NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|9946336|gb|AAG03863|]
View 

hypothetical protein PA0474 [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 ...
 1-134 9.57e-28

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 99.25  E-value: 9.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336    1 MMNVPEGFQPLFRSSPLLDLLGPFFCRQDAQRqLVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAMAFSREPPQPMVT 80
Cdd:COG2050   1 MSDPLERLEGFLAANPFAELLGIELVEVEPGR-AVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9946336   81 VGLRLDFCGVARVGDWLEVHTRVDKLGQRMAFASARLHSGE-RLVASASGVFHLP 134
Cdd:COG2050  80 IELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDgKLVATATGTFAVL 134
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-134 9.57e-28

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 99.25  E-value: 9.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336    1 MMNVPEGFQPLFRSSPLLDLLGPFFCRQDAQRqLVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAMAFSREPPQPMVT 80
Cdd:COG2050   1 MSDPLERLEGFLAANPFAELLGIELVEVEPGR-AVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9946336   81 VGLRLDFCGVARVGDWLEVHTRVDKLGQRMAFASARLHSGE-RLVASASGVFHLP 134
Cdd:COG2050  80 IELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDgKLVATATGTFAVL 134
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-133 2.13e-26

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: 94.93  E-value: 2.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336   21 LGPFFCRQDAQRQLVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAMAFSREPPQPMVTVGLRLDFCGVARVGDwLEVH 100
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGD-LTAR 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 9946336  101 TRVDKLGQRMAFASARLHSGE-RLVASASGVFHL 133
Cdd:cd03443  80 ARVVKLGRRLAVVEVEVTDEDgKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-125 2.56e-15

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: 65.74  E-value: 2.56e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9946336     48 GGTAHGGLLSTLADVGLGYAMAFSREPPQPMVTVGLRLDFCGVARVGDWLEVHTRVDKLGQRMAFASARLHSGERLVA 125
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 33-125 1.78e-08

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: 48.96  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336     33 QLVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAmafSREPPQPMVTVGLRLDFCGVARVGDWLEVHTRVDKLGQRMAF 112
Cdd:TIGR02286  15 FARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYA---CNSYGDAAVAAQCTIDFLRPGRAGERLEAEAVEVSRGGRTGT 91

                          90
                  ....*....|....
gi 9946336    113 ASARL-HSGERLVA 125
Cdd:TIGR02286  92 YDVEVvNQEGELVA 105
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-134 9.57e-28

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 99.25  E-value: 9.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336    1 MMNVPEGFQPLFRSSPLLDLLGPFFCRQDAQRqLVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAMAFSREPPQPMVT 80
Cdd:COG2050   1 MSDPLERLEGFLAANPFAELLGIELVEVEPGR-AVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9946336   81 VGLRLDFCGVARVGDWLEVHTRVDKLGQRMAFASARLHSGE-RLVASASGVFHLP 134
Cdd:COG2050  80 IELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDgKLVATATGTFAVL 134
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-133 2.13e-26

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: 94.93  E-value: 2.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336   21 LGPFFCRQDAQRQLVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAMAFSREPPQPMVTVGLRLDFCGVARVGDwLEVH 100
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGD-LTAR 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 9946336  101 TRVDKLGQRMAFASARLHSGE-RLVASASGVFHL 133
Cdd:cd03443  80 ARVVKLGRRLAVVEVEVTDEDgKLVATARGTFAV 113
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 34-131 3.75e-16

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: 68.66  E-value: 3.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336   34 LVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAMAFSREPPQPMVTVGLRLDFCGVARVGDWLEVHTRVDKLGQRMAFA 113
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                        90
                ....*....|....*....
gi 9946336  114 SARLHSG-ERLVASASGVF 131
Cdd:cd03440  81 EVEVRNEdGKLVATATATF 99
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-125 2.56e-15

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: 65.74  E-value: 2.56e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9946336     48 GGTAHGGLLSTLADVGLGYAMAFSREPPQPMVTVGLRLDFCGVARVGDWLEVHTRVDKLGQRMAFASARLHSGERLVA 125
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 33-125 1.78e-08

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: 48.96  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336     33 QLVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAmafSREPPQPMVTVGLRLDFCGVARVGDWLEVHTRVDKLGQRMAF 112
Cdd:TIGR02286  15 FARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYA---CNSYGDAAVAAQCTIDFLRPGRAGERLEAEAVEVSRGGRTGT 91

                          90
                  ....*....|....
gi 9946336    113 ASARL-HSGERLVA 125
Cdd:TIGR02286  92 YDVEVvNQEGELVA 105
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
44-131 7.11e-08

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 48.25  E-value: 7.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336   44 HCNHGGTAHGG-LLSTLADVGLGYAMAFSReppQPMVTVGL-RLDFCGVARVGDWLEVHTRVDKLGQR-M-----AFASA 115
Cdd:COG1607  17 DTNHHGTLFGGwLLSWMDEAAAIAAARHAR---GRVVTASVdSVDFLRPVRVGDIVELYARVVRVGRTsMevgveVWAED 93

                        90
                ....*....|....*.
gi 9946336  116 RLHSGERLVASASGVF 131
Cdd:COG1607  94 LRTGERRLVTEAYFTF 109
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 43-103 1.83e-05

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: 41.40  E-value: 1.83e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9946336   43 KHCNHGGTAHGG-LLSTLADVGLGYAMAFSREPPqpmVTVGL-RLDFCGVARVGDWLEVHTRV 103
Cdd:cd03442  17 EDTNHHGTIFGGwLLEWMDELAGIAAYRHAGGRV---VTASVdRIDFLKPVRVGDVVELSARV 76
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 33-132 2.00e-04

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: 38.48  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9946336     33 QLVVALRIDEKHCNHGGTAHGGLLSTLADVGLGYAMAFSREPPQPMVTVGLRLDFCGVARVGDwLEVHTRVDKLGQRMAF 112
Cdd:TIGR00369  17 FLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGK-VRAIAQVVHLGRQTGV 95

                          90       100
                  ....*....|....*....|.
gi 9946336    113 ASARL-HSGERLVASASGVFH 132
Cdd:TIGR00369  96 AEIEIvDEQGRLCALSRGTTA 116
 
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