Skip Header

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

Reviewed, UniProtKB/Swiss-Prot A5UFW1 (FABH_HAEIG)

Last modified June 16, 2009. Version 15. 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=2.3.1.41
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: CGSHiGG_03380
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

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

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. 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.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3163163-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056364

Regions

Region244 – 2485ACP-binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A5UFW1-1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 2D00ADD61DCB6A66

FASTA31634,280
        10         20         30         40         50         60 
MNSRILSTGS YLPSHIRTNA DLEKMVDTSD EWIVTRSGIR ERRIAAEDET VATMGFEAAK 

        70         80         90        100        110        120 
NAIEAAQINP QDIELIIVAT TSHSHAYPSA ACQVQGLLNI DDAISFDLAA ACTGFVYALS 

       130        140        150        160        170        180 
VADQFIRAGK VKKALVIGSD LNSRKLDETD RSTVVLFGDG AGAVILEASE QEGIISTHLH 

       190        200        210        220        230        240 
ASADKNNALV LAQPERGIEK SGYIEMQGNE TFKLAVRELS NVVEETLLAN NLDKKDLDWL 

       250        260        270        280        290        300 
VPHQANLRII TATAKKLEMD MSQVVVTLDK YANNSAATVP VALDEAIRDG RIQRGQLLLL 

       310 
EAFGGGWTWG SALVRF 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:RESEARCH103.1-RESEARCH103.18(2007) [PubMed: 17550610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000672 Genomic DNA. Translation: ABQ99666.1.
RefSeqYP_001292050.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5227157.
GenomeReviewsGene locus CGSHiGG_03380 in contig CP000672_GR.
KEGGhiq:CGSHiGG_03380.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA5UFW1. YSRITGT.

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. 1 hit.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH_HAEIG
AccessionPrimary (citable) accession number: A5UFW1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: June 16, 2009
This is version 15 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