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Conserved domains on  [gi|281374963|gb|ADA64481|]
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1,4-Dihydroxy-2-naphthoyl-CoA thioesterase [Lactococcus lactis subsp. lactis KF147]

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 ...
 33-135 7.32e-20

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 79.22  E-value: 7.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  33 KMILSDFHAQPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKCEGFVNACGLLLKNGKRNHVWEIK 112
Cdd:COG2050   36 RLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVE 115

                         90       100
                 ....*....|....*....|...
gi 281374963 113 ITDENETLISQITVVNALVPQKN 135
Cdd:COG2050  116 VTDEDGKLVATATGTFAVLPKRP 138
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 33-135 7.32e-20

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 79.22  E-value: 7.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  33 KMILSDFHAQPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKCEGFVNACGLLLKNGKRNHVWEIK 112
Cdd:COG2050   36 RLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVE 115

                         90       100
                 ....*....|....*....|...
gi 281374963 113 ITDENETLISQITVVNALVPQKN 135
Cdd:COG2050  116 VTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 34-130 6.85e-18

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: 73.36  E-value: 6.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  34 MILSDFHAQPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKcEGFVNACGLLLKNGKRNHVWEIKI 113
Cdd:cd03443   18 LPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPAR-GGDLTARARVVKLGRRLAVVEVEV 96

                         90
                 ....*....|....*..
gi 281374963 114 TDENETLISQITVVNAL 130
Cdd:cd03443   97 TDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 40-121 1.77e-12

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: 59.67  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963   40 HAQPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKcEGFVNACGLLLKNGKRNHVWEIKITDENET 119
Cdd:TIGR00369  28 TLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAR-EGKVRAIAQVVHLGRQTGVAEIEIVDEQGR 106


                  ..
gi 281374963  120 LI 121
Cdd:TIGR00369 107 LC 108
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-121 1.08e-09

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: 51.49  E-value: 1.08e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281374963   44 HGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKCEGFVNACGLLLKNGKRNHVWEIKITDENETLI 121
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
42-131 1.73e-09

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 52.32  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  42 QPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKcEGFVNACGLLLKNGKRNHVWEIKITDENETLI 121
Cdd:PRK10293  48 QPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAR-EGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLC 126

                         90
                 ....*....|
gi 281374963 122 SQITVVNALV 131
Cdd:PRK10293 127 CSSRLTTAIL 136
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 33-135 7.32e-20

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 79.22  E-value: 7.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  33 KMILSDFHAQPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKCEGFVNACGLLLKNGKRNHVWEIK 112
Cdd:COG2050   36 RLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVE 115

                         90       100
                 ....*....|....*....|...
gi 281374963 113 ITDENETLISQITVVNALVPQKN 135
Cdd:COG2050  116 VTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 34-130 6.85e-18

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: 73.36  E-value: 6.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  34 MILSDFHAQPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKcEGFVNACGLLLKNGKRNHVWEIKI 113
Cdd:cd03443   18 LPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPAR-GGDLTARARVVKLGRRLAVVEVEV 96

                         90
                 ....*....|....*..
gi 281374963 114 TDENETLISQITVVNAL 130
Cdd:cd03443   97 TDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 40-121 1.77e-12

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: 59.67  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963   40 HAQPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKcEGFVNACGLLLKNGKRNHVWEIKITDENET 119
Cdd:TIGR00369  28 TLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAR-EGKVRAIAQVVHLGRQTGVAEIEIVDEQGR 106


                  ..
gi 281374963  120 LI 121
Cdd:TIGR00369 107 LC 108
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-121 1.08e-09

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: 51.49  E-value: 1.08e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281374963   44 HGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKCEGFVNACGLLLKNGKRNHVWEIKITDENETLI 121
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
42-131 1.73e-09

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 52.32  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  42 QPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKcEGFVNACGLLLKNGKRNHVWEIKITDENETLI 121
Cdd:PRK10293  48 QPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAR-EGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLC 126

                         90
                 ....*....|
gi 281374963 122 SQITVVNALV 131
Cdd:PRK10293 127 CSSRLTTAIL 136
PRK10254 PRK10254
proofreading thioesterase EntH;
42-116 1.07e-06

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 44.98  E-value: 1.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281374963  42 QPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHlNSKKCEGFVNACGLLLKNGKRNHVWEIKITDE 116
Cdd:PRK10254  48 QPFGLLHGGASAALAETLGSMAGFLMTRDGQCVVGTELNATH-HRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDE 121
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 30-127 9.85e-06

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: 41.69  E-value: 9.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  30 FSSKMILSDFHAQPHGFLNGGASLALAEITAGMASNAIGSSQYFALGQSISANHLNSKKCEGFVNACGLLLKNGKRNHVW 109
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90
                 ....*....|....*...
gi 281374963 110 EIKITDENETLISQITVV 127
Cdd:cd03440   81 EVEVRNEDGKLVATATAT 98
PLN02322 PLN02322
acyl-CoA thioesterase
 29-137 1.52e-05

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 41.97  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281374963  29 KFSSKMILSDFHAQPHGFLNGGASLALAEITAGMASNAIGSSQYFAlGQSISANHLNSKKCEGFVNACGLLLKNGKRNHV 108
Cdd:PLN02322  27 RVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVA-GIQLSINHLKSADLGDLVFAEATPVSTGKTIQV 105

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 281374963 109 WEIKI------TDENETLI--SQITVV-NALVPQKNSD 137
Cdd:PLN02322 106 WEVKLwkttdkDKANKILIssSRVTLIcNLPIPDNAKD 143
 
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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