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Protein

Lipoyl synthase 2, chloroplastic

Gene

LIP1P-2

Organism
Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
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

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 1, chloroplastic (LIP1P-1), Lipoyl synthase, chloroplastic (LIP1P), Lipoyl synthase, chloroplastic (LIP1P), Lipoyl synthase, chloroplastic (LIP1P), Lipoyl synthase, mitochondrial (LIP1), Lipoyl synthase, mitochondrial (LIP1), Lipoyl synthase, mitochondrial (POPTR_0005s08840g), Lipoyl synthase, mitochondrial (POPTR_005G086200v3), Lipoyl synthase, mitochondrial (POPTR_0005s08840g), Lipoyl synthase, mitochondrial (LIP1), Lipoyl synthase 2, chloroplastic (LIP1P-2), Lipoyl synthase, mitochondrial (POPTR_0007s06900g)
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 bindingi128Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi133Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi139Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi159Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi163Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi166Iron-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 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:POPTR_0019s13380g
OrganismiPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Taxonomic identifieri3694 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus
Proteomesi
  • UP000006729 Componentsi: Chromosome 19, Linkage group LGXIX, 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
Transit peptidei1 – 35ChloroplastUniRule annotationAdd BLAST35
ChainiPRO_000039886836 – 397Lipoyl synthase 2, chloroplasticAdd BLAST362

Interactioni

Protein-protein interaction databases

STRINGi3694.POPTR_0019s13380.1

Structurei

3D structure databases

ProteinModelPortaliB9N2B0
SMRiB9N2B0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
HOGENOMiHOG000235998
InParanoidiB9N2B0
KOiK03644
OMAiDSSENAM
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
IPR031691 LIAS_N
IPR003698 Lipoyl_synth
IPR027526 Lipoyl_synth_chlpt
IPR007197 rSAM
PANTHERiPTHR10949:SF14 PTHR10949:SF14, 1 hit
PfamiView protein in Pfam
PF16881 LIAS_N, 1 hit
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

B9N2B0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEQSLSKPS FSLSIPIPKA PKSKSSFFCS YSKIRCESVD YPSLTKIDAK
60 70 80 90 100
HPQNSTTINN GSSSSASVDL KNNEKGPYPY PGGGKMGPYT GRDLNEKKPE
110 120 130 140 150
WLRQRAPQGE RFEEVKESIS RLNLNTVCQE AQCPNIGECW NGGGDGIATA
160 170 180 190 200
TIMVLGDTCT RGCRFCAVKT SRTPPPPDPM EPLNTALAIA SWGVDYIVIT
210 220 230 240 250
SVDRDDLSDG GSGHFAQTVR AMKELKPEIM VECLTSDFRG DLKAVDTLVH
260 270 280 290 300
SGLDVFAHNV ETVKRLQRIV RDPRAGYEQS LSVLKHAKVS KKGMITKTSI
310 320 330 340 350
MLGLGETDDE VKEAMTDLRA IDVDILTFGQ YLQPTPLHLT VKEYVSPEKF
360 370 380 390
AYWKEYGESI GFRYVASGPL VRSSYRAGEL FVKTMVKESA KEAAAIS
Length:397
Mass (Da):43,638
Last modified:March 24, 2009 - v1
Checksum:iFC77A8FC05480DA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000355 Genomic DNA Translation: ERP49380.1
RefSeqiXP_006371583.1, XM_006371521.1

Genome annotation databases

EnsemblPlantsiPOPTR_0019s13380.1; POPTR_0019s13380.1; POPTR_0019s13380
GeneIDi18108579
GrameneiPOPTR_0019s13380.1; POPTR_0019s13380.1; POPTR_0019s13380
KEGGipop:POPTR_0019s13380g

Similar proteinsi

Entry informationi

Entry nameiLISC2_POPTR
AccessioniPrimary (citable) accession number: B9N2B0
Secondary accession number(s): U5FF64
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 24, 2009
Last modified: May 23, 2018
This is version 63 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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