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Protein

Lipoyl synthase 2, chloroplastic

Gene

LIP1P-2

Organism
Oryza sativa subsp. indica (Rice)
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 bindingi108 – 1081Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi113 – 1131Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi119 – 1191Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi145 – 1451Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi149 – 1491Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi152 – 1521Iron-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 2, chloroplastic (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthase 2UniRule annotation
Short name:
LS 2UniRule annotation
Short name:
Lip-syn 2UniRule annotation
Lipoate synthase, plastidial 2UniRule annotation
Short name:
LIP1p 2UniRule annotation
Lipoic acid synthase 2UniRule annotation
Gene namesi
Name:LIP1P-2UniRule annotation
ORF Names:OsI_20590
OrganismiOryza sativa subsp. indica (Rice)
Taxonomic identifieri39946 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
ProteomesiUP000007015 Componenti: Chromosome 5

Organism-specific databases

GrameneiB8B016.

Subcellular locationi

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 – 4848ChloroplastUniRule annotationAdd
BLAST
Chaini49 – 384336Lipoyl synthase 2, chloroplasticPRO_0000398865Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi39947.LOC_Os05g43576.1.

Structurei

3D structure databases

ProteinModelPortaliB8B016.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
OMAiPRLYHIR.

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.

B8B016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYCSRVYH HHPVSPSTMQ GSLARPSIHA GSASLTFRAR PNSVSIVRCD
60 70 80 90 100
ADSPPEGSAV AGWAPPGPYT GRDPAARKPA WLRQRAAQGE KYARLRESLG
110 120 130 140 150
ELKLNTVCVE AQCPNIGECW NGGGGAGGDG DGIATATIML LGDTCTRGCR
160 170 180 190 200
FCAVKTSNKP PPPDALEPLR TAVAVASWGV DYVVLTSVDR DDLPDGGSGH
210 220 230 240 250
FAQTVKALKE LKPGILVECL TSDFRGDLEA VSSLASSGLD VFAHNIETVR
260 270 280 290 300
SLQRIVRDPR AAYDQSLAVL KHAKNCKDGM VTKSSIMLGL GETDEEVKQT
310 320 330 340 350
MCDLRAIDVD ILTLGQYLQP TERHLRVREY VTPEKFDFWK EYGESLGFLY
360 370 380
VASGPLVRSS YRAGELFVQN LVRRKKAELA PTLQ
Length:384
Mass (Da):41,545
Last modified:March 3, 2009 - v1
Checksum:i9DA63FA586CDFFA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000130 Genomic DNA. Translation: EEC79513.1.

Genome annotation databases

EnsemblPlantsiBGIOSGA020168-TA; BGIOSGA020168-PA; BGIOSGA020168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000130 Genomic DNA. Translation: EEC79513.1.

3D structure databases

ProteinModelPortaliB8B016.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os05g43576.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiBGIOSGA020168-TA; BGIOSGA020168-PA; BGIOSGA020168.

Organism-specific databases

GrameneiB8B016.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
OMAiPRLYHIR.

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 genomes of Oryza sativa: a history of duplications."
    Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
    , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
    PLoS Biol. 3:266-281(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. 93-11.

Entry informationi

Entry nameiLISC2_ORYSI
AccessioniPrimary (citable) accession number: B8B016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 3, 2009
Last modified: April 1, 2015
This is version 36 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.