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Protein

3-ketoacyl-CoA thiolase

Gene

fadA

Organism
Pseudomonas fragi
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.UniRule annotation

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.UniRule annotation

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, 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 beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei95Acyl-thioester intermediateUniRule annotation1
Active sitei347Proton acceptorUniRule annotation1
Active sitei377Proton acceptorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.16. 5123.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolaseUniRule annotation (EC:2.3.1.16UniRule annotation)
Alternative name(s):
Acetyl-CoA acyltransferaseUniRule annotation
Beta-ketothiolaseUniRule annotation
Fatty acid oxidation complex subunit betaUniRule annotation
Gene namesi
Name:fadAUniRule annotation
Synonyms:faoB
OrganismiPseudomonas fragi
Taxonomic identifieri296 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002063802 – 3913-ketoacyl-CoA thiolaseAdd BLAST390

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
fadBP287933EBI-1039311,EBI-1039318

Protein-protein interaction databases

DIPiDIP-29090N.
IntActiP28790. 1 interactor.

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 15Combined sources8
Turni21 – 23Combined sources3
Turni25 – 28Combined sources4
Helixi31 – 45Combined sources15
Helixi51 – 53Combined sources3
Beta strandi54 – 60Combined sources7
Beta strandi62 – 66Combined sources5
Turni67 – 71Combined sources5
Helixi72 – 77Combined sources6
Beta strandi80 – 82Combined sources3
Beta strandi86 – 92Combined sources7
Helixi94 – 96Combined sources3
Helixi97 – 110Combined sources14
Beta strandi115 – 124Combined sources10
Turni125 – 127Combined sources3
Turni130 – 133Combined sources4
Helixi138 – 142Combined sources5
Helixi146 – 149Combined sources4
Helixi151 – 162Combined sources12
Helixi166 – 185Combined sources20
Turni186 – 192Combined sources7
Beta strandi196 – 199Combined sources4
Beta strandi205 – 208Combined sources4
Helixi220 – 224Combined sources5
Turni232 – 234Combined sources3
Helixi239 – 241Combined sources3
Beta strandi246 – 256Combined sources11
Helixi257 – 262Combined sources6
Beta strandi268 – 278Combined sources11
Helixi281 – 286Combined sources6
Helixi288 – 299Combined sources12
Helixi303 – 305Combined sources3
Beta strandi308 – 311Combined sources4
Helixi316 – 325Combined sources10
Helixi329 – 331Combined sources3
Helixi332 – 335Combined sources4
Beta strandi336 – 339Combined sources4
Helixi342 – 345Combined sources4
Helixi349 – 366Combined sources18
Beta strandi370 – 378Combined sources9
Turni379 – 381Combined sources3
Beta strandi382 – 389Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WDKX-ray2.50C/D2-391[»]
1WDLX-ray3.50C/D2-391[»]
1WDMX-ray3.80C/D2-391[»]
2D3TX-ray3.40C/D2-391[»]
ProteinModelPortaliP28790.
SMRiP28790.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28790.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.UniRule annotation

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
HAMAPiMF_01620. FadA. 1 hit.
InterProiIPR012805. FadA.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02445. fadA. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KVLERNSKVD
60 70 80 90 100
PGEVEDVIWG CVNQTLEQGW NIARMASLMT QIPHTSAAQT VSRLCGSSMS
110 120 130 140 150
ALHTAAQAIM TGNGDVFVVG GVEHMGHVSM MHGVDPNPHM SLYAAKASGM
160 170 180 190 200
MGLTAEMLGK MHGISREQQD AFAVRSHQLA HKATVEGKFK DEIIPMQGYD
210 220 230 240 250
ENGFLKIFDY DETIRPDTTL ESLAALKPAF NPKGGTVTAG TSSQITDGAS
260 270 280 290 300
CMIVMSAQRA KDLGLEPLAV IRSMAVAGVD PAIMGYGPVP ATQKALKRAG
310 320 330 340 350
LNMADIDFIE LNEAFAAQAL PVLKDLKVLD KMNEKVNLHG GAIALGHPFG
360 370 380 390
CSGARISGTL LNVMKQNGGT FGLSTMCIGL GQGIATVFER V
Length:391
Mass (Da):41,606
Last modified:January 23, 2007 - v2
Checksum:i3C5F24D816DB9EA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10390 Genomic DNA. Translation: BAA01228.1.
PIRiJS0624.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10390 Genomic DNA. Translation: BAA01228.1.
PIRiJS0624.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WDKX-ray2.50C/D2-391[»]
1WDLX-ray3.50C/D2-391[»]
1WDMX-ray3.80C/D2-391[»]
2D3TX-ray3.40C/D2-391[»]
ProteinModelPortaliP28790.
SMRiP28790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29090N.
IntActiP28790. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00659.
BRENDAi2.3.1.16. 5123.

Miscellaneous databases

EvolutionaryTraceiP28790.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
HAMAPiMF_01620. FadA. 1 hit.
InterProiIPR012805. FadA.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02445. fadA. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFADA_PSEFR
AccessioniPrimary (citable) accession number: P28790
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 100 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, Direct protein sequencing

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.