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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Acyl-thioester intermediateUniRule annotation
Active sitei347 – 3471Proton acceptorUniRule annotation
Active sitei377 – 3771Proton acceptorUniRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 3913903-ketoacyl-CoA thiolasePRO_0000206380Add
BLAST

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 interaction.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158Combined sources
Turni21 – 233Combined sources
Turni25 – 284Combined sources
Helixi31 – 4515Combined sources
Helixi51 – 533Combined sources
Beta strandi54 – 607Combined sources
Beta strandi62 – 665Combined sources
Turni67 – 715Combined sources
Helixi72 – 776Combined sources
Beta strandi80 – 823Combined sources
Beta strandi86 – 927Combined sources
Helixi94 – 963Combined sources
Helixi97 – 11014Combined sources
Beta strandi115 – 12410Combined sources
Turni125 – 1273Combined sources
Turni130 – 1334Combined sources
Helixi138 – 1425Combined sources
Helixi146 – 1494Combined sources
Helixi151 – 16212Combined sources
Helixi166 – 18520Combined sources
Turni186 – 1927Combined sources
Beta strandi196 – 1994Combined sources
Beta strandi205 – 2084Combined sources
Helixi220 – 2245Combined sources
Turni232 – 2343Combined sources
Helixi239 – 2413Combined sources
Beta strandi246 – 25611Combined sources
Helixi257 – 2626Combined sources
Beta strandi268 – 27811Combined sources
Helixi281 – 2866Combined sources
Helixi288 – 29912Combined sources
Helixi303 – 3053Combined sources
Beta strandi308 – 3114Combined sources
Helixi316 – 32510Combined sources
Helixi329 – 3313Combined sources
Helixi332 – 3354Combined sources
Beta strandi336 – 3394Combined sources
Helixi342 – 3454Combined sources
Helixi349 – 36618Combined sources
Beta strandi370 – 3789Combined sources
Turni379 – 3813Combined sources
Beta strandi382 – 3898Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-391.
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.
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
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. Positions 2-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29090N.
IntActiP28790. 1 interaction.

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.
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...

Publicationsi

  1. "Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid beta-oxidation."
    Sato S., Hayashi M., Imamura S., Ozeki Y., Kawaguchi A.
    J. Biochem. 111:8-15(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: B-0771.

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: December 9, 2015
This is version 98 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.