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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2

Gene

fabH2

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei113 – 1131UniRule annotation
Active sitei251 – 2511UniRule annotation
Active sitei281 – 2811UniRule annotation

GO - Molecular functioni

GO - Biological processi

  • 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

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2UniRule annotation (EC:2.3.1.180UniRule annotation)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III protein 2UniRule annotation
Beta-ketoacyl-ACP synthase III 2UniRule annotation
Short name:
KAS III 2UniRule annotation
Gene namesi
Name:fabH2UniRule annotation
Ordered Locus Names:VC_A0751
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 2

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 – 3623623-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2PRO_0000110503Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243277.VCA0751.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Beta strandi19 – 213Combined sources
Helixi22 – 265Combined sources
Helixi33 – 408Combined sources
Beta strandi44 – 463Combined sources
Helixi52 – 6716Combined sources
Turni71 – 733Combined sources
Beta strandi74 – 807Combined sources
Beta strandi87 – 893Combined sources
Helixi92 – 998Combined sources
Beta strandi105 – 1095Combined sources
Helixi112 – 1143Combined sources
Helixi115 – 12915Combined sources
Beta strandi134 – 1429Combined sources
Helixi143 – 1464Combined sources
Helixi152 – 1554Combined sources
Beta strandi160 – 17314Combined sources
Beta strandi175 – 1839Combined sources
Helixi185 – 1873Combined sources
Beta strandi190 – 1923Combined sources
Turni205 – 2084Combined sources
Helixi216 – 23823Combined sources
Helixi242 – 2443Combined sources
Beta strandi247 – 2504Combined sources
Helixi255 – 26511Combined sources
Helixi269 – 2713Combined sources
Helixi276 – 2794Combined sources
Helixi283 – 2853Combined sources
Helixi286 – 29611Combined sources
Beta strandi305 – 3128Combined sources
Helixi313 – 3153Combined sources
Beta strandi316 – 3238Combined sources
Helixi345 – 35915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WZUX-ray1.88A1-362[»]
4X0OX-ray2.20A/B/C/D/E/F/G/H1-362[»]
4X9KX-ray1.61A1-362[»]
4X9OX-ray2.30A/B1-362[»]
ProteinModelPortaliQ9KLJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni252 – 2565ACP-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.
OMAiMNGREVY.

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.

Q9KLJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQCYAEITG WGKCLPPATL SNHDLSTFLD TSDEWIQSRT GIEQRRISHV
60 70 80 90 100
NTSDLATVAA QHAIACAGVS VEEIDLIIVA TCSPDSLIPN IASRVQQNLG
110 120 130 140 150
IPSAAAFDLN AACTGFLYGL ETATRLMQAS HYRHALVIGA ERLSFYLDWT
160 170 180 190 200
KRDTAVLFGD GAGAVVLSKT EQKVGLQDAQ IGCDAQGRDI LAVPKFGTAM
210 220 230 240 250
DRFDADNGYW AFDFVGKEIF KRAVRGMGAA AQQVLARSGL STEEIDVVIP
260 270 280 290 300
HQANIRIIQT LCDLAGIAQD KAFVNIHRYG NTSAATVPIA LCEALEQGKI
310 320 330 340 350
KPHDDLLVAA FGAGLTWGAG HIRWGERITP LGKSDAQLPS CDHTALDLLS
360
KAIEHCKRHQ SE
Length:362
Mass (Da):39,025
Last modified:August 15, 2003 - v2
Checksum:iE0CC78C504B76213
GO

Sequence cautioni

The sequence AAF96649 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003853 Genomic DNA. Translation: AAF96649.1. Different initiation.
PIRiA82423.
RefSeqiNP_233137.2. NC_002506.1.
WP_000189735.1. NC_002506.1.

Genome annotation databases

EnsemblBacteriaiAAF96649; AAF96649; VC_A0751.
GeneIDi2611892.
KEGGivch:VCA0751.
PATRICi20086054. VBIVibCho83274_3377.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003853 Genomic DNA. Translation: AAF96649.1. Different initiation.
PIRiA82423.
RefSeqiNP_233137.2. NC_002506.1.
WP_000189735.1. NC_002506.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WZUX-ray1.88A1-362[»]
4X0OX-ray2.20A/B/C/D/E/F/G/H1-362[»]
4X9KX-ray1.61A1-362[»]
4X9OX-ray2.30A/B1-362[»]
ProteinModelPortaliQ9KLJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VCA0751.

Protocols and materials databases

DNASUi2611892.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF96649; AAF96649; VC_A0751.
GeneIDi2611892.
KEGGivch:VCA0751.
PATRICi20086054. VBIVibCho83274_3377.

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
KOiK00648.
OMAiMNGREVY.

Enzyme and pathway databases

UniPathwayiUPA00094.

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 nameiFABH2_VIBCH
AccessioniPrimary (citable) accession number: Q9KLJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: August 15, 2003
Last modified: September 7, 2016
This is version 91 of the entry and version 2 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.