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Protein

Lipoyl synthase, mitochondrial

Gene

PMAA_003450

Organism
Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei)
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 (PMAA_003350)
  2. Lipoyl synthase, mitochondrial (PMAA_003450)
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 bindingi142Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi147Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi153Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi173Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi177Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi180Iron-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:PMAA_003450
OrganismiTalaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei)
Taxonomic identifieri441960 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces
Proteomesi
  • UP000001294 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:PMAA_003450

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_000039827934 – 425Lipoyl synthase, mitochondrialAdd BLAST392

Interactioni

Protein-protein interaction databases

STRINGi441960.XP_002152494.1

Structurei

3D structure databases

ProteinModelPortaliB6QSZ4
SMRiB6QSZ4
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
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.

B6QSZ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASSTRLRC LYASSSTWKT SPSQSLISLS RRYATTSSAP PTPSDESSST
60 70 80 90 100
LPKRRKTTTF KDKLNAGPSF ADFVSGNGDS NNAPLDASEA YALETVMIPG
110 120 130 140 150
PAGRGKKEHT RLPSWLKTPI PDSTNYKRIK KDLRGLKLNT VCEEARCPNI
160 170 180 190 200
SDCWGGSDKS AATATIMLMG DSCTRGCRFC SVKTLRTPGP LDPHEPENTA
210 220 230 240 250
EALSRWGLGY VVLTSVDRDD LSDGGAHHFA ETVIKIKQKA PGILVECLTG
260 270 280 290 300
DFAGDFDMVA LVAKSGLDVY AHNVETVEAL TPHVRDRRAT FQQSLRVLEA
310 320 330 340 350
AKRAKPSLIT KTSMMLGFGE TEDQMWDALR QLRASNVDVV TFGQYMRPTK
360 370 380 390 400
RHMAVHEYVT PDKFELWRQR ALEMGFLYVA SGPLVRSSYK AGEAFIENVL
410 420
KKRRGVGNTP GAEVTTEVPV DALAK
Length:425
Mass (Da):46,515
Last modified:December 16, 2008 - v1
Checksum:iE1A082491BFA6990
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS995905 Genomic DNA Translation: EEA19557.1
RefSeqiXP_002152494.1, XM_002152458.1

Genome annotation databases

EnsemblFungiiEEA19557; EEA19557; PMAA_003450
GeneIDi7029911

Similar proteinsi

Entry informationi

Entry nameiLIPA_TALMQ
AccessioniPrimary (citable) accession number: B6QSZ4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 16, 2008
Last modified: May 23, 2018
This is version 50 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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