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Protein

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

Gene

fabH

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
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 sitei113 – 1131UniRule annotation
Active sitei246 – 2461UniRule annotation
Active sitei276 – 2761UniRule 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

BioCyciEFAE226185:GHI1-2816-MONOMER.
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:EF_2885
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5070.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3213213-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110427Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi226185.EF2885.

Chemistry

BindingDBiQ820T1.

Structurei

Secondary structure

1
321
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 strandi42 – 454Combined sources
Helixi52 – 6716Combined sources
Helixi71 – 733Combined sources
Beta strandi76 – 805Combined sources
Beta strandi87 – 893Combined sources
Helixi91 – 988Combined sources
Beta strandi105 – 1095Combined sources
Helixi112 – 1143Combined sources
Helixi115 – 12814Combined sources
Beta strandi135 – 1417Combined sources
Helixi143 – 1464Combined sources
Turni152 – 1543Combined sources
Helixi155 – 1573Combined sources
Beta strandi161 – 17212Combined sources
Beta strandi175 – 1828Combined sources
Helixi184 – 1896Combined sources
Beta strandi190 – 1923Combined sources
Helixi216 – 23217Combined sources
Helixi237 – 2393Combined sources
Beta strandi241 – 2455Combined sources
Helixi250 – 26011Combined sources
Helixi264 – 2663Combined sources
Helixi271 – 2733Combined sources
Helixi278 – 2803Combined sources
Helixi281 – 29111Combined sources
Beta strandi302 – 3098Combined sources
Turni310 – 3123Combined sources
Beta strandi313 – 3208Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IL4X-ray3.00A/B/C/D2-321[»]
3IL5X-ray2.60A/B/C/D1-321[»]
3IL6X-ray2.50A1-321[»]
ProteinModelPortaliQ820T1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ820T1.

Family & Domainsi

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 annotation

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
KOiK00648.
OMAiEKHANCS.
OrthoDBiEOG6J74XN.

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.

Q820T1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNYARISCT SRYVPENCVT NHQLSEMMDT SDEWIHSRTG ISERRIVTQE
60 70 80 90 100
NTSDLCHQVA KQLLEKSGKQ ASEIDFILVA TVTPDFNMPS VACQVQGAIG
110 120 130 140 150
ATEAFAFDIS AACSGFVYAL SMAEKLVLSG RYQTGLVIGG ETFSKMLDWT
160 170 180 190 200
DRSTAVLFGD GAAGVLIEAA ETPHFLNEKL QADGQRWAAL TSGYTINESP
210 220 230 240 250
FYQGHKQASK TLQMEGRSIF DFAIKDVSQN ILSLVTDETV DYLLLHQANV
260 270 280 290 300
RIIDKIARKT KISREKFLTN MDKYGNTSAA SIPILLDEAV ENGTLILGSQ
310 320
QRVVLTGFGG GLTWGSLLLT L
Length:321
Mass (Da):35,182
Last modified:June 1, 2003 - v1
Checksum:i1306C774594D6D9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO82575.1.
RefSeqiNP_816505.1. NC_004668.1.
WP_002365153.1. NZ_KE136528.1.

Genome annotation databases

EnsemblBacteriaiAAO82575; AAO82575; EF_2885.
GeneIDi1201733.
KEGGiefa:EF2885.
PATRICi21855943. VBIEntFae7065_2689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO82575.1.
RefSeqiNP_816505.1. NC_004668.1.
WP_002365153.1. NZ_KE136528.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IL4X-ray3.00A/B/C/D2-321[»]
3IL5X-ray2.60A/B/C/D1-321[»]
3IL6X-ray2.50A1-321[»]
ProteinModelPortaliQ820T1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226185.EF2885.

Chemistry

BindingDBiQ820T1.
ChEMBLiCHEMBL5070.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO82575; AAO82575; EF_2885.
GeneIDi1201733.
KEGGiefa:EF2885.
PATRICi21855943. VBIEntFae7065_2689.

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
KOiK00648.
OMAiEKHANCS.
OrthoDBiEOG6J74XN.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciEFAE226185:GHI1-2816-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ820T1.
PROiQ820T1.

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 700802 / V583.

Entry informationi

Entry nameiFABH_ENTFA
AccessioniPrimary (citable) accession number: Q820T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 90 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.