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Protein

Lipoyl synthase, chloroplastic

Gene

LIP1P

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation

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.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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi155 – 1551Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi160 – 1601Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi166 – 1661Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi183 – 1831Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi187 – 1871Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi190 – 1901Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
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, chloroplasticUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoate synthase, plastidialUniRule annotation
Short name:
LIP1pUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
Name:LIP1PUniRule annotation
ORF Names:CHLREDRAFT_196092
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
ProteomesiUP000006906 Componenti: Unassembled WGS sequence

Subcellular locationi

  1. Plastidchloroplast UniRule annotation

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040ChloroplastUniRule annotationAdd
BLAST
Chaini41 – 430390Lipoyl synthase, chloroplasticPRO_0000398859Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi3055.JGI196092.

Structurei

3D structure databases

ProteinModelPortaliA8I2V9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiA8I2V9.
KOiK03644.
OMAiCAVNTAR.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
MF_03129. Lipoyl_synth_plantC.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027526. Lipoyl_synth_chlpt.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
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.

A8I2V9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSLATLHQS PASCSRSAPV APCPARRANS SRRVARQGPR ARASSPVVET
60 70 80 90 100
ESEDVDITPQ IDAFEELVRL AVEKDPSLAT LAEQHLRSKS KSAAPVSPFA
110 120 130 140 150
APSPGSPSAS SMLGPSLGAL PNQNKPAWLR QRAPQGEIYS GLKDQLRGLK
160 170 180 190 200
LATVCEEAQC PNIGECWNGE LATATIMLLG DTCTRGCRFC AVNTARTPPP
210 220 230 240 250
PDPNEPVNTA TAVASWGVGY VVLTSVDRDD MPDGGSEHFA ATVRTLKQLR
260 270 280 290 300
PGILVECLTP DFKGDLDAVR HLARSGLDVY AHNVETVERL QKRVRDPRAG
310 320 330 340 350
YMQTLDVLRA AKECGVYTKS SIMLGLGETD DEVIDTMLDL KAVGVDIFTL
360 370 380 390 400
GQYLQPTPHH LPVTEFVTPE KFEYWRKFGQ EEIGFRYVAS GPMVRSSYKA
410 420 430
GEFFLHSMIE SDRAKARAAQ EGAAGRVRPL
Length:430
Mass (Da):46,680
Last modified:December 4, 2007 - v1
Checksum:i8C549FCC6E98116E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS496112 Genomic DNA. Translation: EDP07358.1.
RefSeqiXP_001699662.1. XM_001699610.1.

Genome annotation databases

EnsemblPlantsiEDP07358; EDP07358; CHLREDRAFT_196092.
GeneIDi5725443.
KEGGicre:CHLREDRAFT_196092.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS496112 Genomic DNA. Translation: EDP07358.1.
RefSeqiXP_001699662.1. XM_001699610.1.

3D structure databases

ProteinModelPortaliA8I2V9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.JGI196092.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEDP07358; EDP07358; CHLREDRAFT_196092.
GeneIDi5725443.
KEGGicre:CHLREDRAFT_196092.

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiA8I2V9.
KOiK03644.
OMAiCAVNTAR.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
MF_03129. Lipoyl_synth_plantC.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027526. Lipoyl_synth_chlpt.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
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 nameiLISC_CHLRE
AccessioniPrimary (citable) accession number: A8I2V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 4, 2007
Last modified: April 1, 2015
This is version 46 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.