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Q48GW4 (FADA_PSE14) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-ketoacyl-CoA thiolase

EC=2.3.1.16
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta
Gene names
Name:fadA
Ordered Locus Names:PSPPH_3209
OrganismPseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]
Taxonomic identifier264730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed By similarity. HAMAP-Rule MF_01620

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP-Rule MF_01620

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP-Rule MF_01620

Subunit structure

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA) By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01620.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3913913-ketoacyl-CoA thiolase HAMAP-Rule MF_01620
PRO_0000206384

Sites

Active site951Acyl-thioester intermediate By similarity
Active site3471Proton acceptor By similarity
Active site3771Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48GW4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 4A7D53C9E0DE40F9

FASTA39141,656
        10         20         30         40         50         60 
MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNNKVD PAEVEDVIWG 

        70         80         90        100        110        120 
CVNQTLEQGW NIARMASLLT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TNNGDVFVIG 

       130        140        150        160        170        180 
GVEHMGHVSM MHGVDPNPHM SLHAAKASGM MGLTAEMLGK MHGITREQQD AFGLRSHQLA 

       190        200        210        220        230        240 
HKATLEGKFK DEIIPMQGYD ENGFLKVFDY DETIRPDTTL ESLAALKPAF NPKGGTVTAG 

       250        260        270        280        290        300 
TSSQITDGAS CMIVMSAQRA QDLGIQPLAV IRSMAVAGVD PAIMGYGPVP ATQKALKRAG 

       310        320        330        340        350        360 
LTIADIDFIE LNEAFAAQAL PVLKDLKVLD KMNEKVNLHG GAIALGHPFG CSGARISGTL 

       370        380        390 
LNVMKQNGGT FGVSTMCIGL GQGIATVFER V 

« Hide

References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1448A / Race 6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000058 Genomic DNA. Translation: AAZ36601.1.
RefSeqYP_275369.1. NC_005773.3.

3D structure databases

ProteinModelPortalQ48GW4.
SMRQ48GW4. Positions 2-391.
ModBaseSearch...

Protein-protein interaction databases

STRING264730.PSPPH_3209.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ36601; AAZ36601; PSPPH_3209.
GeneID3559224.
KEGGpsp:PSPPH_3209.
PATRIC19975808. VBIPseSyr78478_3376.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHOG000012239.
KOK00632.
OMAAIMTNNG.
ProtClustDBPRK08947.

Enzyme and pathway databases

BioCycPSAV264730:GKDE-3212-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
HAMAPMF_01620. FadA.
InterProIPR012805. FadA.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02445. fadA. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADA_PSE14
AccessionPrimary (citable) accession number: Q48GW4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: September 13, 2005
Last modified: May 29, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families