Skip Header

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

P43711 (FABH_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:HI_0157
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_01815.

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

Miscellaneous

Inhibited by the SB418011 antibiotic. Not inhibited by cerulenin, and weakly inhibited by thiolactomycin. HAMAP-Rule MF_01815

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-Rule MF_01815
PRO_0000110432

Regions

Region244 – 2485ACP-binding By similarity

Sites

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

Secondary structure

1 ........................................................ 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43711 [UniParc].

Last modified November 1, 1995. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC21826.1.
PIRF64051.
RefSeqNP_438327.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IL3X-ray2.70A1-316[»]
ProteinModelPortalP43711.
SMRP43711. Positions 1-316.
ModBaseSearch...

Protein-protein interaction databases

STRING71421.HI0157.

Proteomic databases

PRIDEP43711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC21826; AAC21826; HI_0157.
GeneID951067.
KEGGhin:HI0157.
PATRIC20188811. VBIHaeInf48452_0162.

Phylogenomic databases

eggNOGCOG0332.
KOK00648.
OMAAHIVEET.
ProtClustDBPRK09352.

Enzyme and pathway databases

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. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Other

BindingDBP43711.
ChEMBLCHEMBL3822.
EvolutionaryTraceP43711.

Entry information

Entry nameFABH_HAEIN
AccessionPrimary (citable) accession number: P43711
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents