NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1839964822|gb|QJR15333|]
View 

Putative esterase [Usitatibacter palustris]

Protein Classification

hotdog fold thioesterase( domain architecture ID 10794535)

hotdog fold thioesterase similar to Bacillus subtilis putative esterase ComA2 and to thioesterase PaaI that functions in the aerobic phenylacetate degradation pathway

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 7-124 3.31e-39

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: 127.46  E-value: 3.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822   7 TLLTTLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNvDSSKENVVGIEINANHLRGKKDGV 86
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLC-NSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1839964822  87 VTATATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAV 124
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
 
Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 7-124 3.31e-39

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: 127.46  E-value: 3.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822   7 TLLTTLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNvDSSKENVVGIEINANHLRGKKDGV 86
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLC-NSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1839964822  87 VTATATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAV 124
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-128 3.97e-38

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 125.44  E-value: 3.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822   4 DRQTLLTTLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNVDsSKENVVGIEINANHLR-GK 82
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP-PGRRAVTIELNINFLRpAR 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1839964822  83 KDGVVTATATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAVVPKE 128
Cdd:COG2050    92 LGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 11-124 3.19e-34

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: 114.58  E-value: 3.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822  11 TLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNVDSSKeNVVGIEINANHLRGKKDGVVTAT 90
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGA-LAVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1839964822  91 ATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAV 124
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PRK10254 PRK10254
proofreading thioesterase EntH;
3-125 6.64e-31

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 107.38  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822   3 TDRQTLLTTLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMnVDSSKENVVGIEINANHLRGK 82
Cdd:PRK10254   15 TSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFL-MTRDGQCVVGTELNATHHRPV 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1839964822  83 KDGVVTATATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAVV 125
Cdd:PRK10254   94 SEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 38-116 1.12e-14

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: 63.81  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822  38 FGLLHGGASVALAETAASLAgWMNVDSSKENVVGIEINANHLR-GKKDGVVTATATPVHIGRRTHVWQVSITDEQGKGIC 116
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAA-ARRLGGSQQVVVVVELSIDFLRpARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 7-124 3.31e-39

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: 127.46  E-value: 3.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822   7 TLLTTLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNvDSSKENVVGIEINANHLRGKKDGV 86
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLC-NSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1839964822  87 VTATATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAV 124
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-128 3.97e-38

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 125.44  E-value: 3.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822   4 DRQTLLTTLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNVDsSKENVVGIEINANHLR-GK 82
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP-PGRRAVTIELNINFLRpAR 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1839964822  83 KDGVVTATATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAVVPKE 128
Cdd:COG2050    92 LGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 11-124 3.19e-34

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: 114.58  E-value: 3.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822  11 TLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNVDSSKeNVVGIEINANHLRGKKDGVVTAT 90
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGA-LAVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1839964822  91 ATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAV 124
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PRK10254 PRK10254
proofreading thioesterase EntH;
3-125 6.64e-31

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 107.38  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822   3 TDRQTLLTTLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMnVDSSKENVVGIEINANHLRGK 82
Cdd:PRK10254   15 TSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFL-MTRDGQCVVGTELNATHHRPV 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1839964822  83 KDGVVTATATPVHIGRRTHVWQVSITDEQGKGICVSRCTLAVV 125
Cdd:PRK10254   94 SEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
12-125 5.81e-29

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 102.40  E-value: 5.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822  12 LDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMnVDSSKENVVGIEINANHLRGKKDGVVTATA 91
Cdd:PRK10293   24 LDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYL-CTEGEQKVVGLEINANHVRSAREGRVRGVC 102

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1839964822  92 TPVHIGRRTHVWQVSITDEQGKGICVSRCTLAVV 125
Cdd:PRK10293  103 KPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
PLN02322 PLN02322
acyl-CoA thioesterase
 9-122 1.96e-17

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 73.17  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822   9 LTTLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNvdSSKENVVGIEINANHLRGKKDG-VV 87
Cdd:PLN02322   13 LHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMA--SGFKRVAGIQLSINHLKSADLGdLV 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1839964822  88 TATATPVHIGRRTHVWQVSI-----TDEQGKG-ICVSRCTL 122
Cdd:PLN02322   91 FAEATPVSTGKTIQVWEVKLwkttdKDKANKIlISSSRVTL 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 38-116 1.12e-14

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: 63.81  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822  38 FGLLHGGASVALAETAASLAgWMNVDSSKENVVGIEINANHLR-GKKDGVVTATATPVHIGRRTHVWQVSITDEQGKGIC 116
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAA-ARRLGGSQQVVVVVELSIDFLRpARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 24-123 3.25e-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: 50.55  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822  24 VVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNVDSSKeNVVGIEINANHLR-GKKDGVVTATATPVHIGRRTHV 102
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGL-GAVTLSLDVRFLRpVRPGDTLTVEAEVVRVGRSSVT 79

                          90       100
                  ....*....|....*....|.
gi 1839964822 103 WQVSITDEQGKGICVSRCTLA 123
Cdd:cd03440    80 VEVEVRNEDGKLVATATATFV 100
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 11-121 3.06e-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: 40.70  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839964822  11 TLDIQIVERSKERVVLTMPVGPKVHQPFGLLHGGASVALAETAASLAGWMNVDSSKENVV-GIEInaNHLRgKKDGVVTA 89
Cdd:pfam14539  17 TIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPkGMTV--DYLA-KATGDLTA 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1839964822  90 TAT--PVHIGRRTHV-WQVSITDEqgKGICVSRCT 121
Cdd:pfam14539  94 VAEldPEDWGEKGDLpVPVEVRDD--AGTEVVRAT 126
 
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