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Protein

Lipoyl synthase, mitochondrial

Gene

LIP1

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi33 – 331Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi39 – 391Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi59 – 591Iron-sulfur 2 (4Fe-4S-S-AdoMet)By similarity
Metal bindingi63 – 631Iron-sulfur 2 (4Fe-4S-S-AdoMet)By similarity
Metal bindingi66 – 661Iron-sulfur 2 (4Fe-4S-S-AdoMet)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-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
ProteomesiUP000006906 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 318Lipoyl synthase, mitochondrialPRO_0000398845
Transit peptidei1 – ?MitochondrionSequence Analysis

Interactioni

Protein-protein interaction databases

STRINGi3055.JGI194766.

Structurei

3D structure databases

ProteinModelPortaliA8JGF7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiA8JGF7.
KOiK03644.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
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.
KEGGicre:CHLREDRAFT_194766.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliA8JGF7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.JGI194766.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEDO97051; EDO97051; CHLREDRAFT_194766.
GeneIDi5727843.
KEGGicre:CHLREDRAFT_194766.

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiA8JGF7.
KOiK03644.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The Chlamydomonas genome reveals the evolution of key animal and plant functions."
    Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P.
    , Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.
    Science 318:245-250(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CC-503 and cw92.

Entry informationi

Entry nameiLIAS_CHLRE
AccessioniPrimary (citable) accession number: A8JGF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 4, 2007
Last modified: May 27, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.