Skip Header

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

Q5L608 (Q5L608_CHLAB) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 49. 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 EMBL CAH63923.1
Ordered Locus Names:CAB470
OrganismChlamydophila abortus [Complete proteome] [HAMAP]
Taxonomic identifier83555 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length337 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

Region262 – 2665ACP-binding By similarity HAMAP MF_01815

Sites

Active site1201 By similarity HAMAP MF_01815
Active site2611 By similarity HAMAP MF_01815
Active site2911 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q5L608 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: F58CBF284A0CB88C

FASTA33736,299
        10         20         30         40         50         60 
MWLCVKKTRK ASIWATGSYL PEKILSNSDL EQMVDTSDEW ILTRTGIKER RIAAANEYTS 

        70         80         90        100        110        120 
IMGAKAAERA IQKAGLTKDQ IECIIFSTSA PDYIFPSSAA LAQAYLGIKD IPAFDCMAAC 

       130        140        150        160        170        180 
TGYLYGLSVA KAYVESGMYN NVLLIAADKL SSFVNYKDRN TCVLFGDGGA ACIIGESRPG 

       190        200        210        220        230        240 
ALEITNVNLG ADGSVADLLS LPAGGSRVPA SQETLEAGKH YIFMEGKEVF KHAVRRMESA 

       250        260        270        280        290        300 
AKTCIAGAGI EESDIDWLVP HQANERIIDA IAKRFEIDEG KVFKTLCKYG NTAASSVCIA 

       310        320        330 
LDELLQSHII HAGEYLLLVA FGGGLSWGAV VLQQVES 

« Hide

References

[1]"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation."
Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.
Genome Res. 15:629-640(2005) [PubMed: 15837807] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S26/3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR848038 Genomic DNA. Translation: CAH63923.1.
RefSeqYP_219884.1. NC_004552.2.

3D structure databases

ProteinModelPortalQ5L608.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3338041.
GenomeReviewsGene locus CAB470 in contig CR848038_GR.
KEGGcab:CAB470.
PATRIC20202419. VBIChlAbo21869_0525.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMAMAKISPE.
PhylomeDBQ5L608.
ProtClustDBPRK09352.

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 nameQ5L608_CHLAB
AccessionPrimary (citable) accession number: Q5L608
Entry history
Integrated into UniProtKB/TrEMBL: June 21, 2005
Last sequence update: June 21, 2005
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)