NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15599166|ref|NP_252660|]
View 

hypothetical protein PA3971 [Pseudomonas aeruginosa PAO1]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 9-139 6.82e-25

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 92.31  E-value: 6.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166   9 ELVEQGFAAASFVGDLGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLN 88
Cdd:COG2050   6 ERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNIN 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15599166  89 LLRPALC-QRLLCRAEVLKAGRQVTVVEAEVFAErDGRrhLFSKATVTMAVV 139
Cdd:COG2050  86 FLRPARLgDRLTAEARVVRRGRRLAVVEVEVTDE-DGK--LVATATGTFAVL 134
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 9-139 6.82e-25

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 92.31  E-value: 6.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166   9 ELVEQGFAAASFVGDLGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLN 88
Cdd:COG2050   6 ERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNIN 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15599166  89 LLRPALC-QRLLCRAEVLKAGRQVTVVEAEVFAErDGRrhLFSKATVTMAVV 139
Cdd:COG2050  86 FLRPARLgDRLTAEARVVRRGRRLAVVEVEVTDE-DGK--LVATATGTFAVL 134
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 24-138 1.10e-23

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: 88.38  E-value: 1.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166  24 LGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPALCQRLLCRAE 103
Cdd:cd03443   2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARAR 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599166 104 VLKAGRQVTVVEAEVFAErDGRrhLFSKATVTMAV 138
Cdd:cd03443  82 VVKLGRRLAVVEVEVTDE-DGK--LVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 19-123 3.43e-11

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 56.58  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166    19 SFVGDLGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPALCQRL 98
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKV 80

                          90       100
                  ....*....|....*....|....*
gi 15599166    99 LCRAEVLKAGRQVTVVEAEVFAERD 123
Cdd:TIGR00369  81 RAIAQVVHLGRQTGVAEIEIVDEQG 105
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 50-124 2.06e-08

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 48.41  E-value: 2.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599166    50 NGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPA-LCQRLLCRAEVLKAGRQVTVVEAEVFAERDG 124
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPArLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76
PRK10254 PRK10254
proofreading thioesterase EntH;
19-126 2.64e-03

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 35.73  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166   19 SFVGDLGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPALCQRL 98
Cdd:PRK10254  19 TMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCVVGTELNATHHRPVSEGKV 98

                         90       100
                 ....*....|....*....|....*...
gi 15599166   99 LCRAEVLKAGRQVTVVEAEVFAERdGRR 126
Cdd:PRK10254  99 RGVCQPLHLGRQNQSWEIVVFDEQ-GRR 125
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 9-139 6.82e-25

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 92.31  E-value: 6.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166   9 ELVEQGFAAASFVGDLGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLN 88
Cdd:COG2050   6 ERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNIN 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15599166  89 LLRPALC-QRLLCRAEVLKAGRQVTVVEAEVFAErDGRrhLFSKATVTMAVV 139
Cdd:COG2050  86 FLRPARLgDRLTAEARVVRRGRRLAVVEVEVTDE-DGK--LVATATGTFAVL 134
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 24-138 1.10e-23

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: 88.38  E-value: 1.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166  24 LGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPALCQRLLCRAE 103
Cdd:cd03443   2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARAR 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599166 104 VLKAGRQVTVVEAEVFAErDGRrhLFSKATVTMAV 138
Cdd:cd03443  82 VVKLGRRLAVVEVEVTDE-DGK--LVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 19-123 3.43e-11

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 56.58  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166    19 SFVGDLGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPALCQRL 98
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKV 80

                          90       100
                  ....*....|....*....|....*
gi 15599166    99 LCRAEVLKAGRQVTVVEAEVFAERD 123
Cdd:TIGR00369  81 RAIAQVVHLGRQTGVAEIEIVDEQG 105
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 50-124 2.06e-08

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 48.41  E-value: 2.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599166    50 NGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPA-LCQRLLCRAEVLKAGRQVTVVEAEVFAERDG 124
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPArLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 36-123 2.32e-05

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: 40.92  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166  36 VEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPALC-QRLLCRAEVLKAGRQVTVV 114
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPgDTLTVEAEVVRVGRSSVTV 80


                ....*....
gi 15599166 115 EAEVFAERD 123
Cdd:cd03440  81 EVEVRNEDG 89
PRK10254 PRK10254
proofreading thioesterase EntH;
19-126 2.64e-03

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 35.73  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599166   19 SFVGDLGIRPLDCGPGWVEAGLDILPRHAQQNGFIHAGVQATLADHAAGAAAATLVEEGQTVLTLEFKLNLLRPALCQRL 98
Cdd:PRK10254  19 TMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCVVGTELNATHHRPVSEGKV 98

                         90       100
                 ....*....|....*....|....*...
gi 15599166   99 LCRAEVLKAGRQVTVVEAEVFAERdGRR 126
Cdd:PRK10254  99 RGVCQPLHLGRQNQSWEIVVFDEQ-GRR 125
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH