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Conserved domains on  [gi|1436945971|emb|SUA53143|]
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Surfactin synthase thioesterase subunit [Oligella urethralis]

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 ...
9-242 2.63e-54

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


:

Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 174.66  E-value: 2.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971   9 TLYCLPSAGSSASMYHPWQNLAPTHFRIKAIDYSGHGSRITEALIQHPGNLINDIADTILATHDqtKDIVLFGHSLGAgL 88
Cdd:COG3208     8 RLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLLD--RPFALFGHSMGA-L 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  89 LPF-VAQKIQKESTSQHIALmVISGRG--YRSKTRATQHELDDQnALLNFLQRYEGIPAALLTNQEALDFFFPIIKNDIL 165
Cdd:COG3208    85 LAFeLARRLERRGRPLPAHL-FVSGRRapHLPRRRRPLHDLSDA-ELLAELRRLGGTPEEVLADPELLELFLPILRADFR 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945971 166 LNNALLRLHSEMtiTTTPLLVFSGAEDRNVTLETLNEWRHLTNQWRGVEFFEGGHFYLSStkNISAMLKSILTHLQR 242
Cdd:COG3208   163 LLETYRYTPGPP--LDCPITALGGDDDPLVSPEELAAWREHTTGPFRLRVFPGGHFFLRD--HPAELLALIRAALAA 235
 
Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
9-242 2.63e-54

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 174.66  E-value: 2.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971   9 TLYCLPSAGSSASMYHPWQNLAPTHFRIKAIDYSGHGSRITEALIQHPGNLINDIADTILATHDqtKDIVLFGHSLGAgL 88
Cdd:COG3208     8 RLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLLD--RPFALFGHSMGA-L 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  89 LPF-VAQKIQKESTSQHIALmVISGRG--YRSKTRATQHELDDQnALLNFLQRYEGIPAALLTNQEALDFFFPIIKNDIL 165
Cdd:COG3208    85 LAFeLARRLERRGRPLPAHL-FVSGRRapHLPRRRRPLHDLSDA-ELLAELRRLGGTPEEVLADPELLELFLPILRADFR 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945971 166 LNNALLRLHSEMtiTTTPLLVFSGAEDRNVTLETLNEWRHLTNQWRGVEFFEGGHFYLSStkNISAMLKSILTHLQR 242
Cdd:COG3208   163 LLETYRYTPGPP--LDCPITALGGDDDPLVSPEELAAWREHTTGPFRLRVFPGGHFFLRD--HPAELLALIRAALAA 235
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
9-225 1.59e-20

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: 86.67  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971   9 TLYCLPSAGSSASMYHPWQNLAPTHFRIKAIDYSGHGSriTEALIQHPGNLINDIADTILATHDQtKDIVLFGHSLGaGL 88
Cdd:pfam00975   2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGR--GEPPLNSIEALADEYAEALRQIQPE-GPYALFGHSMG-GM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  89 LPF-VAQKIQKESTSqhIALMVISGRGYRSKTRATQHELDDQNALLNFLQRYEGIPAALLTNQEALDFFFPIIKNDILln 167
Cdd:pfam00975  78 LAFeVARRLERQGEA--VRSLFLSDASAPHTVRYEASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYR-- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436945971 168 naLLRLHSEMTITTTPLLVFSGAEDRNVTLETLNEW-RHltnQWRG---VEFFEGGHFYLSS 225
Cdd:pfam00975 154 --ALESYSCPPLDAQSATLFYGSDDPLHDADDLAEWvRD---HTPGefdVHVFDGDHFYLIE 210
 
Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
9-242 2.63e-54

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 174.66  E-value: 2.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971   9 TLYCLPSAGSSASMYHPWQNLAPTHFRIKAIDYSGHGSRITEALIQHPGNLINDIADTILATHDqtKDIVLFGHSLGAgL 88
Cdd:COG3208     8 RLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLLD--RPFALFGHSMGA-L 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  89 LPF-VAQKIQKESTSQHIALmVISGRG--YRSKTRATQHELDDQnALLNFLQRYEGIPAALLTNQEALDFFFPIIKNDIL 165
Cdd:COG3208    85 LAFeLARRLERRGRPLPAHL-FVSGRRapHLPRRRRPLHDLSDA-ELLAELRRLGGTPEEVLADPELLELFLPILRADFR 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945971 166 LNNALLRLHSEMtiTTTPLLVFSGAEDRNVTLETLNEWRHLTNQWRGVEFFEGGHFYLSStkNISAMLKSILTHLQR 242
Cdd:COG3208   163 LLETYRYTPGPP--LDCPITALGGDDDPLVSPEELAAWREHTTGPFRLRVFPGGHFFLRD--HPAELLALIRAALAA 235
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
9-225 1.59e-20

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: 86.67  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971   9 TLYCLPSAGSSASMYHPWQNLAPTHFRIKAIDYSGHGSriTEALIQHPGNLINDIADTILATHDQtKDIVLFGHSLGaGL 88
Cdd:pfam00975   2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGR--GEPPLNSIEALADEYAEALRQIQPE-GPYALFGHSMG-GM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  89 LPF-VAQKIQKESTSqhIALMVISGRGYRSKTRATQHELDDQNALLNFLQRYEGIPAALLTNQEALDFFFPIIKNDILln 167
Cdd:pfam00975  78 LAFeVARRLERQGEA--VRSLFLSDASAPHTVRYEASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYR-- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436945971 168 naLLRLHSEMTITTTPLLVFSGAEDRNVTLETLNEW-RHltnQWRG---VEFFEGGHFYLSS 225
Cdd:pfam00975 154 --ALESYSCPPLDAQSATLFYGSDDPLHDADDLAEWvRD---HTPGefdVHVFDGDHFYLIE 210
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
8-221 6.83e-09

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: 54.82  E-value: 6.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971   8 YTLYCLPSAGSSASMYHPW-QNLAPTHFRIKAIDYSGHG-SRITEALIQHPGNLINDIADTILATHDQTKdIVLFGHSLG 85
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLaPALARDGFRVIALDLRGFGkSSRPKAQDDYRTDDLAEDLEYILEALGLEK-VNLVGHSMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  86 AGLLPFVAQKIQkestsQHIALMVISGrgyrSKTRATQHELDDQNALLNFLQRYEGIPAALLTNQEA------------- 152
Cdd:pfam00561  80 GLIALAYAAKYP-----DRVKALVLLG----ALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGrlvakllallllr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971 153 LDFFFPI------IKNDILLNNALL---RLHSEMTITTT-----------PLLVFSGAEDRNVTLETLNEWRHLTNQWRG 212
Cdd:pfam00561 151 LRLLKALpllnkrFPSGDYALAKSLvtgALLFIETWSTElrakflgrldePTLIIWGDQDPLVPPQALEKLAQLFPNARL 230

                  ....*....
gi 1436945971 213 VEFFEGGHF 221
Cdd:pfam00561 231 VVIPDAGHF 239
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
9-221 6.95e-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: 51.54  E-value: 6.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971   9 TLYCLPSAGSSASMYHPWQNLAPTHFRIKAIDYSGHGSRITEALIQHPGNLINDIADtiLATHDQTKDIVLFGHSLGAGL 88
Cdd:COG0596    25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA--LLDALGLERVVLVGHSMGGMV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  89 LPFVAQKIqkestSQHIALMVISGrgyrsktratqhelDDQNALLNFLQRYEGIPAALLTNQEALDFFfpiikndillnN 168
Cdd:COG0596   103 ALELAARH-----PERVAGLVLVD--------------EVLAALAEPLRRPGLAPEALAALLRALART-----------D 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1436945971 169 ALLRLHSemtiTTTPLLVFSGAEDRNVTLETLNEWRHLTNQWRGVEFFEGGHF 221
Cdd:COG0596   153 LRERLAR----ITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHF 201
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
9-221 6.28e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 45.76  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971   9 TLYCLPSAGSSASMYHPW-QNLAPTHFRIKAIDYSGHG-SRITEALIQHPGNLINDIADTI-LATHDQTKDIVLFGHSLG 85
Cdd:COG2267    30 TVVLVHGLGEHSGRYAELaEALAAAGYAVLAFDLRGHGrSDGPRGHVDSFDDYVDDLRAALdALRARPGLPVVLLGHSMG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  86 AGLLPFVAQKIQkestsQHIALMVISGRGYRSktratqhelddqnallnflQRYEGIPAALLtnqealdfffpiikNDIL 165
Cdd:COG2267   110 GLIALLYAARYP-----DRVAGLVLLAPAYRA-------------------DPLLGPSARWL--------------RALR 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945971 166 LNNALLRLhsemtitTTPLLVFSGAEDRNVTLETLNEW-RHLTNQWRGVEFFEGGHF 221
Cdd:COG2267   152 LAEALARI-------DVPVLVLHGGADRVVPPEAARRLaARLSPDVELVLLPGARHE 201
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
23-225 1.99e-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: 44.39  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971  23 YHPWQNLAPTHFRIKAIDYSGHGSRITEALiqhpgnLINDIAD--TILATHDQTKDIVLFGHSLGAgllpFVAQKIQKES 100
Cdd:pfam12697  11 AAPLAALLAAGVAVLAPDLPGHGSSSPPPL------DLADLADlaALLDELGAARPVVLVGHSLGG----AVALAAAAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945971 101 TSQHIALMVISGRGYRSKTRATQHELDDQNALLNFLQRYEGIPAALLTNQEALDFFFPIIKNDILLNNALLRLHSEMTIT 180
Cdd:pfam12697  81 LVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALALLPLAAWRD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1436945971 181 TTPLLVFSGAEDRNVTlETLNEWRHLTNQWRGVEFFEGGHFYLSS 225
Cdd:pfam12697 161 LPVPVLVLAEEDRLVP-ELAQRLLAALAGARLVVLPGAGHLPLDD 204
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
17-88 1.72e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.77  E-value: 1.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436945971  17 GSSASMyHPW-QNLAPTHFRIKAIDYSGHGSRiTEALIQ-HPGNLINDIADTILATHDQTKDIVLFGHSLGAGL 88
Cdd:COG1647    26 GSPAEM-RPLaEALAKAGYTVYAPRLPGHGTS-PEDLLKtTWEDWLEDVEEAYEILKAGYDKVIVIGLSMGGLL 97
 
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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