 183 TELVMAQPLPSKNTLDKSLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASHAPFISH 262
Cdd:TIGR01738 154 KQTLLARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSH 233


                  ....*...
gi 1694914174 263 LPEFSQIL 270
Cdd:TIGR01738 234 AEAFCALL 241
 
Name Accession Description Interval E-value
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 24-270 6.28e-78

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: 236.64  E-value: 6.28e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  24 IVFLHGWGLNSAIWQPLLDEitplLADEFEFITVDLPGFGqnNHIDLNAYSLDSICQLISENIAQPAIYLGWSLGGLVAT 103
Cdd:TIGR01738   7 LVLIHGWGMNAEVFRCLDEE----LSAHFTLHLVDLPGHG--RSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 104 KMALDFNQQVLGLISVASTPLFVEQQDaltdeiiWP-GIKPAILSSFHQQLSQDSAKTIKGFLKIQAMGSPHIRQDLKQI 182
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSARED-------WPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARAL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 183 TELVMAQPLPSKNTLDKSLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASHAPFISH 262
Cdd:TIGR01738 154 KQTLLARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSH 233


                  ....*...
gi 1694914174 263 LPEFSQIL 270
Cdd:TIGR01738 234 AEAFCALL 241
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
24-270 7.70e-74

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 226.44  E-value: 7.70e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  24 IVFLHGWGLNSAIWQPLLDEitplLADEFEFITVDLPGFGQNNhiDLNAYSLDSICQLISENIAQPAIYLGWSLGGLVAT 103
Cdd:PRK10349   16 LVLLHGWGLNAEVWRCIDEE----LSSHFTLHLVDLPGFGRSR--GFGALSLADMAEAVLQQAPDKAIWLGWSLGGLVAS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 104 KMALDFNQQVLGLISVASTPLFVEQQDaltdeiiWPGIKPAILSSFHQQLSQDSAKTIKGFLKIQAMGSPHIRQDLKQIT 183
Cdd:PRK10349   90 QIALTHPERVQALVTVASSPCFSARDE-------WPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 184 ELVMAQPLPSKNTLDKSLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASHAPFISHL 263
Cdd:PRK10349  163 KTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHP 242


                  ....*..
gi 1694914174 264 PEFSQIL 270
Cdd:PRK10349  243 AEFCHLL 249
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 23-274 4.86e-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: 120.49  E-value: 4.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  23 PIVFLHGWGLNSAIWQPLLdeitPLLADEFEFITVDLPGFGQNNHIDLNaYSLDS----ICQLISENIAQPAIYLGWSLG 98
Cdd:COG0596    25 PVVLLHGLPGSSYEWRPLI----PALAAGYRVIAPDLRGHGRSDKPAGG-YTLDDladdLAALLDALGLERVVLVGHSMG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  99 GLVATKMALDFNQQVLGLISVAstplfvEQQDALTDEIIWPGIKPAILSSFhqqlsqdsaktikgflkiqamgsphirqd 178
Cdd:COG0596   100 GMVALELAARHPERVAGLVLVD------EVLAALAEPLRRPGLAPEALAAL----------------------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 179 lkqitelvmaqplpskntldksLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASHAP 258
Cdd:COG0596   145 ----------------------LRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                         250
                  ....*....|....*.
gi 1694914174 259 FISHLPEFSQILANWL 274
Cdd:COG0596   203 PLEQPEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 23-262 6.66e-26

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: 102.20  E-value: 6.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  23 PIVFLHGWGLNSAIWQPLLDeitPLLADEFEFITVDLPGFGQN-NHIDLNAYSLDSIC----QLISENIAQPAIYLGWSL 97
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAP---ALARDGFRVIALDLRGFGKSsRPKAQDDYRTDDLAedleYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  98 GGLVATKMALDFNQQVLGLISVAS-TPLFVEQQDALTDEIIWPGIKPAILSSFHQQLSQDSAKTIKGFLKIQAMGSPHIR 176
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAlDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 177 QDLKQITELVMAQPLPSKNTLDKSLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASH 256
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*.
gi 1694914174 257 APFISH 262
Cdd:pfam00561 239 FAFLEG 244
 
Name Accession Description Interval E-value
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 24-270 6.28e-78

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: 236.64  E-value: 6.28e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  24 IVFLHGWGLNSAIWQPLLDEitplLADEFEFITVDLPGFGqnNHIDLNAYSLDSICQLISENIAQPAIYLGWSLGGLVAT 103
Cdd:TIGR01738   7 LVLIHGWGMNAEVFRCLDEE----LSAHFTLHLVDLPGHG--RSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 104 KMALDFNQQVLGLISVASTPLFVEQQDaltdeiiWP-GIKPAILSSFHQQLSQDSAKTIKGFLKIQAMGSPHIRQDLKQI 182
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSARED-------WPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARAL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 183 TELVMAQPLPSKNTLDKSLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASHAPFISH 262
Cdd:TIGR01738 154 KQTLLARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSH 233


                  ....*...
gi 1694914174 263 LPEFSQIL 270
Cdd:TIGR01738 234 AEAFCALL 241
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
24-270 7.70e-74

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 226.44  E-value: 7.70e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  24 IVFLHGWGLNSAIWQPLLDEitplLADEFEFITVDLPGFGQNNhiDLNAYSLDSICQLISENIAQPAIYLGWSLGGLVAT 103
Cdd:PRK10349   16 LVLLHGWGLNAEVWRCIDEE----LSSHFTLHLVDLPGFGRSR--GFGALSLADMAEAVLQQAPDKAIWLGWSLGGLVAS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 104 KMALDFNQQVLGLISVASTPLFVEQQDaltdeiiWPGIKPAILSSFHQQLSQDSAKTIKGFLKIQAMGSPHIRQDLKQIT 183
Cdd:PRK10349   90 QIALTHPERVQALVTVASSPCFSARDE-------WPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 184 ELVMAQPLPSKNTLDKSLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASHAPFISHL 263
Cdd:PRK10349  163 KTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHP 242


                  ....*..
gi 1694914174 264 PEFSQIL 270
Cdd:PRK10349  243 AEFCHLL 249
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 23-274 4.86e-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: 120.49  E-value: 4.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  23 PIVFLHGWGLNSAIWQPLLdeitPLLADEFEFITVDLPGFGQNNHIDLNaYSLDS----ICQLISENIAQPAIYLGWSLG 98
Cdd:COG0596    25 PVVLLHGLPGSSYEWRPLI----PALAAGYRVIAPDLRGHGRSDKPAGG-YTLDDladdLAALLDALGLERVVLVGHSMG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  99 GLVATKMALDFNQQVLGLISVAstplfvEQQDALTDEIIWPGIKPAILSSFhqqlsqdsaktikgflkiqamgsphirqd 178
Cdd:COG0596   100 GMVALELAARHPERVAGLVLVD------EVLAALAEPLRRPGLAPEALAAL----------------------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 179 lkqitelvmaqplpskntldksLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASHAP 258
Cdd:COG0596   145 ----------------------LRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                         250
                  ....*....|....*.
gi 1694914174 259 FISHLPEFSQILANWL 274
Cdd:COG0596   203 PLEQPEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 23-262 6.66e-26

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: 102.20  E-value: 6.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  23 PIVFLHGWGLNSAIWQPLLDeitPLLADEFEFITVDLPGFGQN-NHIDLNAYSLDSIC----QLISENIAQPAIYLGWSL 97
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAP---ALARDGFRVIALDLRGFGKSsRPKAQDDYRTDDLAedleYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  98 GGLVATKMALDFNQQVLGLISVAS-TPLFVEQQDALTDEIIWPGIKPAILSSFHQQLSQDSAKTIKGFLKIQAMGSPHIR 176
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAlDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 177 QDLKQITELVMAQPLPSKNTLDKSLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEHHIFEGASH 256
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*.
gi 1694914174 257 APFISH 262
Cdd:pfam00561 239 FAFLEG 244
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 23-274 3.56e-21

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: 89.58  E-value: 3.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  23 PIVFLHGWGLNSAIWQPLLdeitPLLADEFEFITVDLPGFGQN-NHIDLNAYSLDSICQLISENIAQ-----PAIYLGWS 96
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALI----EALGPHFRCLAIDLPGHGSSqSPSDIERYDFEEAAQLLLATLLDqlgiePFFLVGYS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  97 LGGLVATKMALDFNQQVLGLISVASTP-LFVE-------QQD-ALTDEIIWPGIkPAILSSFHQQ-LsqdsaktikgFLK 166
Cdd:TIGR03695  80 MGGRIALYYALQYPERVQGLILESGSPgLQTEeeraarrQNDeQLAQRFEQEGL-EAFLDDWYQQpL----------FAS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 167 IQAMgSPHIRQdlkQITELVMAQplpSKNTLDKSLSLLET---SDFRAKLAHIQQPFLRLYGRNDSlvpKTVcpKIN--- 240
Cdd:TIGR03695 149 QKNL-PPEQRQ---ALRAERLAN---NPEGLAKMLRATGLgkqPSLWPKLQALKIPVLYLCGERDE---KFV--QIAkem 216

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1694914174 241 -ALMPKSEHHIFEGASHApfiSHL--PE-FSQILANWL 274
Cdd:TIGR03695 217 qKLIPNLTLHIIPNAGHN---IHLenPEaFAKILLAFL 251
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 24-259 5.00e-13

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 66.73  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  24 IVFLHGWGLNSAiwqplldEITPLLADEFEFITVDLPGFGQNNHIDLNAYSLDSICQLISENIAQPAIYL-GWSLGGLVA 102
Cdd:pfam12697   1 VVLVHGAGLSAA-------PLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPVVLvGHSLGGAVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 103 TKMAldfnqQVLGLISVASTPLFVEqqdaltdeiiwPGIKPAILSSFHQQLSQDSAKTikgFLKIQAMGSPHIRQDLKQI 182
Cdd:pfam12697  74 LAAA-----AAALVVGVLVAPLAAP-----------PGLLAALLALLARLGAALAAPA---WLAAESLARGFLDDLPADA 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1694914174 183 TELVMAQPLPsknTLDKSLSLLETSDFRAKLAHIqqpflRLYGRNDSLVPKTVcPKINALMPKSEHHIFEGASHAPF 259
Cdd:pfam12697 135 EWAAALARLA---ALLAALALLPLAAWRDLPVPV-----LVLAEEDRLVPELA-QRLLAALAGARLVVLPGAGHLPL 202
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
15-274 1.32e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.41  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  15 LPKQAKKIPIVFLHGWGLNSAIWQPLLDEitpLLADEFEFITVDLPGFGQN-------NHIDLNAYSLDSICQLISENIA 87
Cdd:COG2267    22 RPAGSPRGTVVLVHGLGEHSGRYAELAEA---LAAAGYAVLAFDLRGHGRSdgprghvDSFDDYVDDLRAALDALRARPG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  88 QPAIYLGWSLGGLVATKMALDFNQQVLGLISVAstplfveqqdaltdeiiwpgikpailssfhqqlsqdsaktikgflki 167
Cdd:COG2267    99 LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA----------------------------------------------- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 168 qamgsPHIRQDlkqitelvmaqPLpskntLDKSLSLLETSDFRAKLAHIQQPFLRLYGRNDSLVP-KTVCPKINALMPKS 246
Cdd:COG2267   132 -----PAYRAD-----------PL-----LGPSARWLRALRLAEALARIDVPVLVLHGGADRVVPpEAARRLAARLSPDV 190

                         250       260
                  ....*....|....*....|....*....
gi 1694914174 247 EHHIFEGASHAPFISHL-PEFSQILANWL 274
Cdd:COG2267   191 ELVLLPGARHELLNEPArEEVLAAILAWL 219
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 22-279 6.96e-12

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 64.97  E-value: 6.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  22 IPIVFLHGWG--LNSaiWQPLLDEitplLADEFEFITVDLPGFGQNNHiDLNAYSLDSICQ-----LISENIAQpAIYLG 94
Cdd:PRK14875  132 TPVVLIHGFGgdLNN--WLFNHAA----LAAGRPVIALDLPGHGASSK-AVGAGSLDELAAavlafLDALGIER-AHLVG 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  95 WSLGGLVATKMALDFNQQV--LGLISVAstplfveqqdaltdeiiwpGIKPAILSSFhqqlsqdsaktIKGFLKIQAmgs 172
Cdd:PRK14875  204 HSMGGAVALRLAARAPQRVasLTLIAPA-------------------GLGPEINGDY-----------IDGFVAAES--- 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 173 phiRQDLKQITELVMAQP-LPSKNTLDKSLSLL---------------------ETSDFRAKLAHIQQPFLRLYGRNDSL 230
Cdd:PRK14875  251 ---RRELKPVLELLFADPaLVTRQMVEDLLKYKrldgvddalraladalfaggrQRVDLRDRLASLAIPVLVIWGEQDRI 327

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1694914174 231 VPKtvcPKINALMPKSEHHIFEGASHAPfisHLPEFSQILAnwLIKEFI 279
Cdd:PRK14875  328 IPA---AHAQGLPDGVAVHVLPGAGHMP---QMEAAADVNR--LLAEFL 368
PLN02578 PLN02578
hydrolase
 18-274 1.03e-10

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 61.40  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  18 QAKKIPIVFLHGWGLNSAIWQPLLdeitPLLADEFEFITVDLPGFGQNNH--IDLNAYS-LDSICQLISENIAQPAIYLG 94
Cdd:PLN02578   83 QGEGLPIVLIHGFGASAFHWRYNI----PELAKKYKVYALDLLGFGWSDKalIEYDAMVwRDQVADFVKEVVKEPAVLVG 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  95 WSLGGLVATKMALDFNQQVLGLISVASTPLF------VEQQDALTDEII-WPGIKPA-------ILSSFHQQLSQDSakT 160
Cdd:PLN02578  159 NSLGGFTALSTAVGYPELVAGVALLNSAGQFgsesreKEEAIVVEETVLtRFVVKPLkewfqrvVLGFLFWQAKQPS--R 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 161 IKGFLK-------------IQAMGSPHIRQDLKQITELVMAQPL--PSKNTLDKSLSLLETsdfraklahiqqPFLRLYG 225
Cdd:PLN02578  237 IESVLKsvykdksnvddylVESITEPAADPNAGEVYYRLMSRFLfnQSRYTLDSLLSKLSC------------PLLLLWG 304

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1694914174 226 RNDSLVPKTVCPKINALMPKSEHHIFEgASHAPFiSHLPE-FSQILANWL 274
Cdd:PLN02578  305 DLDPWVGPAKAEKIKAFYPDTTLVNLQ-AGHCPH-DEVPEqVNKALLEWL 352
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 18-121 3.81e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 53.29  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  18 QAKKIPIVFLHGWGLNSAIWQPLLDEitpLLADEFEFITVDLPGFgqNNHIDLNAYSLDSICQLISENIAQPAIYL-GWS 96
Cdd:COG1075     2 AATRYPVVLVHGLGGSAASWAPLAPR---LRAAGYPVYALNYPST--NGSIEDSAEQLAAFVDAVLAATGAEKVDLvGHS 76

                          90       100
                  ....*....|....*....|....*..
gi 1694914174  97 LGGLVATKMA--LDFNQQVLGLISVAS 121
Cdd:COG1075    77 MGGLVARYYLkrLGGAAKVARVVTLGT 103
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 24-102 2.59e-08

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 53.30  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  24 IVFLHGWGLNSAIWQPLLdeitPLLADeFEFITVDLPGFGQNNHIDLNaySLDSICQLISENIAQPAIY----LGWSLGG 99
Cdd:PRK11126    5 LVFLHGLLGSGQDWQPVG----EALPD-YPRLYIDLPGHGGSAAISVD--GFADVSRLLSQTLQSYNILpywlVGYSLGG 77


                  ...
gi 1694914174 100 LVA 102
Cdd:PRK11126   78 RIA 80
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 24-259 2.60e-06

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: 47.59  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  24 IVFLHGWGLNSAIWQPLLDEitpLLADEFEFITVDLPGFGQN----NHID-LNAYSLDSIC---QLISENIAQPAIYLGW 95
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADA---LAAQGFAVYAYDHRGHGRSdgkrGHVPsFDDYVDDLDTfvdKIREEHPGLPLFLLGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  96 SLGGLVATKMALDFNQQVLGLISVAstPLFveqqdaltdeiiwpGIKPAILSSFHQQLSQDSAKTIKGfLKIQAMGSPHI 175
Cdd:pfam12146  84 SMGGLIAALYALRYPDKVDGLILSA--PAL--------------KIKPYLAPPILKLLAKLLGKLFPR-LRVPNNLLPDS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 176 RQDLKQITELVMAQPL----PSKNTLdksLSLLETSDF-RAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALMPKSEH-- 248
Cdd:pfam12146 147 LSRDPEVVAAYAADPLvhggISARTL---YELLDAGERlLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKtl 223

                         250
                  ....*....|.
gi 1694914174 249 HIFEGASHAPF 259
Cdd:pfam12146 224 KLYPGLYHELL 234
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
14-276 1.91e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.01  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  14 TLPKQAKKIP-IVFLHGWGlnSAIWQPLLDEITPLLADEFEFITVDLPGFGQN-------NHIDLnaysLDSICQLISEN 85
Cdd:COG1506    15 YLPADGKKYPvVVYVHGGP--GSRDDSFLPLAQALASRGYAVLAPDYRGYGESagdwggdEVDDV----LAAIDYLAARP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  86 IAQP---AIYlGWSLGGLVATKMALDFNQQVLGLISVAStplfveqqdaltdeiiwpgikpaiLSSFHQQLSQdsaktik 162
Cdd:COG1506    89 YVDPdriGIY-GHSYGGYMALLAAARHPDRFKAAVALAG------------------------VSDLRSYYGT------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174 163 gflkiqamgsphirqdLKQITELVMAQPLPSKNTLDKSlSLLetsdfrAKLAHIQQPFLRLYGRNDSLVPKTVCPKI-NA 241
Cdd:COG1506   137 ----------------TREYTERLMGGPWEDPEAYAAR-SPL------AYADKLKTPLLLIHGEADDRVPPEQAERLyEA 193

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1694914174 242 LM---PKSEHHIFEGASHAPFISHLPEFSQILANWLIK 276
Cdd:COG1506   194 LKkagKPVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 23-106 1.73e-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: 42.77  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  23 PIVFLHGWGLNSAIWQPLLDEitplLADEFEFITVDLPGFgqnnhiDLNAYSLDSICQLISENIA-----QPA--IYL-G 94
Cdd:COG3319   603 PLFCVHPAGGNVLCYRPLARA----LGPDRPVYGLQAPGL------DGGEPPPASVEEMAARYVEairavQPEgpYHLlG 672

                          90
                  ....*....|..
gi 1694914174  95 WSLGGLVATKMA 106
Cdd:COG3319   673 WSFGGLVAYEMA 684
PRK05855 PRK05855
SDR family oxidoreductase;
24-76 3.85e-04

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 41.51  E-value: 3.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1694914174  24 IVFLHGWGLNSAIWqpllDEITPLLADEFEFITVDLPGFGQNNH-IDLNAYSLD 76
Cdd:PRK05855   28 VVLVHGYPDNHEVW----DGVAPLLADRFRVVAYDVRGAGRSSApKRTAAYTLA 77
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 24-123 8.33e-04

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 41.00  E-value: 8.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174   24 IVFLHGWGLNSAIWQPLLDEITPlladEFEFITVDLPGFGQN---NHIDLN----AYSLDSICQLISENIAQ----PAIY 92
Cdd:PLN02980  1374 VLFLHGFLGTGEDWIPIMKAISG----SARCISIDLPGHGGSkiqNHAKETqtepTLSVELVADLLYKLIEHitpgKVTL 1449

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1694914174   93 LGWSLGGLVATKMALDFNQQVLGLISVASTP 123
Cdd:PLN02980  1450 VGYSMGARIALYMALRFSDKIEGAVIISGSP 1480
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
206-257 1.47e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.18  E-value: 1.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1694914174 206 TSDFRAKLAHIQQPFLRLYGRNDSLVPKTVCPKINALM----PKSEHHIFEGASHA 257
Cdd:COG0412   145 ADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALaaagVDVELHVYPGAGHG 200
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 23-131 4.40e-03

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: 37.75  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  23 PIVFLHGWGLNSA-IWQPLldeiTPLLADEFEFITVDLPGFGQ-----NNHIDLNAYSLDSICQLISENiaqPAIYLGWS 96
Cdd:pfam00975   1 RPLFCFPPAGGSAsSFRSL----ARRLPPPAEVLAVQYPGRGRgepplNSIEALADEYAEALRQIQPEG---PYALFGHS 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1694914174  97 LGGLVATKMALDFNQQ---VLGLISVASTPLFVEQQDA 131
Cdd:pfam00975  74 MGGMLAFEVARRLERQgeaVRSLFLSDASAPHTVRYEA 111
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 23-132 5.71e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 37.80  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694914174  23 PIVFLHGWGLNSAIWQplldEITPLLADEFEFITVDLPGFGQNNHIDLNAYSLDSI-------CQL---ISENIAQPAIY 92
Cdd:PLN02824   31 ALVLVHGFGGNADHWR----KNTPVLAKSHRVYAIDLLGYGYSDKPNPRSAPPNSFytfetwgEQLndfCSDVVGDPAFV 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1694914174  93 LGWSLGGLVATKMALDFNQQVLG--LISVASTPLFVEQQDAL 132
Cdd:PLN02824  107 ICNSVGGVVGLQAAVDAPELVRGvmLINISLRGLHIKKQPWL 148
 
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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