Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei121 – 12111 Publication
Active sitei257 – 25711 Publication
Active sitei288 – 28811 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3393393-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110489Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 2010Combined sources
Beta strandi25 – 273Combined sources
Helixi28 – 314Combined sources
Turni32 – 343Combined sources
Helixi39 – 468Combined sources
Beta strandi49 – 524Combined sources
Helixi60 – 7516Combined sources
Helixi79 – 813Combined sources
Beta strandi84 – 885Combined sources
Helixi99 – 1079Combined sources
Beta strandi113 – 1186Combined sources
Helixi120 – 1223Combined sources
Helixi123 – 13715Combined sources
Beta strandi143 – 1508Combined sources
Helixi151 – 1544Combined sources
Turni160 – 1656Combined sources
Beta strandi168 – 18013Combined sources
Beta strandi187 – 1904Combined sources
Helixi192 – 1976Combined sources
Beta strandi198 – 2014Combined sources
Helixi204 – 2074Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi218 – 2203Combined sources
Helixi222 – 24221Combined sources
Turni243 – 2453Combined sources
Helixi248 – 2503Combined sources
Beta strandi252 – 2565Combined sources
Helixi261 – 27111Combined sources
Beta strandi277 – 2793Combined sources
Helixi283 – 2864Combined sources
Helixi292 – 30413Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi312 – 3198Combined sources
Turni320 – 3223Combined sources
Beta strandi323 – 3308Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZJX-ray2.10A/B1-339[»]
ProteinModelPortaliQ9F6D4.
SMRiQ9F6D4. Positions 2-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F6D4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni258 – 2625ACP-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 annotationCurated

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZJX-ray2.10A/B1-339[»]
ProteinModelPortaliQ9F6D4.
SMRiQ9F6D4. Positions 2-335.
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.
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. "Cloning, nucleotide sequence, and heterologous expression of the biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor antagonist. Insights into an unusual priming mechanism."
    Marti T., Hu Z., Pohl N.L., Shah A.N., Khosla C.
    J. Biol. Chem. 275:33443-33448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase."
    Meadows E.S., Khosla C.
    Biochemistry 40:14855-14861(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
  3. "Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway."
    Pan H., Tsai S.-C., Meadows E.S., Miercke L.J.W., Keatinge-Clay A.T., O'Connell J.D. III, Khosla C., Stroud R.M.
    Structure 10:1559-1568(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT, ACTIVE SITE.

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: January 20, 2016
This is version 75 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.