Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A5WH98 (FADA_PSYWF)

Last modified November 3, 2009. Version 21. 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: PsycPRwf_2099
OrganismPsychrobacter sp. (strain PRwf-1) [Complete proteome] [HAMAP]
Taxonomic identifier349106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length390 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 – 3903903-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_1000073633

Sites

Active site951Acyl-thioester intermediate By similarity
Active site3461Proton acceptor By similarity
Active site3761Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
A5WH98-1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: A57A837BAA5300AF

FASTA39041,510
        10         20         30         40         50         60 
MTTLSPKDVV IVDGVRTAMG KSKNGMFRNV RADSMSAELV RALVKRNDFD TNEVEDIIWG 

        70         80         90        100        110        120 
CVNQTLEQGM NIGRNIGLLA DIPKTAGGQT VNRLCGSSMQ ALHTAAAQIM TNQGDVFIIG 

       130        140        150        160        170        180 
GVEHMGHVGM MHGIDINPEA SKHYAKASNM MGLTAEMLGR MNGITREQQD EFGYESHRRA 

       190        200        210        220        230        240 
WAATQAGRFD NEIIGIEGHD AEGRLQLCTV DEVIRPDTSM ESLAKLRPVF DPANGTVTAA 

       250        260        270        280        290        300 
TSSALSDGAS AMLVMSAQKA KDLGLKPRAR IRSMAIAGCD AAIMGYGPVP ATQKALKRAG 

       310        320        330        340        350        360 
LTVEDMQTIE LNEAFAAQGL SVLKALNLLD KRDIINVNGG AIALGHPLGC SGARITVTLL 

       370        380        390 
NAMEQMDTEI GLATMCIGLG QGISTVIERV 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter sp. PRwf-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000713 Genomic DNA. Translation: ABQ95039.1.
RefSeqYP_001280989.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5WH98.

Genome annotation databases

GeneID5206031.
GenomeReviewsGene locus PsycPRwf_2099 in contig CP000713_GR.
KEGGprw:PsycPRwf_2099.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAAIDDIYW.

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_PSYWF
AccessionPrimary (citable) accession number: A5WH98
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 10, 2007
Last modified: November 3, 2009
This is version 21 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