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Protein

Lipoyl synthase, mitochondrial

Gene

Pa_1_14620

Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
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. no protein annotated in this organism
  2. Lipoyl synthase, mitochondrial (Pa_1_14620)
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 bindingi140Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi145Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi151Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi171Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi175Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi178Iron-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
Ordered Locus Names:Pa_1_14620
ORF Names:PODANS_1_14620
OrganismiPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Taxonomic identifieri515849 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora
Proteomesi

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 – 29MitochondrionUniRule annotationAdd BLAST29
ChainiPRO_000039828430 – 426Lipoyl synthase, mitochondrialAdd BLAST397

Proteomic databases

PRIDEiB2AT43

Interactioni

Protein-protein interaction databases

STRINGi515849.XP_001906895.1

Structurei

3D structure databases

ProteinModelPortaliB2AT43
SMRiB2AT43
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.

B2AT43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPAPLQRL QAPLRRSLAR AAVLSSRTYA TIPSPSDPGL TQSSPSPAAS
60 70 80 90 100
TTPAKKAPRP SYFKDTTVAS FSEFVGSQSA PLSLSEAYEI KTAEVGPAGR
110 120 130 140 150
KRTITRLPEW LKTPIPSSGA NPNFGKIKAD LRGLNLHTVC EEARCPNIGE
160 170 180 190 200
CWGGNDKSAA TATIMLMGDT CTRGCRFCSV KTNRKPPPLD PHEPENTAEA
210 220 230 240 250
LARWGLGYVV LTSVDRDDLA DGGARHFAET IRRIKQKKPT LLVEALTGDF
260 270 280 290 300
MGDLDMVKIV AESGLDVYAH NVETVEGLTP YVRDRRATFR QSLKVLEHVK
310 320 330 340 350
AVRGKEGIIT KTSIMLGLGE QEQEIWDTLR ELRKIDVDVV TFGQYMRPTK
360 370 380 390 400
RHLKVEKYVT PDEFDLWKQR ALDMGFLYCA SGPLVRSSYK AGEAFIENVL
410 420
RKRAGERAAA SASLDQVVAA EETKAL
Length:426
Mass (Da):46,688
Last modified:May 20, 2008 - v1
Checksum:i09B7F18A38D991A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633899 Genomic DNA Translation: CAP67566.1
FO904936 Genomic DNA Translation: CDP23827.1
RefSeqiXP_001906895.1, XM_001906860.1

Genome annotation databases

EnsemblFungiiCAP67566; CAP67566; PODANS_1_14620
GeneIDi6191609
KEGGipan:PODANSg3928

Similar proteinsi

Entry informationi

Entry nameiLIPA_PODAN
AccessioniPrimary (citable) accession number: B2AT43
Secondary accession number(s): A0A090CEZ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 20, 2008
Last modified: May 23, 2018
This is version 59 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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