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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1

Gene

fabH1

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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 sitei112UniRule annotation1
Active sitei243UniRule annotation1
Active sitei273UniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • fatty acid beta-oxidation Source: GO_Central
  • fatty acid biosynthetic process Source: TIGR
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

BioCyciVCHO:VC2023-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1UniRule annotation (EC:2.3.1.180UniRule annotation)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III protein 1UniRule annotation
Beta-ketoacyl-ACP synthase III 1UniRule annotation
Short name:
KAS III 1UniRule annotation
Gene namesi
Name:fabH1UniRule annotation
Ordered Locus Names:VC_2023
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

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_00001105021 – 3163-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1Add BLAST316

Proteomic databases

PRIDEiQ9KQH5.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243277.VC2023.

Structurei

Secondary structure

1316
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 11Combined sources10
Beta strandi14 – 18Combined sources5
Helixi19 – 25Combined sources7
Helixi30 – 37Combined sources8
Beta strandi41 – 44Combined sources4
Helixi51 – 66Combined sources16
Helixi70 – 72Combined sources3
Beta strandi75 – 79Combined sources5
Beta strandi84 – 88Combined sources5
Helixi90 – 98Combined sources9
Beta strandi105 – 109Combined sources5
Helixi111 – 113Combined sources3
Helixi114 – 127Combined sources14
Beta strandi132 – 141Combined sources10
Helixi142 – 145Combined sources4
Helixi151 – 154Combined sources4
Beta strandi159 – 171Combined sources13
Beta strandi173 – 181Combined sources9
Helixi186 – 188Combined sources3
Beta strandi189 – 192Combined sources4
Helixi208 – 229Combined sources22
Helixi234 – 236Combined sources3
Beta strandi239 – 242Combined sources4
Helixi247 – 256Combined sources10
Helixi261 – 263Combined sources3
Helixi268 – 271Combined sources4
Helixi275 – 277Combined sources3
Helixi278 – 288Combined sources11
Beta strandi297 – 304Combined sources8
Turni305 – 307Combined sources3
Beta strandi308 – 315Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NHDX-ray1.78A/B/C/D1-316[»]
ProteinModelPortaliQ9KQH5.
SMRiQ9KQH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 248ACP-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.
KOiK00648.
OMAiESGMYEN.

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.

Q9KQH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYSKILGTGS YLPSQVRTNA DLEKMVETSD EWIVARTGIR ERRIAADNET
60 70 80 90 100
VADMAFFAAQ NAINMAGIDK HDIDMIIVAT TSASHTFPSA ACQVQGKLGI
110 120 130 140 150
KGCPAFDLAA ACSGFMYALS IADQHVKSGM CKHVLVIGAD ALSKTCDPTD
160 170 180 190 200
RSTIILFGDG AGAVVVGASN EPGILSTHIH ADGEFGDLLS LEVPVRGGDS
210 220 230 240 250
DKWLHMAGNE VFKVAVTQLS KLVVDTLKAN NMHKSELDWL VPHQANYRII
260 270 280 290 300
SATAKKLSMS LDQVVITLDR HGNTSAATVP TALDEAVRDG RIQRGQMLLL
310
EAFGGGFTWG SALVKF
Length:316
Mass (Da):33,749
Last modified:October 1, 2000 - v1
Checksum:i041CF820D7C35173
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95171.1.
PIRiH82128.
RefSeqiNP_231657.1. NC_002505.1.
WP_000287010.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF95171; AAF95171; VC_2023.
GeneIDi2613402.
KEGGivch:VC2023.
PATRICi20083078. VBIVibCho83274_1933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95171.1.
PIRiH82128.
RefSeqiNP_231657.1. NC_002505.1.
WP_000287010.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NHDX-ray1.78A/B/C/D1-316[»]
ProteinModelPortaliQ9KQH5.
SMRiQ9KQH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC2023.

Proteomic databases

PRIDEiQ9KQH5.

Protocols and materials databases

DNASUi2613402.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF95171; AAF95171; VC_2023.
GeneIDi2613402.
KEGGivch:VC2023.
PATRICi20083078. VBIVibCho83274_1933.

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
KOiK00648.
OMAiESGMYEN.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciVCHO:VC2023-MONOMER.

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 nameiFABH1_VIBCH
AccessioniPrimary (citable) accession number: Q9KQH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 93 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.