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O67185

- FABH_AQUAE

UniProt

O67185 - FABH_AQUAE

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Protein

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

Gene

fabH

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei111 – 1111UniRule annotation
Active sitei236 – 2361UniRule annotation
Active sitei266 – 2661UniRule annotation

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: InterPro
  2. beta-ketoacyl-acyl-carrier-protein synthase III activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciAAEO224324:GJBH-783-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:aq_1099
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
ProteomesiUP000000798: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3093093-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110392Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224324.aq_1099.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Beta strandi14 – 185Combined sources
Helixi19 – 235Combined sources
Helixi30 – 378Combined sources
Beta strandi41 – 444Combined sources
Helixi50 – 6516Combined sources
Helixi69 – 713Combined sources
Beta strandi73 – 786Combined sources
Beta strandi83 – 875Combined sources
Helixi89 – 979Combined sources
Beta strandi103 – 1086Combined sources
Helixi110 – 1123Combined sources
Helixi113 – 12614Combined sources
Beta strandi131 – 14010Combined sources
Helixi141 – 1433Combined sources
Turni150 – 1556Combined sources
Beta strandi158 – 16710Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi173 – 1819Combined sources
Helixi183 – 1886Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi197 – 1993Combined sources
Helixi201 – 22323Combined sources
Helixi227 – 2293Combined sources
Beta strandi231 – 2355Combined sources
Helixi240 – 24910Combined sources
Helixi254 – 2563Combined sources
Helixi261 – 2644Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 28111Combined sources
Beta strandi290 – 2978Combined sources
Turni298 – 3003Combined sources
Beta strandi301 – 3088Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBDX-ray2.10A/B1-309[»]
ProteinModelPortaliO67185.
SMRiO67185. Positions 1-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67185.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni237 – 2415ACP-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

eggNOGiCOG0332.
HOGENOMiHOG000246674.
InParanoidiO67185.
KOiK00648.
OMAiAHIVEET.
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.
IPR016038. Thiolase-like_subgr.
[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.

O67185-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGTKIIGTGV YLPKNVLTNF DLEKIVDTSD EWITTRTGIK ERRIAKEETI
60 70 80 90 100
TYMATQAAKE ALREANLSPE ELDLIILATL TPQKRFPSTA CLVQAQLKAK
110 120 130 140 150
GVYAFDISAA CSGFIYALDI ADSFIKSGKA KNVLVIGAEK LSEAVDWEDR
160 170 180 190 200
STCVLFGDGA GAVVVTRSED KSDILATRMY AEGSLEELLH ADNCGYIRMK
210 220 230 240 250
GRELFKVAVR SMEEVCREVL EKAGVKPEEV SLVIPHQANV RIINALAEKL
260 270 280 290 300
NIPKEKVFVN IQKYGNTSAA SIPIALHEAI KEGKVKRGDL ILMTAMGGGL

TWGAVLLRY
Length:309
Mass (Da):33,825
Last modified:August 1, 1998 - v1
Checksum:iEB97518DB168140D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07144.1.
PIRiF70394.
RefSeqiNP_213748.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07144; AAC07144; aq_1099.
GeneIDi1193819.
KEGGiaae:aq_1099.
PATRICi20959474. VBIAquAeo85532_0857.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07144.1 .
PIRi F70394.
RefSeqi NP_213748.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EBD X-ray 2.10 A/B 1-309 [» ]
ProteinModelPortali O67185.
SMRi O67185. Positions 1-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224324.aq_1099.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC07144 ; AAC07144 ; aq_1099 .
GeneIDi 1193819.
KEGGi aae:aq_1099.
PATRICi 20959474. VBIAquAeo85532_0857.

Phylogenomic databases

eggNOGi COG0332.
HOGENOMi HOG000246674.
InParanoidi O67185.
KOi K00648.
OMAi AHIVEET.
OrthoDBi EOG6J74XN.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci AAEO224324:GJBH-783-MONOMER.

Miscellaneous databases

EvolutionaryTracei O67185.

Family and domain databases

Gene3Di 3.40.47.10. 2 hits.
HAMAPi MF_01815. FabH.
InterProi IPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 1 hit.
TIGRFAMsi TIGR00747. fabH. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.
  2. "Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    Strain: VF5.

Entry informationi

Entry nameiFABH_AQUAE
AccessioniPrimary (citable) accession number: O67185
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 97 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

External Data

Dasty 3