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Conserved domains on  [gi|1543041088|ref|WP_125951092|]
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MULTISPECIES: PaaI family thioesterase [unclassified Variovorax]

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 ...
 47-177 4.15e-36

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 122.36  E-value: 4.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  47 AMLNGDIPYAAIAKTLDFTILEVRQGVAIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVN 126
Cdd:COG2050     6 ERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNIN 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1543041088 127 YVKGLTPKvQRVRAEGKVIHCGKQLATAEARLYGPDGTLYAHATTTCLVFE 177
Cdd:COG2050    86 FLRPARLG-DRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLP 135
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 47-177 4.15e-36

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 122.36  E-value: 4.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  47 AMLNGDIPYAAIAKTLDFTILEVRQGVAIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVN 126
Cdd:COG2050     6 ERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNIN 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1543041088 127 YVKGLTPKvQRVRAEGKVIHCGKQLATAEARLYGPDGTLYAHATTTCLVFE 177
Cdd:COG2050    86 FLRPARLG-DRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 61-175 3.86e-32

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: 111.50  E-value: 3.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  61 TLDFTILEVRQGVAIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVNYVKglTPKVQRVRA 140
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLR--PARGGDLTA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1543041088 141 EGKVIHCGKQLATAEARLYGPDGTLYAHATTTCLV 175
Cdd:cd03443    79 RARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 57-175 2.47e-19

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: 78.93  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  57 AIAKTLDFTILEVRQGVAIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVNYVKGLTPKvq 136
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREG-- 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1543041088 137 RVRAEGKVIHCGKQLATAEARLYGPDGTLYAHATTTCLV 175
Cdd:TIGR00369  79 KVRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 88-167 4.85e-13

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: 61.50  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  88 LGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVNYVKGLTPKvQRVRAEGKVIHCGKQLATAEARLYGPDGTLYA 167
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLG-DRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 47-177 4.15e-36

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 122.36  E-value: 4.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  47 AMLNGDIPYAAIAKTLDFTILEVRQGVAIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVN 126
Cdd:COG2050     6 ERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNIN 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1543041088 127 YVKGLTPKvQRVRAEGKVIHCGKQLATAEARLYGPDGTLYAHATTTCLVFE 177
Cdd:COG2050    86 FLRPARLG-DRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 61-175 3.86e-32

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: 111.50  E-value: 3.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  61 TLDFTILEVRQGVAIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVNYVKglTPKVQRVRA 140
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLR--PARGGDLTA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1543041088 141 EGKVIHCGKQLATAEARLYGPDGTLYAHATTTCLV 175
Cdd:cd03443    79 RARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 57-175 2.47e-19

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: 78.93  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  57 AIAKTLDFTILEVRQGVAIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVNYVKGLTPKvq 136
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREG-- 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1543041088 137 RVRAEGKVIHCGKQLATAEARLYGPDGTLYAHATTTCLV 175
Cdd:TIGR00369  79 KVRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 74-174 2.04e-14

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: 65.57  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  74 AIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVNYVKGLTPKvQRVRAEGKVIHCGKQLAT 153
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPG-DTLTVEAEVVRVGRSSVT 79

                          90       100
                  ....*....|....*....|.
gi 1543041088 154 AEARLYGPDGTLYAHATTTCL 174
Cdd:cd03440    80 VEVEVRNEDGKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 88-167 4.85e-13

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: 61.50  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  88 LGTIHGGWVATMLDSALGCSVHTMMPPGRAYTTAELGVNYVKGLTPKvQRVRAEGKVIHCGKQLATAEARLYGPDGTLYA 167
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLG-DRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
80-103 3.58e-04

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 39.01  E-value: 3.58e-04
                          10        20
                  ....*....|....*....|....
gi 1543041088  80 PLPQHLNPLGTIHGGWVATMLDSA 103
Cdd:COG1607    13 VMPEDTNHHGTLFGGWLLSWMDEA 36
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 59-167 3.59e-04

phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.


Pssm-ID: 131339  Cd Length: 114  Bit Score: 38.56  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  59 AKTLDFTILEVRQGVAIFQGTPLPQHLNPLGTIHGGWVATMLDSALGCSVHTMmppGRAYTTAELGVNYVKGLTPKvQRV 138
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSY---GDAAVAAQCTIDFLRPGRAG-ERL 76

                          90       100
                  ....*....|....*....|....*....
gi 1543041088 139 RAEGKVIHCGKQLATAEARLYGPDGTLYA 167
Cdd:TIGR02286  77 EAEAVEVSRGGRTGTYDVEVVNQEGELVA 105
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 75-176 4.86e-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: 35.27  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543041088  75 IFQGTPLPQHLNPLGTIHGGWVATMLDSA-------LGCSVHTMMPPGRAYTTAELGVNYVKGLTPKvQRVRAEGKVIHC 147
Cdd:cd00586     2 TLEIRVRFGDTDAAGHVNNARYLRYFEEAreeflreLGLGYDELEEQGLGLVVVELEIDYLRPLRLG-DRLTVETRVLRL 80

                          90       100
                  ....*....|....*....|....*....
gi 1543041088 148 GKQLATAEARLYGPDGTLYAHATTTCLVF 176
Cdd:cd00586    81 GRKSFTFEQEIFREDGELLATAETVLVCV 109
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 81-107 5.09e-03

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 35.24  E-value: 5.09e-03
                          10        20
                  ....*....|....*....|....*..
gi 1543041088  81 LPQHLNPLGTIHGGWVATMLDSALGCS 107
Cdd:cd03442    15 LPEDTNHHGTIFGGWLLEWMDELAGIA 41
 
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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