Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot B0UUZ0 (FABH_HAES2)

Last modified November 3, 2009. Version 9. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-oxoacyl-[acyl-carrier-protein] synthase 3
    EC=2.3.1.180
Alternative name(s):
    3-oxoacyl-[acyl-carrier-protein] synthase III
    Beta-ketoacyl-ACP synthase III
      Short name=KAS III
Gene names
Name: fabH
Ordered Locus Names: HSM_0032
OrganismHaemophilus somnus (strain 2336) (Histophilus somni (strain 2336)) [Complete proteome] [HAMAP]
Taxonomic identifier228400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Probable.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.

Sequence similarities

Belongs to the fabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3163163-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000088313

Regions

Region244 – 2485ACP-binding By similarity

Sites

Active site1121 By similarity
Active site2431 By similarity
Active site2731 By similarity

Sequences

Sequence LengthMass (Da)Tools
B0UUZ0-1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: F1FC6113822E139A

FASTA31634,232
        10         20         30         40         50         60 
MYSRILATGS YIPANIRTNA DLEKMVETSD EWITTRSGIK ERRIAGENET VATMGFEAAK 

        70         80         90        100        110        120 
NALQLANICP NDIDLVLVAT TSHSYAYPSA ACQIQGMLDI DDAISFDLAA ACTGFIYALS 

       130        140        150        160        170        180 
VADQFIKTGK VKKALVIGAD INSRKLDETD RSTVILFGDG AGAVILESSD IEGIISTHLH 

       190        200        210        220        230        240 
ASLDKSNALI LPQTQQGEVQ SGYIQMQGNA TFKLAVRELS NVVEETLRDN HLDKADLDWL 

       250        260        270        280        290        300 
VPHQANLRII TATAEKLNMS LDQVVITLDK YGNTSAATVP VALDEAVRDG RIKRGQLLLL 

       310 
EAFGGGWTWG SALVRF 

« Hide

References

[1]"Complete sequence of Haemophilus somnus 2336."
Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F., Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M., Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S., Dyer D.W., Inzana T.J.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000947 Genomic DNA. Translation: ACA31952.1.
RefSeqYP_001783387.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6108084.
GenomeReviewsGene locus HSM_0032 in contig CP000947_GR.
KEGGhsm:HSM_0032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAATSTPNR.

Family and domain databases

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

Entry information

Entry nameFABH_HAES2
AccessionPrimary (citable) accession number: B0UUZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: November 3, 2009
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents