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A8I2V9 (LISC_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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, chloroplastic

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoate synthase, plastidial
Short name=LIP1p
Lipoic acid synthase
Gene names
Name:LIP1P
ORF Names:CHLREDRAFT_196092
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii) [Reference proteome]
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length430 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_03129

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_03129

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_03129

Subcellular location

Plastidchloroplast Potential HAMAP-Rule MF_03129.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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 – 4040Chloroplast Potential
Chain41 – 430390Lipoyl synthase, chloroplastic HAMAP-Rule MF_03129
PRO_0000398859

Sites

Metal binding1551Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1601Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1661Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1831Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1871Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1901Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A8I2V9 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 8C549FCC6E98116E

FASTA43046,680
        10         20         30         40         50         60 
MRSLATLHQS PASCSRSAPV APCPARRANS SRRVARQGPR ARASSPVVET ESEDVDITPQ 

        70         80         90        100        110        120 
IDAFEELVRL AVEKDPSLAT LAEQHLRSKS KSAAPVSPFA APSPGSPSAS SMLGPSLGAL 

       130        140        150        160        170        180 
PNQNKPAWLR QRAPQGEIYS GLKDQLRGLK LATVCEEAQC PNIGECWNGE LATATIMLLG 

       190        200        210        220        230        240 
DTCTRGCRFC AVNTARTPPP PDPNEPVNTA TAVASWGVGY VVLTSVDRDD MPDGGSEHFA 

       250        260        270        280        290        300 
ATVRTLKQLR PGILVECLTP DFKGDLDAVR HLARSGLDVY AHNVETVERL QKRVRDPRAG 

       310        320        330        340        350        360 
YMQTLDVLRA AKECGVYTKS SIMLGLGETD DEVIDTMLDL KAVGVDIFTL GQYLQPTPHH 

       370        380        390        400        410        420 
LPVTEFVTPE KFEYWRKFGQ EEIGFRYVAS GPMVRSSYKA GEFFLHSMIE SDRAKARAAQ 

       430 
EGAAGRVRPL 

« 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
DS496112 Genomic DNA. Translation: EDP07358.1.
RefSeqXP_001699662.1. XM_001699610.1.

3D structure databases

ProteinModelPortalA8I2V9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3055.JGI196092.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsEDP07358; EDP07358; CHLREDRAFT_196092.
GeneID5725443.
KEGGcre:CHLREDRAFT_196092.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMARKVDCDI.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03129. Lipoyl_synth_plantC.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027526. Lipoyl_synth_chlpt.
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 nameLISC_CHLRE
AccessionPrimary (citable) accession number: A8I2V9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 4, 2007
Last modified: May 14, 2014
This is version 40 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