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Protein

Lipoyl synthase, mitochondrial

Gene

LmjF19.0350

Organism
Leishmania major
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.

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.

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.

Cofactori

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

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].
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Lipoyl synthase, mitochondrial (LmjF19.0350)
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 bindingi125Iron-sulfur 1 (4Fe-4S)1
Metal bindingi130Iron-sulfur 1 (4Fe-4S)1
Metal bindingi136Iron-sulfur 1 (4Fe-4S)1
Metal bindingi157Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi161Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi164Iron-sulfur 2 (4Fe-4S-S-AdoMet)1

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, mitochondrial (EC:2.8.1.8)
Alternative name(s):
Lipoate synthase
Short name:
LS
Short name:
Lip-syn
Lipoic acid synthase
Gene namesi
ORF Names:LmjF19.0350, LmjF_19_0350
OrganismiLeishmania major
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
Proteomesi
  • UP000000542 Componenti: Chromosome 19

Subcellular locationi

  • Mitochondrion

GO - Cellular componenti

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003982381 – 410Lipoyl synthase, mitochondrialAdd BLAST410

Interactioni

Protein-protein interaction databases

STRINGi5664.LmjF.19.0350.

Structurei

3D structure databases

ProteinModelPortaliQ4QDI6.
SMRiQ4QDI6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
HOGENOMiHOG000235998.
InParanoidiQ4QDI6.
KOiK03644.

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.

Q4QDI6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCPTAVPSRV SPVAAAAAAD IAGSSESTVS LVADVDKKNS QYKQIFLERF
60 70 80 90 100
RKKLQSDKTG MNNLESFVEL PEGVAPSAAS IGPIKRGSEP LPPWIKLKVP
110 120 130 140 150
KGMTHRPRFN RIRRSMREKN LSTVCEEAKC PNIGECWGGS DEEGTATATI
160 170 180 190 200
MVMGSHCTRG CRFCSVLTSR RPPPLDPEEP EKVAAAVHEM GVDYIVMTMV
210 220 230 240 250
DRDDLPDGGA SHVCCCIHTI KKKNPELMLE ALVGDFHGDL KLVEQLAVTP
260 270 280 290 300
LSVYAHNIEC VERITPRVRD RRASYRQSLQ TLEHVTKWTN GNMLTKSSIM
310 320 330 340 350
LGLGEEEAEV RQTLRDLRTA GVSAVTLGQY LQPSHTRLKV SRYAHPKEFE
360 370 380 390 400
MWEKEAMDMG FLYCASGPMV RSSYRAGEYY IKNILKQRQS AEGGKAAAAA
410
TAVNAGTAIA
Length:410
Mass (Da):45,055
Last modified:July 19, 2005 - v1
Checksum:i70CED969AE71BD5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796415 Genomic DNA. Translation: CAJ07120.1.
RefSeqiXP_001682612.1. XM_001682560.1.

Genome annotation databases

GeneDBiLmjF.19.0350:pep.
GeneIDi5651134.
KEGGilma:LMJF_19_0350.

Similar proteinsi

Entry informationi

Entry nameiLIPA_LEIMA
AccessioniPrimary (citable) accession number: Q4QDI6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 19, 2005
Last modified: October 25, 2017
This is version 72 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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