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Protein

Lipoyl synthase, chloroplastic

Gene

LIP1P

Organism
Sorghum bicolor (Sorghum) (Sorghum vulgare)
Status
Reviewed-Annotation score: -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

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.UniRule annotation

Catalytic activityi

Protein N6-(octanoyl)lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Lipoyl synthase, chloroplastic (LIP1P), Lipoyl synthase, mitochondrial (LIP1)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi94Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi99Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi105Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi131Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi135Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi138Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Ligand4Fe-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
Ordered Locus Names:Sb03g035760
OrganismiSorghum bicolor (Sorghum) (Sorghum vulgare)
Taxonomic identifieri4558 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeSorghinaeSorghum
Proteomesi
  • UP000000768 Componentsi: Chromosome 3, Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003988701 – 368Lipoyl synthase, chloroplasticAdd BLAST368

Proteomic databases

PRIDEiC5XKZ1

Interactioni

Protein-protein interaction databases

STRINGi4558.Sb03g035760.1

Structurei

3D structure databases

ProteinModelPortaliC5XKZ1
SMRiC5XKZ1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
InParanoidiC5XKZ1
KOiK03644
OMAiPYCDIDF
OrthoDBiEOG093604CP

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00206 Lipoyl_synth, 1 hit
MF_03129 Lipoyl_synth_plantC, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR003698 Lipoyl_synth
IPR027526 Lipoyl_synth_chlpt
IPR007197 rSAM
PANTHERiPTHR10949:SF14 PTHR10949:SF14, 1 hit
PfamiView protein in Pfam
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF005963 Lipoyl_synth, 1 hit
SFLDiSFLDG01058 lipoyl_synthase_like, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

C5XKZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSSLARPLR PPVLAGCGGR RGHGAPRGSV SVARCRAEAA PPTVGTASRA
60 70 80 90 100
PAGPYTGRDP EVKKPAWLRQ RAAQGDKYAR LRESIGELKL NTVCVEAQCP
110 120 130 140 150
NIGECWNGGG GAGGEGDGIA TATIMVLGDT CTRGCRFCAV KTSNKPPPPD
160 170 180 190 200
PLEPLNTALA VASWGVDYVV LTSVDRDDLP DGGSSHFAQT VRALKELKPG
210 220 230 240 250
ILVECLTSDF RGDLEAVSSL ANSGLDVYAH NIETVRSLQR IVRDPRAGYD
260 270 280 290 300
QSLAVLKHAK DCREGMITKS SIMLGLGETD EEVKQAMIDL RAIGVDILTL
310 320 330 340 350
GQYLQPTERH LTVREYVTPE KFQFWKEYGE SVGFRYVASG PLVRSSYRAG
360
ELFVQNLVRN NKTGSSSS
Length:368
Mass (Da):39,528
Last modified:September 1, 2009 - v1
Checksum:iB63753E5085C935C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000762 Genomic DNA Translation: EES01528.1
RefSeqiXP_002456408.1, XM_002456363.1

Genome annotation databases

EnsemblPlantsiEES01528; EES01528; SORBI_3003G309300
GeneIDi8072124
GrameneiEES01528; EES01528; SORBI_3003G309300
KEGGisbi:8072124

Similar proteinsi

Entry informationi

Entry nameiLISC_SORBI
AccessioniPrimary (citable) accession number: C5XKZ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 1, 2009
Last modified: May 23, 2018
This is version 52 of the entry and version 1 of the sequence. See 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
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