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Protein

Lipoyl synthase, mitochondrial

Gene

PABG_05724

Organism
Paracoccidioides brasiliensis (strain Pb03)
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 (PABG_05708)
  2. Lipoyl synthase, mitochondrial (PABG_05724)
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 bindingi144Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi149Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi155Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi175Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi179Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi182Iron-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:PABG_05724
OrganismiParacoccidioides brasiliensis (strain Pb03)
Taxonomic identifieri482561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenales incertae sedisParacoccidioides
Proteomesi
  • UP000002740 Componenti: Unassembled WGS sequence

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_000039827732 – 434Lipoyl synthase, mitochondrialAdd BLAST403

Proteomic databases

PRIDEiC0SDG9

Structurei

3D structure databases

ProteinModelPortaliC0SDG9
SMRiC0SDG9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiC0SDG9
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.

C0SDG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASARGLRT LQSAHSSTTV PRLQLAVSRC YATTTSPDPP ITNSSNSSNS
60 70 80 90 100
TPTPKQRITA FKDKLNAGPS FSDFVSGGGG GASNDRVPLD PAEAYALKTA
110 120 130 140 150
LVGPPGRKKQ IIRLPSWLKT PIPDTPNYRR IKSDLRGLNL HTVCEEARCP
160 170 180 190 200
NISDCWGGSS KSAATATIML MGDTCTRGCR FCSVKTSRTP PPLDPHEPEN
210 220 230 240 250
TAEALSRWGL GYVVMTSVDR DDLADGGARH VAETVRKVKQ KAPGILLECL
260 270 280 290 300
TGDYAGDLEM VALVATSGLD VFAHNVETVE ALTPFVRDRR ATFQQSLRVL
310 320 330 340 350
KAAKEARPEL ITKTSIMLGL GETETQLWET LRALRTVDVD VVTFGQYMRP
360 370 380 390 400
TKRHMAVHEY VRPGVFDLWK ERALEMGFLY CASGPLVRSS YKAGEAFIEN
410 420 430
VLKKRRGEGA DGGDGGNSTR REDVERLVAG GVVR
Length:434
Mass (Da):47,106
Last modified:May 5, 2009 - v1
Checksum:i02DABF6FB68CDDA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN305539 Genomic DNA Translation: EEH23513.1

Genome annotation databases

EnsemblFungiiEEH23513; EEH23513; PABG_05724

Similar proteinsi

Entry informationi

Entry nameiLIPA_PARBP
AccessioniPrimary (citable) accession number: C0SDG9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 5, 2009
Last modified: May 23, 2018
This is version 45 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

Documents

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

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