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Conserved domains on  [gi|490279402|ref|WP_004175339|]
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MULTISPECIES: yersiniabactin biosynthesis thioesterase YbtT [Enterobacterales]

Protein Classification

thioesterase II family protein( domain architecture ID 10007057)

thioesterase II family protein such as gramicidin S biosynthesis protein GrsT, S-acyl fatty acid synthase thioesterase, and the surfactin synthase thioesterase subunit, which is involved in the surfactin biosynthesis pathway

CATH:  3.40.50.1820
EC:  3.1.2.-
Gene Ontology:  GO:0009058
PubMed:  3732600

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
18-248 3.97e-78

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 236.29  E-value: 3.97e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  18 TAHLVMCPFAGGSSSAFRHWQAEQLADCALSLVTWPGRDRLRHLEPLRSITQLAALLANELEASVspDTPLLLAGHSMGA 97
Cdd:COG3208    6 RLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLL--DRPFALFGHSMGA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  98 QVAFETCRLLEQRGL-APQGLIISGCHAPHLHS-ERQLSHRDDADFIAELIDIGGCSPELRENQELMSLFLPLLRADFYA 175
Cdd:COG3208   84 LLAFELARRLERRGRpLPAHLFVSGRRAPHLPRrRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADFRL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490279402 176 TESYHYDSPdvcPPLRTPALLLCGSHDREASWQQVDAWRQWLSHVTGPVVIDGDHFYPIQQARSFFTQIVRHF 248
Cdd:COG3208  164 LETYRYTPG---PPLDCPITALGGDDDPLVSPEELAAWREHTTGPFRLRVFPGGHFFLRDHPAELLALIRAAL 233
 
Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
18-248 3.97e-78

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 236.29  E-value: 3.97e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  18 TAHLVMCPFAGGSSSAFRHWQAEQLADCALSLVTWPGRDRLRHLEPLRSITQLAALLANELEASVspDTPLLLAGHSMGA 97
Cdd:COG3208    6 RLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLL--DRPFALFGHSMGA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  98 QVAFETCRLLEQRGL-APQGLIISGCHAPHLHS-ERQLSHRDDADFIAELIDIGGCSPELRENQELMSLFLPLLRADFYA 175
Cdd:COG3208   84 LLAFELARRLERRGRpLPAHLFVSGRRAPHLPRrRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADFRL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490279402 176 TESYHYDSPdvcPPLRTPALLLCGSHDREASWQQVDAWRQWLSHVTGPVVIDGDHFYPIQQARSFFTQIVRHF 248
Cdd:COG3208  164 LETYRYTPG---PPLDCPITALGGDDDPLVSPEELAAWREHTTGPFRLRVFPGGHFFLRDHPAELLALIRAAL 233
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
19-252 1.99e-69

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: 213.40  E-value: 1.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402   19 AHLVMCPFAGGSSSAFRHWQAEQLADCALSLVTWPGRDRlrHLEPLRSITQLAALLANELEASVsPDTPLLLAGHSMGAQ 98
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGR--GEPPLNSIEALADEYAEALRQIQ-PEGPYALFGHSMGGM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402   99 VAFETCRLLEQRGLAPQGLIISGCHAPHlHSERQLSHR-DDADFIAELIDIGGCSPELRENQELMSLFLPLLRADFYATE 177
Cdd:pfam00975  78 LAFEVARRLERQGEAVRSLFLSDASAPH-TVRYEASRApDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALE 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490279402  178 SYHydspdvCPPLRTP-ALLLCGSHDREASWQQVDAW-RQWLSHVTGPVVIDGDHFYPIQQarsfFTQIVRHFPHAF 252
Cdd:pfam00975 157 SYS------CPPLDAQsATLFYGSDDPLHDADDLAEWvRDHTPGEFDVHVFDGDHFYLIEH----LEAVLEIIEAKL 223
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
62-231 4.32e-05

Thioesterase; 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: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 43.37  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402    62 EPL-RSITQLAALLANELEASVsPDTPLLLAGHSMGAQVAFETCRLLEQRGLAPQGLIISGCHAPhlhserqlSHRDDAD 140
Cdd:smart00824  40 EPLpASADALVEAQAEAVLRAA-GGRPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLDTYPP--------GDPAPEG 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402   141 FIAELidiggcspeLRENQELMSLFLPLLRADFYATESYH--YDSPDVcPPLRTPALLLCGShDREASWQ--QVDAWRQW 216
Cdd:smart00824 111 WLPEL---------LRGVFEREDSFVPMDDARLTAMGAYLrlFGGWTP-GPVAAPTLLVRAS-EPLAEWPdeDPDGWRAH 179
                          170
                   ....*....|....*
gi 490279402   217 LSHVTGPVVIDGDHF 231
Cdd:smart00824 180 WPLPHTVVDVPGDHF 194
 
Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
18-248 3.97e-78

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 236.29  E-value: 3.97e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  18 TAHLVMCPFAGGSSSAFRHWQAEQLADCALSLVTWPGRDRLRHLEPLRSITQLAALLANELEASVspDTPLLLAGHSMGA 97
Cdd:COG3208    6 RLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLL--DRPFALFGHSMGA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  98 QVAFETCRLLEQRGL-APQGLIISGCHAPHLHS-ERQLSHRDDADFIAELIDIGGCSPELRENQELMSLFLPLLRADFYA 175
Cdd:COG3208   84 LLAFELARRLERRGRpLPAHLFVSGRRAPHLPRrRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADFRL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490279402 176 TESYHYDSPdvcPPLRTPALLLCGSHDREASWQQVDAWRQWLSHVTGPVVIDGDHFYPIQQARSFFTQIVRHF 248
Cdd:COG3208  164 LETYRYTPG---PPLDCPITALGGDDDPLVSPEELAAWREHTTGPFRLRVFPGGHFFLRDHPAELLALIRAAL 233
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
19-252 1.99e-69

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: 213.40  E-value: 1.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402   19 AHLVMCPFAGGSSSAFRHWQAEQLADCALSLVTWPGRDRlrHLEPLRSITQLAALLANELEASVsPDTPLLLAGHSMGAQ 98
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGR--GEPPLNSIEALADEYAEALRQIQ-PEGPYALFGHSMGGM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402   99 VAFETCRLLEQRGLAPQGLIISGCHAPHlHSERQLSHR-DDADFIAELIDIGGCSPELRENQELMSLFLPLLRADFYATE 177
Cdd:pfam00975  78 LAFEVARRLERQGEAVRSLFLSDASAPH-TVRYEASRApDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALE 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490279402  178 SYHydspdvCPPLRTP-ALLLCGSHDREASWQQVDAW-RQWLSHVTGPVVIDGDHFYPIQQarsfFTQIVRHFPHAF 252
Cdd:pfam00975 157 SYS------CPPLDAQsATLFYGSDDPLHDADDLAEWvRDHTPGEFDVHVFDGDHFYLIEH----LEAVLEIIEAKL 223
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
28-248 1.30e-08

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: 53.85  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  28 GGSSSAFRHWQAEQLADCALSLVTWPGRDRLRHLEPLRSITQLAALLANELEASvsPDTPLLLAGHSMGAQVAFETCRLL 107
Cdd:COG0596   33 PGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDAL--GLERVVLVGHSMGGMVALELAARH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402 108 EQRglaPQGLIISGchaphlhserqlshrDDADFIAELIDIGGCSPElrenqELMSLFLPLLRADFYATEsyhydspdvc 187
Cdd:COG0596  111 PER---VAGLVLVD---------------EVLAALAEPLRRPGLAPE-----ALAALLRALARTDLRERL---------- 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490279402 188 PPLRTPALLLCGSHDREASWQQVDAWRQWLSHVTGPVVIDGDHFYPIQQARsFFTQIVRHF 248
Cdd:COG0596  158 ARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPE-AFAAALRDF 217
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
62-231 1.18e-06

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: 49.32  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  62 EPLRSITQLAALLANELEAsVSPDTPLLLAGHSMGAQVAFETCRLLEQRGLAPQGLIISGCHAPHlhserQLSHRDDADF 141
Cdd:COG3319  643 PPPASVEEMAARYVEAIRA-VQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYAPG-----ALARLDEAEL 716
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402 142 IAELIDIGGCSPELRENQELMSLFLPLLRADFYATESYHYDSPD------------------------VCPPLRTPALLL 197
Cdd:COG3319  717 LAALLRDLARGVDLPLDAEELRALDPEERLARLLERLREAGLPAgldaerlrrllrvfranlralrryRPRPYDGPVLLF 796
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490279402 198 CGSHDREasWQQVDAWRQWLSHVTGPV---VIDGDHF 231
Cdd:COG3319  797 RAEEDPP--GRADDPALGWRPLVAGGLevhDVPGDHF 831
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
10-248 1.26e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 48.07  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  10 LWPARNGNTAHLVMCPFAGGSSSAFRHWqAEQLADCALSLVT--WPG-----RDRLRHLEPLRSITQLAALLAnelEASV 82
Cdd:COG2267   20 RWRPAGSPRGTVVLVHGLGEHSGRYAEL-AEALAAAGYAVLAfdLRGhgrsdGPRGHVDSFDDYVDDLRAALD---ALRA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  83 SPDTPLLLAGHSMGAQVAfetCRLLEQRGLAPQGLIIsgchaphlhserqlshrddadfiaelidiggCSPELREnQELM 162
Cdd:COG2267   96 RPGLPVVLLGHSMGGLIA---LLYAARYPDRVAGLVL-------------------------------LAPAYRA-DPLL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402 163 SLFLPLLRAdfyatesyhYDSPDVCPPLRTPALLLCGSHDREASWQQVDAWRQWLSHVTGPVVIDG-DHFYPIQQARSFF 241
Cdd:COG2267  141 GPSARWLRA---------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGaRHELLNEPAREEV 211

                 ....*..
gi 490279402 242 TQIVRHF 248
Cdd:COG2267  212 LAAILAW 218
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
62-231 4.32e-05

Thioesterase; 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: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 43.37  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402    62 EPL-RSITQLAALLANELEASVsPDTPLLLAGHSMGAQVAFETCRLLEQRGLAPQGLIISGCHAPhlhserqlSHRDDAD 140
Cdd:smart00824  40 EPLpASADALVEAQAEAVLRAA-GGRPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLDTYPP--------GDPAPEG 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402   141 FIAELidiggcspeLRENQELMSLFLPLLRADFYATESYH--YDSPDVcPPLRTPALLLCGShDREASWQ--QVDAWRQW 216
Cdd:smart00824 111 WLPEL---------LRGVFEREDSFVPMDDARLTAMGAYLrlFGGWTP-GPVAAPTLLVRAS-EPLAEWPdeDPDGWRAH 179
                          170
                   ....*....|....*
gi 490279402   217 LSHVTGPVVIDGDHF 231
Cdd:smart00824 180 WPLPHTVVDVPGDHF 194
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
29-231 6.22e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 42.85  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402   29 GSSSAFRHWQAEQLADCALSLVTWPGR-DRLRHLEPLRSITQLAALLANELEAsvspdTPLLLAGHSMGAQVAFETCRLL 107
Cdd:pfam12697   6 GAGLSAAPLAALLAAGVAVLAPDLPGHgSSSPPPLDLADLADLAALLDELGAA-----RPVVLVGHSLGGAVALAAAAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490279402  108 EQRG--LAPQGLIISGCHAPHLHSERQLSHRDDADFIAELIDIGGCSPELRENQELMSLFLPLLRADFYATESYHYDSPD 185
Cdd:pfam12697  81 LVVGvlVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALALLPLAAWRD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 490279402  186 VcpplrTPALLLCGSHDREASWQQVDAWRQWlSHVTGPVVIDGDHF 231
Cdd:pfam12697 161 L-----PVPVLVLAEEDRLVPELAQRLLAAL-AGARLVVLPGAGHL 200
 
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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