Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

ACLA_034510

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.UniRule annotation

Catalytic activityi

Protein N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Octanoyltransferase (ACLA_034640)
  2. Lipoyl synthase, mitochondrial (ACLA_034510)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi132Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi137Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi143Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi163Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi167Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi170Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
ORF Names:ACLA_034510
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006701 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ACLA_034510.

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

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 33MitochondrionUniRule annotationAdd BLAST33
ChainiPRO_000039825134 – 415Lipoyl synthase, mitochondrialAdd BLAST382

Interactioni

Protein-protein interaction databases

STRINGi5057.CADACLAP00003729.

Structurei

3D structure databases

ProteinModelPortaliA1CJC4.
SMRiA1CJC4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998.
KOiK03644.
OMAiPYCDIDF.
OrthoDBiEOG092C13O2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
PfamiView protein in Pfam
PF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SFLDiSFLDG01058. lipoyl_synthase_like. 1 hit.
SFLDS00029. Radical_SAM. 1 hit.
SMARTiView protein in SMART
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A1CJC4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTSHLRS LCSSTRSLSR SGVIVTPIAC RGYATTDPSP SATTPTPVRR
60 70 80 90 100
RTTFKDKLNA GPSFSDFVSN GNDNAPLDPS EAYALKTALV GPAGRKKEMT
110 120 130 140 150
RLPSWLKTPI PDSKNYQRLK KDLRGLNLHT VCEEARCPNI SDCWGGSDKS
160 170 180 190 200
SATATIMLMG DTCTRGCRFC SVKTSRAPPP LDPHEPENTA EAISRWGLGY
210 220 230 240 250
VVLTSVDRDD LVDGGARHFA ETVIKIKQKA PSILVECLTG DYAGDLDMVK
260 270 280 290 300
LVARSGLDVY AHNVETVEAL TPQVRDRRAN FQQSLRVLDA AKKAQPTLIT
310 320 330 340 350
KTSLMLGLGE TDEQLWDALR QLRAVNVDVV TFGQYMRPTK RHMAVHEYVT
360 370 380 390 400
PDRFELWRQR ALEMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAASGGA
410
ETIGERPVAV DEASR
Length:415
Mass (Da):45,519
Last modified:January 23, 2007 - v1
Checksum:iDE25AD5BD2982A90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027056 Genomic DNA. Translation: EAW09248.1.
RefSeqiXP_001270674.1. XM_001270673.1.

Genome annotation databases

EnsemblFungiiCADACLAT00003809; CADACLAP00003729; CADACLAG00003809.
GeneIDi4702900.
KEGGiact:ACLA_034510.

Similar proteinsi

Entry informationi

Entry nameiLIPA_ASPCL
AccessioniPrimary (citable) accession number: A1CJC4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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