Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

ACO22_01519

Organism
Paracoccidioides brasiliensis
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 (ACO22_01535), Octanoyltransferase (GX48_06160)
  2. Lipoyl synthase, mitochondrial (GX48_06141), Lipoyl synthase, mitochondrial (ACO22_01519)
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 bindingi146Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi151Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi157Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi177Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi181Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi184Iron-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:ACO22_01519Imported
OrganismiParacoccidioides brasiliensisImported
Taxonomic identifieri121759 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenales incertae sedisParacoccidioides

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
Domaini167 – 381Elp3InterPro annotationAdd BLAST215

Sequence similaritiesi

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

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.

A0A1D2JLA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASARGLRT LQSAHSSTTV PRLQLAVSRC YATTTSPDPP ITNSSNSSNS
60 70 80 90 100
SNSTPTPKQR ITAFKDKLNA GPSFSDFVSG GGGASNDRVP LDPAEAYALK
110 120 130 140 150
TALVGPPGRK KQIIRLPSWL KTPIPDTPNY RRIKSDLRGL NLHTVCEEAR
160 170 180 190 200
CPNISDCWGG SSKSAATATI MLMGDTCTRG CRFCSVKTSR TPPPLDPHEP
210 220 230 240 250
ENTAEALSRW GLGYVVMTSV DRDDLADGGA RHVVETVRKV KQKAPGILLE
260 270 280 290 300
CLTGDYAGDL EMVALVATSG LDVFAHNVET VEALTPFVRD RRATFQQSLR
310 320 330 340 350
VLKAAKEARP ELITKTSIML GLGETETQLW ETLRALRAVD VDVVTFGQYM
360 370 380 390 400
RPTKRHMAVH EYVRPEVFDL WKERALEMGF LYCASGPLVR SSYKAGEAFI
410 420 430 440 450
ENVLKKRRGE GADGGDGGNS TRLTHHALHE TRDFNKSQSW PFKISPSLLK

LDMQN
Length:455
Mass (Da):49,773
Last modified:November 30, 2016 - v1
Checksum:iB1F820ACD4039BE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LZYO01000038 Genomic DNA. Translation: ODH40762.1.

Genome annotation databases

EnsemblFungiiODH40762; ODH40762; ACO22_01519.

Similar proteinsi

Entry informationi

Entry nameiA0A1D2JLA0_PARBR
AccessioniPrimary (citable) accession number: A0A1D2JLA0
Entry historyiIntegrated into UniProtKB/TrEMBL: November 30, 2016
Last sequence update: November 30, 2016
Last modified: October 25, 2017
This is version 7 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported