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Protein

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

Gene

fabH

Organism
Streptomyces lividans
Status
Reviewed-Annotation score: Annotation score: 4 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. Has some substrate preference for butyryl-CoA and can tolerate branched substrates. Can also prime acyl-CoA. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. Involved in the biosynthesis of R1128 polyketide.1 Publication

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 sitei1211 Publication1
Active sitei2571 Publication1
Active sitei2881 Publication1

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:fabH
Synonyms:zhuH
OrganismiStreptomyces lividans
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001104891 – 3393-oxoacyl-[acyl-carrier-protein] synthase 3Add BLAST339

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 20Combined sources10
Beta strandi25 – 27Combined sources3
Helixi28 – 31Combined sources4
Turni32 – 34Combined sources3
Helixi39 – 46Combined sources8
Beta strandi49 – 52Combined sources4
Helixi60 – 75Combined sources16
Helixi79 – 81Combined sources3
Beta strandi84 – 88Combined sources5
Helixi99 – 107Combined sources9
Beta strandi113 – 118Combined sources6
Helixi120 – 122Combined sources3
Helixi123 – 137Combined sources15
Beta strandi143 – 150Combined sources8
Helixi151 – 154Combined sources4
Turni160 – 165Combined sources6
Beta strandi168 – 180Combined sources13
Beta strandi187 – 190Combined sources4
Helixi192 – 197Combined sources6
Beta strandi198 – 201Combined sources4
Helixi204 – 207Combined sources4
Beta strandi211 – 213Combined sources3
Beta strandi218 – 220Combined sources3
Helixi222 – 242Combined sources21
Turni243 – 245Combined sources3
Helixi248 – 250Combined sources3
Beta strandi252 – 256Combined sources5
Helixi261 – 271Combined sources11
Beta strandi277 – 279Combined sources3
Helixi283 – 286Combined sources4
Helixi292 – 304Combined sources13
Beta strandi305 – 307Combined sources3
Beta strandi312 – 319Combined sources8
Turni320 – 322Combined sources3
Beta strandi323 – 330Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MZJX-ray2.10A/B1-339[»]
ProteinModelPortaliQ9F6D4.
SMRiQ9F6D4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F6D4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni258 – 262ACP-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 annotationCurated

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.

Q9F6D4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGLRVPERR FSRVLGVGSY RPRREVSNKE VCTWIDSTEE WIETRTGIRS
60 70 80 90 100
RRIAEPDETI QVMGVAASRR ALEHAGVDPA EIDLVVVSTM TNFVHTPPLS
110 120 130 140 150
VAIAHELGAD NAGGFDLSAA CAGFCHALSI AADAVESGGS RHVLVVATER
160 170 180 190 200
MTDVIDLADR SLSFLFGDGA GAAVVGPSDV PGIGPVVRGI DGTGLGSLHM
210 220 230 240 250
SSSWDQYVED PSVGRPALVM DGKRVFRWAV ADVVPAAREA LEVAGLTVGD
260 270 280 290 300
LVAFVPHQAN LRIIDVLVDR LGVPEHVVVS RDAEDTGNTS SASVALALDR
310 320 330
LVRSGAVPGG GPALMIGFGA GLSYAGQALL LPDPPSTPA
Length:339
Mass (Da):35,392
Last modified:March 1, 2001 - v1
Checksum:iF0CA49FD80A7A26D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293442 Genomic DNA. Translation: AAG30195.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293442 Genomic DNA. Translation: AAG30195.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MZJX-ray2.10A/B1-339[»]
ProteinModelPortaliQ9F6D4.
SMRiQ9F6D4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

EvolutionaryTraceiQ9F6D4.

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_STRLI
AccessioniPrimary (citable) accession number: Q9F6D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 77 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, Multifunctional enzyme

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.