Skip Header

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

B1LM31 (B1LM31_ECOSM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 30. Feed History...

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

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:EcSMS35_4226
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP] EMBL ACB18300.1
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length387 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 site911Acyl-thioester intermediate By similarity HAMAP MF_01620
Active site3431Proton acceptor By similarity HAMAP MF_01620
Active site3731Proton acceptor By similarity HAMAP MF_01620

Sequences

Sequence LengthMass (Da)Tools
B1LM31 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: CF39506D818B761B

FASTA38740,851
        10         20         30         40         50         60 
MEQVVIVDAI RTPMGRSKGG AFRHVRAEDL SAHLMRSLLA RNPALEAAAL DDIYWGCVQQ 

        70         80         90        100        110        120 
TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QACLVGGVEH 

       130        140        150        160        170        180 
MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDAFAA RSHARAWAAT 

       190        200        210        220        230        240 
QSGAFKNEII PTGGHDADGV LKQFNYDEVI RPETTVEALA TLRPAFDPVS GTVTAGTSSA 

       250        260        270        280        290        300 
LSDGAAAMLV MSESRARELG LKPRARVRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS 

       310        320        330        340        350        360 
DIGVFEMNEA FAAQILPCIK DLGLMEQIDE KINLNGGAIA LGHPLGCSGA RISTTLLNLM 

       370        380 
ERKDAQFGLA TMCIGLGQGI ATVFERI

« Hide

References

[1]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed: 18708504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000970 Genomic DNA. Translation: ACB18300.1.
RefSeqYP_001746177.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LM31.
SMRB1LM31. Positions 4-387.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1LM31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000061435; EBESCP00000059077; EBESCG00000060482.
GeneID6147277.
GenomeReviewsGene locus EcSMS35_4226 in contig CP000970_GR.
KEGGecm:EcSMS35_4226.
PATRIC18437378. VBIEscCol6161_4360.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009707.
HOGENOMHBG370930.
OMAAIDDIYW.
ProtClustDBPRK08947.

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.
IPR020610. Thiolase_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.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB1LM31_ECOSM
AccessionPrimary (citable) accession number: B1LM31
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: December 14, 2011
This is version 30 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