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Protein

Lipoyl synthase, mitochondrial

Gene

LIP1

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
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.By similarity

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] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.By similarity

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. no protein annotated in this organism
  2. Lipoyl synthase, chloroplastic (LIP1P), Lipoyl synthase, mitochondrial (CHLRE_08g359700v5), Lipoyl synthase, mitochondrial (LIP1), Lipoyl synthase, chloroplastic (LIP1P)
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 bindingi28Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi33Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi39Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi59Iron-sulfur 2 (4Fe-4S-S-AdoMet)By similarity1
Metal bindingi63Iron-sulfur 2 (4Fe-4S-S-AdoMet)By similarity1
Metal bindingi66Iron-sulfur 2 (4Fe-4S-S-AdoMet)By similarity1

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
Name:LIP1
ORF Names:CHLREDRAFT_194766
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000398845? – 318Lipoyl synthase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

PaxDbiA8JGF7

Interactioni

Protein-protein interaction databases

STRINGi3055.EDO97051

Structurei

3D structure databases

ProteinModelPortaliA8JGF7
SMRiA8JGF7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
InParanoidiA8JGF7
KOiK03644

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.

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

A8JGF7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRNKLPGGD KYTEIKAKLR ELKLSTVCEE ARCPNLGECW GGGDGHTATA
60 70 80 90 100
TIMLMGDTCT RGCKFCAVKT SKAPPPLDPH EPENVSKAIA AWGLDYVVLT
110 120 130 140 150
SVDRDDLPDG GAAHIASTIR LLKQKTEGRL LVEALVPDFQ GDMGGVQTIV
160 170 180 190 200
EAGLDVYAHN IETVERLQGQ VRDRRAGWAQ SLATLSAAKR VSGGRLLTKS
210 220 230 240 250
SIMLGCGESR EEVVDTLKAL RANGVDVVTL GQYMRPTKKH MAVAEFVTPE
260 270 280 290 300
AFAAYEQIAK DLGFLYVASG PMVRSSYRAG ELYITNVLKG RRGGEGEGGE
310
GQQQQQGQQQ QQARAATA
Length:318
Mass (Da):34,234
Last modified:December 4, 2007 - v1
Checksum:i1D7C892346AE7116
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS496184 Genomic DNA Translation: EDO97051.1
RefSeqiXP_001702321.1, XM_001702269.1
UniGeneiCre.3605

Genome annotation databases

EnsemblPlantsiEDO97051; EDO97051; CHLREDRAFT_194766
GeneIDi5727843
GrameneiEDO97051; EDO97051; CHLREDRAFT_194766
KEGGicre:CHLREDRAFT_194766

Similar proteinsi

Entry informationi

Entry nameiLIAS_CHLRE
AccessioniPrimary (citable) accession number: A8JGF7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 4, 2007
Last modified: April 25, 2018
This is version 60 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health