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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 3

Gene

fabH

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2.UniRule annotation

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei111 – 1111UniRule annotation
Active sitei249 – 2491UniRule annotation
Active sitei279 – 2791UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3UniRule annotation (EC:2.3.1.180UniRule annotation)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase IIIUniRule annotation
Beta-ketoacyl-ACP synthase IIIUniRule annotation
Short name:
KAS IIIUniRule annotation
Gene namesi
Name:fabHUniRule annotation
Ordered Locus Names:PA3333
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3333.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3303303-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110455Add
BLAST

Proteomic databases

PaxDbiQ9HYR2.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi208964.PA3333.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1310Combined sources
Beta strandi18 – 203Combined sources
Helixi21 – 277Combined sources
Helixi32 – 398Combined sources
Beta strandi43 – 453Combined sources
Helixi52 – 6716Combined sources
Beta strandi73 – 786Combined sources
Beta strandi83 – 875Combined sources
Helixi90 – 967Combined sources
Beta strandi102 – 1087Combined sources
Helixi110 – 1123Combined sources
Helixi113 – 12614Combined sources
Beta strandi131 – 1399Combined sources
Helixi141 – 1444Combined sources
Helixi150 – 1556Combined sources
Beta strandi159 – 16810Combined sources
Beta strandi175 – 1839Combined sources
Helixi185 – 1873Combined sources
Beta strandi190 – 1945Combined sources
Helixi198 – 2036Combined sources
Helixi214 – 23623Combined sources
Helixi240 – 2423Combined sources
Beta strandi244 – 2485Combined sources
Helixi253 – 26311Combined sources
Helixi267 – 2693Combined sources
Helixi274 – 2774Combined sources
Helixi281 – 2833Combined sources
Helixi284 – 29411Combined sources
Beta strandi303 – 3108Combined sources
Turni311 – 3133Combined sources
Beta strandi314 – 3218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X3EX-ray1.81A/B1-330[»]
ProteinModelPortaliQ9HYR2.
SMRiQ9HYR2. Positions 3-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HYR2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni250 – 2545ACP-bindingUniRule annotation

Domaini

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.UniRule annotation

Sequence similaritiesi

Belongs to the FabH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
InParanoidiQ9HYR2.
KOiK00648.
OMAiEKHANCS.
OrthoDBiEOG6J74XN.
PhylomeDBiQ9HYR2.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH.
InterProiIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
TIGRFAMsiTIGR00747. fabH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HYR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRAAVVCGL GSYLPEAVLS NDMLAAELDT SDAWISSRTG VRQRHIAGDL
60 70 80 90 100
GSGDLALRAA SAALASAGLE RVDAVVLATS TGDFCCPATA PRVAARLGLV
110 120 130 140 150
GALAFDLSAA CTGFVYGLAS VGSLISAGLA DSALLVGVDT FSHTLDPADR
160 170 180 190 200
STRALFGDGA GAVVLRAGDA EEEGALLAFD LGSDGHQFDL LMTPAVSRAE
210 220 230 240 250
RSSGQASNYF RMDGKAVFGQ AVTQMSDSVR RVLDRVGWQA SDLHHLVPHQ
260 270 280 290 300
ANTRILAAVA DQLDLPVERV VSNIAEVGNT VAASIPLALA HGLRQGILRD
310 320 330
GGNMVLTGFG AGLTWGSVAL RWPKIVPTMD
Length:330
Mass (Da):34,004
Last modified:March 1, 2001 - v1
Checksum:i6F032604DF695F1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06721.1.
PIRiA83230.
RefSeqiNP_252023.1. NC_002516.2.
WP_003091712.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG06721; AAG06721; PA3333.
GeneIDi882498.
KEGGipae:PA3333.
PATRICi19841265. VBIPseAer58763_3491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06721.1.
PIRiA83230.
RefSeqiNP_252023.1. NC_002516.2.
WP_003091712.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X3EX-ray1.81A/B1-330[»]
ProteinModelPortaliQ9HYR2.
SMRiQ9HYR2. Positions 3-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3333.

Proteomic databases

PaxDbiQ9HYR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06721; AAG06721; PA3333.
GeneIDi882498.
KEGGipae:PA3333.
PATRICi19841265. VBIPseAer58763_3491.

Organism-specific databases

PseudoCAPiPA3333.

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
InParanoidiQ9HYR2.
KOiK00648.
OMAiEKHANCS.
OrthoDBiEOG6J74XN.
PhylomeDBiQ9HYR2.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

EvolutionaryTraceiQ9HYR2.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH.
InterProiIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
TIGRFAMsiTIGR00747. fabH. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiFABH_PSEAE
AccessioniPrimary (citable) accession number: Q9HYR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2001
Last modified: November 11, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.