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Protein

Lipoyl synthase, mitochondrial

Gene

COCHEDRAFT_1178395

Organism
Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern corn leaf blight fungus) (Bipolaris maydis)
Status
Unreviewed-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.UniRule annotation

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.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 (COCHEDRAFT_1177823)
  2. Lipoyl synthase, mitochondrial (COCHEDRAFT_1178395)
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 bindingi129Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi134Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi140Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi160Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi164Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi167Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotation
Ligand4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotation

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:COCHEDRAFT_1178395Imported
OrganismiCochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern corn leaf blight fungus) (Bipolaris maydis)Imported
Taxonomic identifieri701091 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeBipolaris
Proteomesi
  • UP000016936 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

MitochondrionUniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini150 – 359Elp3InterPro annotationAdd BLAST210

Sequence similaritiesi

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

Phylogenomic databases

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.
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.

M2UQ93-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASIPRTRC LAALKAVPRS TAPLRSFATT SDAPQPPASE TPSKRSRPAT
60 70 80 90 100
SFSDTLNAGP SFGDFVNPNA PLSPAEAYEI KTVQVGPEGR KKTITRLPEW
110 120 130 140 150
LRTPIPSNAN QNYKQIKKDL RGLNLATVCE EARCPNISDC WGGSSKSAAT
160 170 180 190 200
ATIMLMGDTC TRGCRFCAVK TSKAPPPLDP HEPENTAEAL RRWGLGYVVI
210 220 230 240 250
TVVDRDDLAD SGAHHIAETI MKIKQKNPTQ LVELLGGDYG GNLEMAKVVA
260 270 280 290 300
RSGVDVFAHN IETTERLTPF VRDRRAKFRQ SLDVLRSAKE AQPELITKTS
310 320 330 340 350
MMLGLGETDE DVWHALRELR ANGVDVVTFG QYMRPTKRHL AVHEYVTPDK
360 370 380 390 400
FELWRQRALD MGFLYCASGP LVRSSYKAGE AFIENVLKKR RLGASAETKV
410
ADLNTPEEAG KAL
Length:413
Mass (Da):45,318
Last modified:May 1, 2013 - v1
Checksum:iBC24E15D1EC82D23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KB445578 Genomic DNA. Translation: EMD90072.1.

Genome annotation databases

EnsemblFungiiEMD90072; EMD90072; COCHEDRAFT_1178395.

Similar proteinsi

Entry informationi

Entry nameiM2UQ93_COCH5
AccessioniPrimary (citable) accession number: M2UQ93
Entry historyiIntegrated into UniProtKB/TrEMBL: May 1, 2013
Last sequence update: May 1, 2013
Last modified: October 25, 2017
This is version 33 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported