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Reviewed, UniProtKB/Swiss-Prot Q2SD23 (FADA_HAHCH)

Last modified November 3, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-ketoacyl-CoA thiolase
    EC=2.3.1.16
Alternative name(s):
    Fatty acid oxidation complex subunit beta
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
Gene names
Name: fadA
Ordered Locus Names: HCH_04754
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHahellaceaeHahella

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity.

Subcellular location

Cytoplasm By similarity.

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 metabolic process

Inferred from electronic annotation. Source: HAMAP

lipid catabolic process

Inferred from electronic annotation. Source: HAMAP

   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 MF_01620
PRO_0000292891

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q2SD23-1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: F8266805C537EF30

FASTA39141,536
        10         20         30         40         50         60 
MSLNPRDVVV IDCVRSPMGR AKAGCFRNVR AETLSATLID ALFDRNDKVD PAEVEDLIWG 

        70         80         90        100        110        120 
CVNQTLEQGF NVARQISLLT RIPHTSSAQT VNRLCGSAMS AIHTAAQAIM TGNGDVFVVG 

       130        140        150        160        170        180 
GVEHMGHVPM TQGFDHNPAA SKYSAKASNM MGLTAEMLAK MHGISRQQQD EFGARSHRLA 

       190        200        210        220        230        240 
HEATLEGRFR NEIISIQGHD DDGFPALIEN DETIRPETTA ESLAQLRPAF DPKSGTVTAG 

       250        260        270        280        290        300 
QSSQLTDGAS AMLLMSAERA QALGLTPMAK IRSMATAGCD PAIMGYGPVP ATKKALKRAG 

       310        320        330        340        350        360 
LKVEDIDFWE LNEAFAAQSL PVIKDLKLMG VVDQKVNLNG GAIALGHPLG CSGARISTTL 

       370        380        390 
LNVMAAKGGT LGVSTMCIGL GQGIATVWER I 

« Hide

References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000155 Genomic DNA. Translation: ABC31451.1.
RefSeqYP_435876.1.

3D structure databases

SMRQ2SD23. Positions 2-391.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2SD23.

Genome annotation databases

GeneID3843594.
GenomeReviewsGene locus HCH_04754 in contig CP000155_GR.
KEGGhch:HCH_04754.
NMPDRfig|349521.5.peg.4161.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2SD23.
OMAAIDDIYW.

Enzyme and pathway databases

BioCycHCHE349521:HCH_04754-MON.

Family and domain databases

HAMAPMF_01620.
[Tree]
InterProIPR012805. FadA.
IPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
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_HAHCH
AccessionPrimary (citable) accession number: Q2SD23
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: January 24, 2006
Last modified: November 3, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents