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

PADG_06059

Organism
Paracoccidioides brasiliensis (strain Pb18)
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 (PADG_06042)
  2. Lipoyl synthase, mitochondrial (PADG_06059)
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 bindingi148Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi153Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi159Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi179Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi183Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi186Iron-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:PADG_06059
OrganismiParacoccidioides brasiliensis (strain Pb18)
Taxonomic identifieri502780 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenales incertae sedisParacoccidioides
Proteomesi
  • UP000001628 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:PADG_06059

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 – 31MitochondrionUniRule annotationAdd BLAST31
ChainiPRO_000039827832 – 438Lipoyl synthase, mitochondrialAdd BLAST407

Proteomic databases

PRIDEiC1GFM3

Structurei

3D structure databases

ProteinModelPortaliC1GFM3
SMRiC1GFM3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

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.

C1GFM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASARGLRT LQSAHSSTTV PRLQLAVSRC YATTTSPDPP ITNSSNSSNS
60 70 80 90 100
SNSTPTPKQR ITAFKDKLNA GPSFSDFVSG GGGGGASNDR VPLDPAEAYA
110 120 130 140 150
LKTALVGPPG RKKQIIRLPS WLKTPIPDTP NYRRIKSDLR GLNLHTVCEE
160 170 180 190 200
ARCPNISDCW GGSSKSAATA TIMLMGDTCT RGCRFCSVKT SRTPPPLDPH
210 220 230 240 250
EPENTAEALS RWGLGYVVMT SVDRDDLADG GARHVVETVR KVKQKAPGIL
260 270 280 290 300
LECLTGDYAG DLEMVALVAT SGLDVFAHNV ETVEALTPFV RDRRATFQQS
310 320 330 340 350
LRVLKAAKEA RPELITKTSI MLGLGETETQ LWETLRALRA VDVDVVTFGQ
360 370 380 390 400
YMRPTKRHMA VHEYVRPEVF DLWKERALEM GFLYCASGPL VRSSYKAGEA
410 420 430
FIENVLKKRR GEGADGGDGG NSTRREDVER LVAGGVVR
Length:438
Mass (Da):47,521
Last modified:May 26, 2009 - v1
Checksum:i348C53B8A25B3F3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN275963 Genomic DNA Translation: EEH49980.1
RefSeqiXP_010761520.1, XM_010763218.1

Genome annotation databases

EnsemblFungiiEEH49980; EEH49980; PADG_06059
GeneIDi22584868
KEGGipbn:PADG_06059

Similar proteinsi

Entry informationi

Entry nameiLIPA_PARBD
AccessioniPrimary (citable) accession number: C1GFM3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 26, 2009
Last modified: May 23, 2018
This is version 52 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health