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B0KH75 (B0KH75_PSEPG) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-ketoacyl-CoA thiolase HAMAP MF_01620
EC=2.3.1.16 HAMAP MF_01620
Alternative name(s):
Acetyl-CoA acyltransferase HAMAP MF_01620
Beta-ketothiolase HAMAP MF_01620
Fatty acid oxidation complex subunit beta HAMAP MF_01620
Gene names
Name:fadA HAMAP MF_01620
Ordered Locus Names:PputGB1_1677
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP] EMBL ABY97580.1
Taxonomic identifier76869 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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 MF_01620

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620 SAAS SAAS020613

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620 SAAS SAAS020613

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. HAMAP MF_01620 SAAS SAAS020613

Subcellular location

Cytoplasm By similarity HAMAP MF_01620.

Sequence similarities

Belongs to the thiolase family. HAMAP MF_01620

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site951Acyl-thioester intermediate By similarity HAMAP MF_01620
Active site3471Proton acceptor By similarity HAMAP MF_01620
Active site3771Proton acceptor By similarity HAMAP MF_01620

Sequences

Sequence LengthMass (Da)Tools
B0KH75 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: AE4B42AF1BC0CCE3

FASTA39141,573
        10         20         30         40         50         60 
MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNGKVD PKEVEDVIWG 

        70         80         90        100        110        120 
CVNQTLEQGW NIARMASLMT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TGNGDVFVVG 

       130        140        150        160        170        180 
GVEHMGHVSM MHGVDPNPHL SLHAAKASGM MGLTAEMLGK MHGITREQQD LFGVRSHQLA 

       190        200        210        220        230        240 
HKATVEGKFK DEIIPMQGYD ENGFLKVFDF DETIRPETTL EGLASLKPAF NPKGGTVTAG 

       250        260        270        280        290        300 
TSSQITDGAS CMIVMSGQRA MDLGIQPLAV IRSMAVAGVD PAIMGYGPVP STQKALKRAG 

       310        320        330        340        350        360 
LTMADIDFIE LNEAFAAQAL PVLKDLKVLD KMDEKVNLHG GAIALGHPFG CSGARISGTL 

       370        380        390 
LNVMKQNGGT LGVATMCVGL GQGITTVFER V

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000926 Genomic DNA. Translation: ABY97580.1.
RefSeqYP_001667916.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KH75.
SMRB0KH75. Positions 2-391.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0KH75.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5869457.
GenomeReviewsGene locus PputGB1_1677 in contig CP000926_GR.
KEGGppg:PputGB1_1677.
PATRIC19930367. VBIPsePut76638_1681.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG370930.
OMASSMEAIH.
ProtClustDBPRK08947.

Enzyme and pathway databases

BioCycPPUT76869:PPUTGB1_1677-MONOMER.

Family and domain databases

HAMAPMF_01620. FadA.
[Tree]
InterProIPR012805. FadA.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KOK00632.
PANTHERPTHR18919:SF35. PTHR18919:SF35. 1 hit.
PTHR18919. Thiolase. 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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB0KH75_PSEPG
AccessionPrimary (citable) accession number: B0KH75
Entry history
Integrated into UniProtKB/TrEMBL: March 18, 2008
Last sequence update: March 18, 2008
Last modified: December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info