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Protein

3-ketoacyl-CoA thiolase A, peroxisomal

Gene
N/A
Organism
Candida tropicalis (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei112Acyl-thioester intermediateBy similarity1
Active sitei366Proton acceptorPROSITE-ProRule annotation1
Active sitei394Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processFatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

SABIO-RKiP33290.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolase A, peroxisomal (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase A
Beta-ketothiolase A
Peroxisomal 3-oxoacyl-CoA thiolase A
Thiolase IA
OrganismiCandida tropicalis (Yeast)
Taxonomic identifieri5482 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000034075? – 4083-ketoacyl-CoA thiolase A, peroxisomal
Transit peptidei1 – ?Peroxisome

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP33290.
SMRiP33290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1389. Eukaryota.
COG0183. LUCA.

Family and domain databases

CDDicd00751. thiolase. 1 hit.
Gene3Di3.40.47.10. 2 hits.
InterProiView protein in InterPro
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
PfamiView protein in Pfam
PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiView protein in PROSITE
PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P33290-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRLNQLSGQ LKPNAKQSIL QKNPDDVVIV AAYRTAIGKG FKGSFRSVRS
60 70 80 90 100
EFILTEFLKE FIKKTNIDPS LIEDVAIGNV LNQAAGATEH RGACLAAGIP
110 120 130 140 150
YTAAFIAVNR FCSSGLMAIS DIANKIKTGE IECGLAGGAE SMSTNYRDPR
160 170 180 190 200
VAPRIDPHLA DDAQMEKCLI PMGITNENVA NQFNISRERQ DEFAAKSYNK
210 220 230 240 250
AAKAVAAGAF KSEILPIRSI IRNSDGTEKE IIVDTDEGPR EGVTAESLGK
260 270 280 290 300
LRPAFDGTTT AGNASQVSDG AAAVLLMKRS LAEAKGYPII GKYVLCSTAG
310 320 330 340 350
VPPEIMGVGP AYAIPEVLKR TGLTVDDIDV FEINEAFAAQ CLYSAEQVNV
360 370 380 390 400
PEEKLNINGG AIALGHPLGE TGARQYATII PLLKPGQIGL TSMCIGSGMG

SASILVRE
Length:408
Mass (Da):43,262
Last modified:February 1, 1994 - v1
Checksum:i4DC5212708875FA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17320 Genomic DNA. Translation: BAA04142.1.

Similar proteinsi

Entry informationi

Entry nameiTHIKA_CANTR
AccessioniPrimary (citable) accession number: P33290
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: August 30, 2017
This is version 84 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families