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Protein

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

Gene

fabH

Organism
Aquifex aeolicus (strain VF5)
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)DescriptionActionsGraphical viewLength
Active sitei111UniRule annotation1
Active sitei236UniRule annotation1
Active sitei266UniRule annotation1

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:aq_1099
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001103921 – 3093-oxoacyl-[acyl-carrier-protein] synthase 3Add BLAST309

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224324.aq_1099.

Structurei

Secondary structure

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Beta strandi14 – 18Combined sources5
Helixi19 – 23Combined sources5
Helixi30 – 37Combined sources8
Beta strandi41 – 44Combined sources4
Helixi50 – 65Combined sources16
Helixi69 – 71Combined sources3
Beta strandi73 – 78Combined sources6
Beta strandi83 – 87Combined sources5
Helixi89 – 97Combined sources9
Beta strandi103 – 108Combined sources6
Helixi110 – 112Combined sources3
Helixi113 – 126Combined sources14
Beta strandi131 – 140Combined sources10
Helixi141 – 143Combined sources3
Turni150 – 155Combined sources6
Beta strandi158 – 167Combined sources10
Beta strandi169 – 171Combined sources3
Beta strandi173 – 181Combined sources9
Helixi183 – 188Combined sources6
Beta strandi189 – 191Combined sources3
Beta strandi197 – 199Combined sources3
Helixi201 – 223Combined sources23
Helixi227 – 229Combined sources3
Beta strandi231 – 235Combined sources5
Helixi240 – 249Combined sources10
Helixi254 – 256Combined sources3
Helixi261 – 264Combined sources4
Helixi268 – 270Combined sources3
Helixi271 – 281Combined sources11
Beta strandi290 – 297Combined sources8
Turni298 – 300Combined sources3
Beta strandi301 – 308Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBDX-ray2.10A/B1-309[»]
ProteinModelPortaliO67185.
SMRiO67185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67185.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni237 – 241ACP-bindingUniRule annotation5

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.
InParanoidiO67185.
KOiK00648.
OMAiESGMYEN.
OrthoDBiPOG091H02M9.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH. 1 hit.
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.

O67185-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTKIIGTGV YLPKNVLTNF DLEKIVDTSD EWITTRTGIK ERRIAKEETI
60 70 80 90 100
TYMATQAAKE ALREANLSPE ELDLIILATL TPQKRFPSTA CLVQAQLKAK
110 120 130 140 150
GVYAFDISAA CSGFIYALDI ADSFIKSGKA KNVLVIGAEK LSEAVDWEDR
160 170 180 190 200
STCVLFGDGA GAVVVTRSED KSDILATRMY AEGSLEELLH ADNCGYIRMK
210 220 230 240 250
GRELFKVAVR SMEEVCREVL EKAGVKPEEV SLVIPHQANV RIINALAEKL
260 270 280 290 300
NIPKEKVFVN IQKYGNTSAA SIPIALHEAI KEGKVKRGDL ILMTAMGGGL

TWGAVLLRY
Length:309
Mass (Da):33,825
Last modified:August 1, 1998 - v1
Checksum:iEB97518DB168140D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07144.1.
PIRiF70394.
RefSeqiNP_213748.1. NC_000918.1.
WP_010880686.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07144; AAC07144; aq_1099.
GeneIDi1193819.
KEGGiaae:aq_1099.
PATRICi20959474. VBIAquAeo85532_0857.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07144.1.
PIRiF70394.
RefSeqiNP_213748.1. NC_000918.1.
WP_010880686.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBDX-ray2.10A/B1-309[»]
ProteinModelPortaliO67185.
SMRiO67185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_1099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07144; AAC07144; aq_1099.
GeneIDi1193819.
KEGGiaae:aq_1099.
PATRICi20959474. VBIAquAeo85532_0857.

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
InParanoidiO67185.
KOiK00648.
OMAiESGMYEN.
OrthoDBiPOG091H02M9.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

EvolutionaryTraceiO67185.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH. 1 hit.
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...

Entry informationi

Entry nameiFABH_AQUAE
AccessioniPrimary (citable) accession number: O67185
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 109 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.