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Protein

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

Gene

fabH

Organism
Thermus thermophilus
Status
Unreviewed-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 annotationSAAS annotation

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotationSAAS 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 sitei110 – 1101UniRule annotation
Active sitei246 – 2461UniRule annotation
Active sitei276 – 2761UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationSAAS annotation, Transferase

Keywords - Biological processi

Fatty acid biosynthesisUniRule annotationSAAS annotation, 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
Gene namesi
Name:fabHUniRule annotation
OrganismiThermus thermophilusImported
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi262724.TTC0049.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UB7X-ray2.30A/B/C/D1-322[»]
ProteinModelPortaliQ7SI99.
SMRiQ7SI99. Positions 2-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SI99.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 18279ACP_syn_IIIInterPro annotationAdd
BLAST
Domaini230 – 31990ACP_syn_III_CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni247 – 2515ACP-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 annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.

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.

Q7SI99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGILALGAY VPERVMTNAD FEAYLDTSDE WIVTRTGIKE RRVAAEDEYT
60 70 80 90 100
SDLAFKAVED LLRRHPGALE GVDAVIVATN TPDALFPDTA ALVQARFGLK
110 120 130 140 150
AFAYDLLAGC PGWIYALAQA HALVEAGLAQ KVLAVGAEAL SKIIDWNDRA
160 170 180 190 200
TAVLFGDGGG AAVVGKVREG YGFRSFVLGA DGTGAKELYH ACVAPRLPDG
210 220 230 240 250
TSMKNRLYMN GREVFKFAVR VMNTATLEAI EKAGLTPEDI RLFVPHQANL
260 270 280 290 300
RIIDAARERL GLPWERVAVN VDRYGNTSTA SIPLALKEAV DAGRIREGDH
310 320
VLLVSFGAGL TWAAAVLTWG GA
Length:322
Mass (Da):34,517
Last modified:December 15, 2003 - v1
Checksum:i9E83F0BBBCE28BB2
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UB7X-ray2.30A/B/C/D1-322[»]
ProteinModelPortaliQ7SI99.
SMRiQ7SI99. Positions 2-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC0049.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

EvolutionaryTraceiQ7SI99.

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. "The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase III (Fabh) from Thermus Thermophilus."
    Inagaki E., Kuramitsu S., Yokoyama S., Miyano M., Tahirov T.H.
    Submitted (MAR-2003) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).

Entry informationi

Entry nameiQ7SI99_THETH
AccessioniPrimary (citable) accession number: Q7SI99
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 6, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Multifunctional enzymeUniRule annotationSAAS annotation

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.