Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A9WHA3 (A9WHA3_CHLAA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 44. 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-Rule MF_01815

EC=2.3.1.180 HAMAP-Rule MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP-Rule MF_01815
Beta-ketoacyl-ACP synthase III HAMAP-Rule MF_01815
Gene names
Name:fabH HAMAP-Rule MF_01815
Ordered Locus Names:Caur_2406 EMBL ABY35615.1
OrganismChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) [Reference proteome] [HAMAP] EMBL ABY35615.1
Taxonomic identifier324602 [NCBI]
Taxonomic lineageBacteriaChloroflexiChloroflexalesChloroflexaceaeChloroflexus

Protein attributes

Sequence length334 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-Rule MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP-Rule MF_01815 SAAS SAAS013751

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815 SAAS SAAS013751

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01815 SAAS SAAS013751

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01815 SAAS SAAS013751.

Domain

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

Sequence similarities

Belongs to the FabH family. HAMAP-Rule MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region257 – 2615ACP-binding By similarity HAMAP-Rule MF_01815

Sites

Active site1161 By similarity HAMAP-Rule MF_01815
Active site2561 By similarity HAMAP-Rule MF_01815
Active site2861 By similarity HAMAP-Rule MF_01815

Sequences

Sequence LengthMass (Da)Tools
A9WHA3 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 46930E1BAB0DE50C

FASTA33435,770
        10         20         30         40         50         60 
MSRERYAAVI GWGMAVPQRL ITNDELAQRI DTSDEWIRTR TGIRERRVAG PGESTSTLAT 

        70         80         90        100        110        120 
AAGREALTMA GVSPATIDTV IVATCTPDRP FPATACTVQA NLQIPRATAF DLAAACSGFV 

       130        140        150        160        170        180 
YGLTVATSLI KSGVSRRLLL IGADIFTHYI NWNDRNTCVL FGDGAGAVVL EATDEPLGLL 

       190        200        210        220        230        240 
ASTLSANGEL EDLMAVDAGG TRMPLTADLL EAGRQYVYMN GREIFKHAVR EMSDSALQVI 

       250        260        270        280        290        300 
QDAGLTVDDI ALVIPHQANV RIIDAVARRL EIPPERVMVN LDRYGNTSAA SIPIALYEAA 

       310        320        330 
QQERIKAGDN VLLTAFGGGL TWGSGLVRWG KPSR 

« Hide

References

[1]"Complete genome sequence of the filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus."
Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.
BMC Genomics 12:334-334(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29366 / DSM 635 / J-10-fl.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000909 Genomic DNA. Translation: ABY35615.1.
RefSeqYP_001636004.1. NC_010175.1.

3D structure databases

ProteinModelPortalA9WHA3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING324602.Caur_2406.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY35615; ABY35615; Caur_2406.
GeneID5826870.
KEGGcau:Caur_2406.
PATRIC21415937. VBIChlAur28763_2720.

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHOG000246674.
KOK00648.
OMAIRIMEAA.
OrthoDBEOG6J74XN.
ProtClustDBCLSK974275.

Enzyme and pathway databases

BioCycCAUR324602:GIXU-2445-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
HAMAPMF_01815. FabH.
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 1 hit.
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA9WHA3_CHLAA
AccessionPrimary (citable) accession number: A9WHA3
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)