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

CAGL0I10923g

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
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.

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. Octanoyltransferase (CAGL0G08404g)
  2. Lipoyl synthase, mitochondrial (CAGL0I10923g)
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 bindingi120Iron-sulfur 1 (4Fe-4S)1
Metal bindingi125Iron-sulfur 1 (4Fe-4S)1
Metal bindingi131Iron-sulfur 1 (4Fe-4S)1
Metal bindingi151Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi155Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi158Iron-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
Ordered Locus Names:CAGL0I10923g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
Proteomesi
  • UP000002428 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:CAGL0I10923g.

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 – 18MitochondrionAdd BLAST18
ChainiPRO_000039826019 – 388Lipoyl synthase, mitochondrialAdd BLAST370

Interactioni

Protein-protein interaction databases

STRINGi284593.XP_447714.1.

Structurei

3D structure databases

ProteinModelPortaliQ6FPY0.
SMRiQ6FPY0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
InParanoidiQ6FPY0.
KOiK03644.
OMAiPYCDIDF.
OrthoDBiEOG092C13O2.

Family and domain databases

Gene3Di3.80.30.20. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiView protein in InterPro
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6FPY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLTTVQRRF LVSTKAKVSG ASISSTANTG SASAGAPNGQ TRRRRRITEF
60 70 80 90 100
KDALNLGPSF EDFVSGRAAG FTVVDPLEQM RQDREEYKKL PKWLKVPIPK
110 120 130 140 150
GVNYHKLKKD VKELKLSTVC EEARCPNIGE CWGGKDKSKA TATIMLLGDT
160 170 180 190 200
CTRGCRFCSV KTNRNPAKPD PTEPENTAEA ISRWGLGYVV LTTVDRDDLP
210 220 230 240 250
DGGAHHLAET VIKIKQKAPK TLVEALTGDF LGNLEMVDVM AKSGLDVYAH
260 270 280 290 300
NLETVEALTP HVRDRRAGYR QSLNVLKRAK ETVPSLITKT SVMLGLGETD
310 320 330 340 350
DQIIQTMQDL RAINCDVITF GQYMRPTKRH MKVVEYVRPE KFDYWKDKAK
360 370 380
EMGFLYCASG PLVRSSYKAG EAFIENVLNK RKQDNKRI
Length:388
Mass (Da):43,401
Last modified:July 19, 2004 - v1
Checksum:i457598F13CF7B740
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380955 Genomic DNA. Translation: CAG60659.1.
RefSeqiXP_447714.1. XM_447714.1.

Genome annotation databases

EnsemblFungiiCAG60659; CAG60659; CAGL0I10923g.
GeneIDi2889354.
KEGGicgr:CAGL0I10923g.

Similar proteinsi

Entry informationi

Entry nameiLIPA_CANGA
AccessioniPrimary (citable) accession number: Q6FPY0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 19, 2004
Last modified: October 25, 2017
This is version 94 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