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Protein

Lipoyl synthase, mitochondrial

Gene

lip5

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.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. Probable octanoyltransferase (SPAC4F10.05c)
  2. Lipoyl synthase, mitochondrial (lip5)
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 bindingi100Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi105Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi111Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi131Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi135Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi138Iron-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

ReactomeiR-SPO-389661 Glyoxylate metabolism and glycine degradation
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
Name:lip5
ORF Names:pi050, SPBC8D2.15
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC8D2.15
PomBaseiSPBC8D2.15 lip5

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
ChainiPRO_00000177251 – 370Lipoyl synthase, mitochondrialAdd BLAST370

Proteomic databases

MaxQBiO13642
PaxDbiO13642
PRIDEiO13642

Interactioni

Protein-protein interaction databases

STRINGi4896.SPBC8D2.15.1

Structurei

3D structure databases

ProteinModelPortaliO13642
SMRiO13642
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000235998
InParanoidiO13642
KOiK03644
OMAiPYCDIDF
OrthoDBiEOG092C13O2
PhylomeDBiO13642

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.

O13642-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKIGRNATI LKNNFWFASV RFQSGGFSEK LAKGPSFADF LNMDKPLTAD
60 70 80 90 100
EAFELDRKVE LPNGSIHKRL PSWLKTKVPL GTNFNRIKHD LRGSHLHTVC
110 120 130 140 150
EEAKCPNIGE CWGGKDKSRA TATIMLMGDT CTRGCRFCSV KTSRRPGPLD
160 170 180 190 200
PNEPENTAEA IKQWNLGYIV LTSVDRDDLT DLGANHIAKT IQKIKEKAPH
210 220 230 240 250
ILVEALTPDF SGRMDLVEIV AKSGLDVFAH NVETVEELTP FVRDRRATYR
260 270 280 290 300
QSLSVLKHVK KTCPHLITKT SIMLGLGETD AEILTTLKDL LEHNVDVVTF
310 320 330 340 350
GQYMRPTKRH LKVQEYVHPK KFEYWKEVAE KLGFLYVASG PLVRSSYKAG
360 370
EYFMENLIKK RSGNPASMSV
Length:370
Mass (Da):41,690
Last modified:November 1, 1998 - v2
Checksum:i8A43CFE109D68197
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA Translation: CAA17830.1
AB004537 Genomic DNA Translation: BAA21430.1
AB004538 Genomic DNA Translation: BAA21431.1
PIRiT40760
RefSeqiNP_595577.1, NM_001021472.2

Genome annotation databases

EnsemblFungiiSPBC8D2.15.1; SPBC8D2.15.1:pep; SPBC8D2.15
KEGGispo:SPBC8D2.15

Similar proteinsi

Entry informationi

Entry nameiLIPA_SCHPO
AccessioniPrimary (citable) accession number: O13642
Secondary accession number(s): O13643
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 138 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health