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A8JGF7 (LIAS_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LIP1
ORF Names:CHLREDRAFT_194766
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii) [Reference proteome]
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_03128

Catalytic activity

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_03128

Cofactor

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

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_03128

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03128.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 318Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128PRO_0000398845

Sites

Metal binding281Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding331Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding391Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A8JGF7 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 1D7C892346AE7116

FASTA31834,234
        10         20         30         40         50         60 
MKRNKLPGGD KYTEIKAKLR ELKLSTVCEE ARCPNLGECW GGGDGHTATA TIMLMGDTCT 

        70         80         90        100        110        120 
RGCKFCAVKT SKAPPPLDPH EPENVSKAIA AWGLDYVVLT SVDRDDLPDG GAAHIASTIR 

       130        140        150        160        170        180 
LLKQKTEGRL LVEALVPDFQ GDMGGVQTIV EAGLDVYAHN IETVERLQGQ VRDRRAGWAQ 

       190        200        210        220        230        240 
SLATLSAAKR VSGGRLLTKS SIMLGCGESR EEVVDTLKAL RANGVDVVTL GQYMRPTKKH 

       250        260        270        280        290        300 
MAVAEFVTPE AFAAYEQIAK DLGFLYVASG PMVRSSYRAG ELYITNVLKG RRGGEGEGGE 

       310 
GQQQQQGQQQ QQARAATA 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS496184 Genomic DNA. Translation: EDO97051.1.
RefSeqXP_001702321.1. XM_001702269.1.
UniGeneCre.3605.

3D structure databases

ProteinModelPortalA8JGF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3055.JGI194766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsEDO97051; EDO97051; CHLREDRAFT_194766.
GeneID5727843.
KEGGcre:CHLREDRAFT_194766.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIAS_CHLRE
AccessionPrimary (citable) accession number: A8JGF7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 4, 2007
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways