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Conserved domains on  [gi|1320716429|gb|AUL14925|]
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hypothetical protein BTL45_08520 [Bordetella bronchiseptica]

Protein Classification

PaaI family thioesterase( domain architecture ID 10005230)

PaaI family thioesterase is a hotdog fold thioesterase similar to Escherichia coli PaaI, a thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016836|GO:0047617
PubMed:  15307895|16061252
TCDB:  9.B.371

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 75-149 3.71e-06

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.78  E-value: 3.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320716429  75 VYQTYPPIQGIVMAELEMSWHRPiwADETTRVTATGTILRkfekRGRRYVQWEGRFRGADGQPIATLLNTFHVPE 149
Cdd:COG2050    67 ANSALPPGRRAVTIELNINFLRP--ARLGDRLTAEARVVR----RGRRLAVVEVEVTDEDGKLVATATGTFAVLP 135
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 75-149 3.71e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.78  E-value: 3.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320716429  75 VYQTYPPIQGIVMAELEMSWHRPiwADETTRVTATGTILRkfekRGRRYVQWEGRFRGADGQPIATLLNTFHVPE 149
Cdd:COG2050    67 ANSALPPGRRAVTIELNINFLRP--ARLGDRLTAEARVVR----RGRRLAVVEVEVTDEDGKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 80-147 3.04e-04

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: 37.92  E-value: 3.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320716429  80 PPIQGIVMAELEMSWHRPIWADettRVTATGTILRkfekRGRRYVQWEGRFRGADGQPIATLLNTFHV 147
Cdd:cd03443    53 PPGALAVTVDLNVNYLRPARGG---DLTARARVVK----LGRRLAVVEVEVTDEDGKLVATARGTFAV 113
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 75-149 3.71e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.78  E-value: 3.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320716429  75 VYQTYPPIQGIVMAELEMSWHRPiwADETTRVTATGTILRkfekRGRRYVQWEGRFRGADGQPIATLLNTFHVPE 149
Cdd:COG2050    67 ANSALPPGRRAVTIELNINFLRP--ARLGDRLTAEARVVR----RGRRLAVVEVEVTDEDGKLVATATGTFAVLP 135
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
19-148 5.73e-06

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 43.34  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716429  19 YAAFVEGAALGPVSFDITPAIVQEYFEASQADPALYrVDGRQAAA---PNVILP-YMTV-----PVYQTYPPIQGIVMAE 89
Cdd:COG2030     2 FEDLEVGDVLPHGGRTVTEEDIVLFAGATGDPNPIH-LDEEAAAAtgfGGRIAHgMLTLslasgLLVDDLPGTAVANLGL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1320716429  90 LEMSWHRPIWADETtrVTATGTILRKFEKRGRRYVQWEGRFRGADGQPIATLLNTFHVP 148
Cdd:COG2030    81 QEVRFLRPVRVGDT--LRARVEVLEKRESKSRGIVTLRTTVTNQDGEVVLTGEATVLVP 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 80-147 3.04e-04

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: 37.92  E-value: 3.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320716429  80 PPIQGIVMAELEMSWHRPIWADettRVTATGTILRkfekRGRRYVQWEGRFRGADGQPIATLLNTFHV 147
Cdd:cd03443    53 PPGALAVTVDLNVNYLRPARGG---DLTARARVVK----LGRRLAVVEVEVTDEDGKLVATARGTFAV 113
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 84-145 2.46e-03

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 35.53  E-value: 2.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1320716429  84 GIVMAELEMSWHRPIWADETtrVTATGTILRKfekrGRRYVQWEGRFRGADGQPIATLLNTF 145
Cdd:cd03440    44 GAVTLSLDVRFLRPVRPGDT--LTVEAEVVRV----GRSSVTVEVEVRNEDGKLVATATATF 99
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 84-140 5.23e-03

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 34.50  E-value: 5.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1320716429  84 GIVMAELEMSWHRPIWADETTRVTAtgtilrKFEKRGRRYVQWEGRFRGADGQPIAT 140
Cdd:cd00586    51 GLVVVELEIDYLRPLRLGDRLTVET------RVLRLGRKSFTFEQEIFREDGELLAT 101
 
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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