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Protein

3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase

Gene

paaJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the thiolytic cleavage of the beta-keto C8 intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6 intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes also the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA.3 Publications

Catalytic activityi

Succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA.2 Publications
2,3-didehydroadipyl-CoA + acetyl-CoA = CoA + 3-oxo-5,6-didehydrosuberyl-CoA.2 Publications

Pathwayi: phenylacetate degradation

This protein is involved in the pathway phenylacetate degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway phenylacetate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901Acyl-thioester intermediateBy similarity
Active sitei357 – 3571Proton acceptorPROSITE-ProRule annotation
Active sitei387 – 3871Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  • 3-oxoadipyl-CoA thiolase activity Source: UniProtKB
  • transferase activity Source: EcoCyc

GO - Biological processi

  • 3,4-dihydroxybenzoate catabolic process Source: InterPro
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • phenylacetate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:G6718-MONOMER.
MetaCyc:G6718-MONOMER.
UniPathwayiUPA00930.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase (EC:2.3.1.1742 Publications, EC:2.3.1.2232 Publications)
Gene namesi
Name:paaJ
Synonyms:paaE, ydbW
Ordered Locus Names:b1397, JW1392
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13744. paaJ.

Pathology & Biotechi

Disruption phenotypei

Mutants are unable to use phenylacetate as a carbon source.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4014013-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolasePRO_0000206421Add
BLAST

Proteomic databases

PaxDbiP0C7L2.
PRIDEiP0C7L2.

Expressioni

Inductioni

Activated by cAMP receptor protein (CRP), integration host factor (IHF) and by phenylacetyl-coenzyme A (PA-CoA) that prevents PaaX from binding its target sequences. Inhibited by PaaX.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4263012. 238 interactions.
IntActiP0C7L2. 5 interactions.
STRINGi511145.b1397.

Structurei

3D structure databases

ProteinModelPortaliP0C7L2.
SMRiP0C7L2. Positions 3-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012239.
InParanoidiP0C7L2.
KOiK02615.
OMAiAVPPRIM.
PhylomeDBiP0C7L2.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR012793. PcaF.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02430. pcaF. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C7L2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREAFICDGI RTPIGRYGGA LSSVRADDLA AIPLRELLVR NPRLDAECID
60 70 80 90 100
DVILGCANQA GEDNRNVARM ATLLAGLPQS VSGTTINRLC GSGLDALGFA
110 120 130 140 150
ARAIKAGDGD LLIAGGVESM SRAPFVMGKA ASAFSRQAEM FDTTIGWRFV
160 170 180 190 200
NPLMAQQFGT DSMPETAENV AELLKISRED QDSFALRSQQ RTAKAQSSGI
210 220 230 240 250
LAEEIVPVVL KNKKGVVTEI QHDEHLRPET TLEQLRGLKA PFRANGVITA
260 270 280 290 300
GNASGVNDGA AALIIASEQM AAAQGLTPRA RIVAMATAGV EPRLMGLGPV
310 320 330 340 350
PATRRVLERA GLSIHDMDVI ELNEAFAAQA LGVLRELGLP DDAPHVNPNG
360 370 380 390 400
GAIALGHPLG MSGARLALAA SHELHRRNGR YALCTMCIGV GQGIAMILER

V
Length:401
Mass (Da):42,277
Last modified:June 10, 2008 - v1
Checksum:i6B8C26ECB4CFEC00
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74479.1.
AP009048 Genomic DNA. Translation: BAA15002.1.
PIRiH64890.
RefSeqiNP_415915.1. NC_000913.3.
WP_001206197.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74479; AAC74479; b1397.
BAA15002; BAA15002; BAA15002.
GeneIDi946121.
KEGGiecj:JW1392.
eco:b1397.
PATRICi32118080. VBIEscCol129921_1460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74479.1.
AP009048 Genomic DNA. Translation: BAA15002.1.
PIRiH64890.
RefSeqiNP_415915.1. NC_000913.3.
WP_001206197.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0C7L2.
SMRiP0C7L2. Positions 3-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263012. 238 interactions.
IntActiP0C7L2. 5 interactions.
STRINGi511145.b1397.

Proteomic databases

PaxDbiP0C7L2.
PRIDEiP0C7L2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74479; AAC74479; b1397.
BAA15002; BAA15002; BAA15002.
GeneIDi946121.
KEGGiecj:JW1392.
eco:b1397.
PATRICi32118080. VBIEscCol129921_1460.

Organism-specific databases

EchoBASEiEB3507.
EcoGeneiEG13744. paaJ.

Phylogenomic databases

eggNOGiENOG4105CHU. Bacteria.
COG0183. LUCA.
HOGENOMiHOG000012239.
InParanoidiP0C7L2.
KOiK02615.
OMAiAVPPRIM.
PhylomeDBiP0C7L2.

Enzyme and pathway databases

UniPathwayiUPA00930.
BioCyciEcoCyc:G6718-MONOMER.
MetaCyc:G6718-MONOMER.

Miscellaneous databases

PROiP0C7L2.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR012793. PcaF.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02430. pcaF. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPAAJ_ECOLI
AccessioniPrimary (citable) accession number: P0C7L2
Secondary accession number(s): O53017, P77525
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: September 7, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.