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Protein

Lipoyl synthase, mitochondrial

Gene

PAAG_05935

Organism
Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Status
Reviewed-Annotation score: -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 + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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 (PAAG_05951)
  2. Lipoyl synthase, mitochondrial (PAAG_05935)
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 bindingi150Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi155Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi161Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi181Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi185Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi188Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

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:PAAG_05935
OrganismiParacoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Taxonomic identifieri502779 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenales incertae sedisParacoccidioides
Proteomesi
  • UP000002059 Componenti: Partially assembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:PAAG_05935

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 – 37MitochondrionUniRule annotationAdd BLAST37
ChainiPRO_000039827638 – 439Lipoyl synthase, mitochondrialAdd BLAST402

Interactioni

Protein-protein interaction databases

STRINGi502779.XP_002792147.1

Structurei

3D structure databases

ProteinModelPortaliC1H594
SMRiC1H594
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
KOiK03644
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
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.

C1H594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVASARGLRT LHSAHSSISA LPASTVPRLQ LAVSRCYATT TSPDCPITNS
60 70 80 90 100
SNSSNSTPTL TPKQRITAFK DKLNAGPSFS DFVSGGGASN DSVPLDPTEA
110 120 130 140 150
YSLKTALVGP PGKKKQIIRL PSWLKTPIPD SPNFRRIKSD LRGLNLHTVC
160 170 180 190 200
EEARCPNISD CWGGSSKSAA TATIMLMGDT CTRGCRFCSV KTSRTPPPLD
210 220 230 240 250
PHEPENTAEA LSRWGLGYVV MTSVDRDDLA DGGARHVAET VRKVKQKAPN
260 270 280 290 300
ILLECLTGDY AGDLEMVALV ATSGLDVFAH NVETVEALTP FVRDRRATFQ
310 320 330 340 350
QSLRVLKAAK EAKPELITKT SIMLGLGETE AQLWETLKAL RAVDVDVVTF
360 370 380 390 400
GQYMRPTKRH MAVHEYVRPD VFDSWKERAL EMGFLYCASG PLVRSSYKAG
410 420 430
EAFIENVLKK RRGEGADGSG GSSTRREDVE RLVAGGVVR
Length:439
Mass (Da):47,567
Last modified:May 26, 2009 - v1
Checksum:i3BAB21D357F78492
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN294007 Genomic DNA Translation: EEH34888.1
RefSeqiXP_002792147.1, XM_002792101.2

Genome annotation databases

EnsemblFungiiEEH34888; EEH34888; PAAG_05935
GeneIDi9095385
KEGGipbl:PAAG_05935

Similar proteinsi

Entry informationi

Entry nameiLIPA_PARBA
AccessioniPrimary (citable) accession number: C1H594
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 26, 2009
Last modified: May 23, 2018
This is version 54 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

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