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Conserved domains on  [gi|1577374679|ref|WP_130145627|]
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MULTISPECIES: thioesterase family protein [Acinetobacter]

Protein Classification

thioesterase family protein( domain architecture ID 10009353)

thioesterase family protein such as Streptomyces cattleya fluoroacetyl-CoA thioesterase that catalyzes the hydrolysis of fluoroacetyl-coenzyme A, preventing it from metabolizing to 4-hydroxy-trans-aconitate, a lethal inhibitor of the tricarboxylic acid cycle

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
4-137 2.40e-48

Predicted thioesterase [General function prediction only];


:

Pssm-ID: 444247  Cd Length: 129  Bit Score: 151.49  E-value: 2.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374679   4 NIPSGLTYTQEIIVDESLIVPQVSTkftgfaDMPPVFATAYMVGFVEWTCVEALHPYLEPQQRTVGIHVNLSHNAATPVG 83
Cdd:COG5496     1 ELKPGLTATFEFTVTEEDTAAALGS------GDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577374679  84 MKVTAEVTLTHIEGKKLTFAVICRDEVDVICEGTHERFIIDHEKFLTRVQAKSA 137
Cdd:COG5496    75 MTVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAA 128
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
4-137 2.40e-48

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 151.49  E-value: 2.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374679   4 NIPSGLTYTQEIIVDESLIVPQVSTkftgfaDMPPVFATAYMVGFVEWTCVEALHPYLEPQQRTVGIHVNLSHNAATPVG 83
Cdd:COG5496     1 ELKPGLTATFEFTVTEEDTAAALGS------GDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577374679  84 MKVTAEVTLTHIEGKKLTFAVICRDEVDVICEGTHERFIIDHEKFLTRVQAKSA 137
Cdd:COG5496    75 MTVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAA 128
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 45-118 5.91e-03

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 34.46  E-value: 5.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577374679  45 MVGFVEWTCVEALHPYLEPQQRTVGIHVNLSHNAATPVGmKVTAEVTLTHIEGKKLTFAVICRDEVD-VICEGTH 118
Cdd:cd03443    36 IATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVEVEVTDEDGkLVATARG 109
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
4-137 2.40e-48

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 151.49  E-value: 2.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374679   4 NIPSGLTYTQEIIVDESLIVPQVSTkftgfaDMPPVFATAYMVGFVEWTCVEALHPYLEPQQRTVGIHVNLSHNAATPVG 83
Cdd:COG5496     1 ELKPGLTATFEFTVTEEDTAAALGS------GDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577374679  84 MKVTAEVTLTHIEGKKLTFAVICRDEVDVICEGTHERFIIDHEKFLTRVQAKSA 137
Cdd:COG5496    75 MTVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAA 128
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 56-117 1.45e-03

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 36.46  E-value: 1.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577374679  56 ALHPYLEPQQRTVGIHVNLSHNAATPVGMKVTAEVTLTHIeGKKLTF--AVICRDEVDVICEGT 117
Cdd:COG2050    66 AANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRR-GRRLAVveVEVTDEDGKLVATAT 128
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 45-118 5.91e-03

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 34.46  E-value: 5.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577374679  45 MVGFVEWTCVEALHPYLEPQQRTVGIHVNLSHNAATPVGmKVTAEVTLTHIEGKKLTFAVICRDEVD-VICEGTH 118
Cdd:cd03443    36 IATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVEVEVTDEDGkLVATARG 109
 
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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