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Conserved domains on  [gi|2117096889|gb|UCX06013|]
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PaaI family thioesterase [Shewanella glacialimarina]

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 ...
 1-145 3.17e-37

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 123.90  E-value: 3.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889   1 MSIWFREVtladcerldAGMNGKGTLMQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVV 80
Cdd:COG2050     1 MSDPLERL---------EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117096889  81 DfTKFYCVGQEINANHLKASRNG-TLTATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAVVER 145
Cdd:COG2050    72 P-PGRRAVTIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-145 3.17e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 123.90  E-value: 3.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889   1 MSIWFREVtladcerldAGMNGKGTLMQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVV 80
Cdd:COG2050     1 MSDPLERL---------EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117096889  81 DfTKFYCVGQEINANHLKASRNG-TLTATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAVVER 145
Cdd:COG2050    72 P-PGRRAVTIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 25-142 2.07e-36

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: 121.30  E-value: 2.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  25 TLMQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVVDFTKFyCVGQEINANHLKASRNGT 104
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQA-VVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2117096889 105 LTATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAV 142
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PRK10254 PRK10254
proofreading thioesterase EntH;
3-143 3.38e-33

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 113.54  E-value: 3.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889   3 IWFREVTLadcERLDAgmNGKGTLMQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAAnFVVDF 82
Cdd:PRK10254    2 IWKRHLTL---DELNA--TSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG-FLMTR 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2117096889  83 TKFYCVGQEINANHLKASRNGTLTATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAVV 143
Cdd:PRK10254   76 DGQCVVGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 29-142 1.11e-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: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  29 TLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVVDFTKFyCVGQEINANHLKASRNGTLTAT 108
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGAL-AVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2117096889 109 AKPVHIGKRSSVWEILIHNSANDLCCISRMTAAV 142
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 56-134 3.24e-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: 60.73  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  56 LGIVHGGANIALAETVASYAANFVVDFTKfYCVGQEINANHLKASRNG-TLTATAKPVHIGKRSSVWEILIHNSANDLCC 134
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQ-VVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-145 3.17e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 123.90  E-value: 3.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889   1 MSIWFREVtladcerldAGMNGKGTLMQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVV 80
Cdd:COG2050     1 MSDPLERL---------EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117096889  81 DfTKFYCVGQEINANHLKASRNG-TLTATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAVVER 145
Cdd:COG2050    72 P-PGRRAVTIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 25-142 2.07e-36

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: 121.30  E-value: 2.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  25 TLMQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVVDFTKFyCVGQEINANHLKASRNGT 104
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQA-VVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2117096889 105 LTATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAV 142
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PRK10254 PRK10254
proofreading thioesterase EntH;
3-143 3.38e-33

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 113.54  E-value: 3.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889   3 IWFREVTLadcERLDAgmNGKGTLMQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAAnFVVDF 82
Cdd:PRK10254    2 IWKRHLTL---DELNA--TSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG-FLMTR 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2117096889  83 TKFYCVGQEINANHLKASRNGTLTATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAVV 143
Cdd:PRK10254   76 DGQCVVGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 29-142 1.11e-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: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  29 TLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVVDFTKFyCVGQEINANHLKASRNGTLTAT 108
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGAL-AVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2117096889 109 AKPVHIGKRSSVWEILIHNSANDLCCISRMTAAV 142
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
3-143 2.94e-32

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 111.26  E-value: 2.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889   3 IWFREVTLadcERLDAgmNGKGTLMQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVVDF 82
Cdd:PRK10293    2 IWKRKITL---EALNA--MGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2117096889  83 TKfYCVGQEINANHLKASRNGTLTATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAVV 143
Cdd:PRK10293   77 EQ-KVVGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 56-134 3.24e-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: 60.73  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  56 LGIVHGGANIALAETVASYAANFVVDFTKfYCVGQEINANHLKASRNG-TLTATAKPVHIGKRSSVWEILIHNSANDLCC 134
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQ-VVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PLN02322 PLN02322
acyl-CoA thioesterase
 27-125 2.23e-11

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 58.15  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  27 MQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVVDFTKfyCVGQEINANHLKASRNGTLT 106
Cdd:PLN02322   13 LHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKR--VAGIQLSINHLKSADLGDLV 90

                          90       100
                  ....*....|....*....|
gi 2117096889 107 -ATAKPVHIGKRSSVWEILI 125
Cdd:PLN02322   91 fAEATPVSTGKTIQVWEVKL 110
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 27-143 1.40e-10

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: 54.73  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  27 MQTLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAANFVVDFTkfycVGQEINANHLKASRNG-TL 105
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAA----VAAQCTIDFLRPGRAGeRL 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2117096889 106 TATAKPVHIGKRSSVWEILIHNSANDLCCISRMTAAVV 143
Cdd:TIGR02286  77 EAEAVEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL 114
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 44-141 1.11e-09

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: 52.09  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117096889  44 ATMPADPSVHNPLGIVHGGANIALAETVASYAANFVVDFTKFyCVGQEINANHLKASR-NGTLTATAKPVHIGKRSSVWE 122
Cdd:cd03440     3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLG-AVTLSLDVRFLRPVRpGDTLTVEAEVVRVGRSSVTVE 81

                          90
                  ....*....|....*....
gi 2117096889 123 ILIHNSANDLCCISRMTAA 141
Cdd:cd03440    82 VEVRNEDGKLVATATATFV 100
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 29-76 6.99e-05

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 39.93  E-value: 6.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2117096889  29 TLGIKITEIGDDYLKATMPADPSVHNPLGIVHGGANIALAETVASYAA 76
Cdd:pfam14539  17 TIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMA 64
 
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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