Skip Header

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

B5EJC9 (B5EJC9_ACIF5) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 28. 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

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815

EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP MF_01815
Beta-ketoacyl-ACP synthase III HAMAP MF_01815
Gene names
Name:fabH HAMAP MF_01815
Ordered Locus Names:Lferr_1581
OrganismAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP]
Taxonomic identifier380394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids By similarity. HAMAP MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815 SAAS SAAS013747

Subunit structure

Homodimer By similarity. HAMAP MF_01815 SAAS SAAS013747

Subcellular location

Cytoplasm By similarity HAMAP MF_01815 SAAS SAAS013747.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP MF_01815

Sequence similarities

Belongs to the FabH family. HAMAP MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region241 – 2455ACP-binding By similarity HAMAP MF_01815

Sites

Active site1151 By similarity HAMAP MF_01815
Active site2401 By similarity HAMAP MF_01815
Active site2701 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
B5EJC9 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 083E90AEC4897F38

FASTA31433,400
        10         20         30         40         50         60 
MKPIYSRIVA TGGYLPERIL SNRDLEQMVE TSDAWIFART GIRSRHIAAP GEKTVDMAEA 

        70         80         90        100        110        120 
AARQALADAG LNAADLDLII VATTTPDQIF PSTACLLQAR LGNRGAPAFD IQAVCTGFIY 

       130        140        150        160        170        180 
ALATADRFIR SGGARHALVV GVESMSHIVD WTDRGTCILF GDGAGAVVLS AGDQPGIIST 

       190        200        210        220        230        240 
HIHADGAYAD LLQVPGGETR IAMQGNAVFR VAVRTLGEIV QETLAANALT PAEIDWLVPH 

       250        260        270        280        290        300 
QANIRIIEAT ADKLGLPMER VVTTVEHHGN TSAASVPLAL DEAARRGCFQ PRQRLLLEAF 

       310 
GGGFTWGSAL LRWG 

« Hide

References

[1]"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53993.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001132 Genomic DNA. Translation: ACH83803.1.
RefSeqYP_002220010.1. NC_011206.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB5EJC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6877557.
GenomeReviewsGene locus Lferr_1581 in contig CP001132_GR.
KEGGafe:Lferr_1581.
PATRIC20660774. VBIAciFer6930_1589.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMAVIGSEVY.
ProtClustDBCLSK2408028.

Family and domain databases

HAMAPMF_01815. FabH.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KOK00648.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. FabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB5EJC9_ACIF5
AccessionPrimary (citable) accession number: B5EJC9
Entry history
Integrated into UniProtKB/TrEMBL: October 14, 2008
Last sequence update: October 14, 2008
Last modified: December 14, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)