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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: 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

Pathway:iprotein 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, mitochondrial (LIP1), Lipoyl synthase, mitochondrial (LIP1), Lipoyl synthase 2, chloroplastic (LIP1P-2)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi133 – 1331Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi139 – 1391Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi159 – 1591Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi166 – 1661Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

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:POPTR_0019s13380g
OrganismiPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Taxonomic identifieri3694 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus
ProteomesiUP000006729 Componentsi: Linkage group LGXIX, Unassembled WGS sequence

Subcellular locationi

  • Plastidchloroplast UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535ChloroplastUniRule annotationAdd
BLAST
Chaini36 – 397362Lipoyl synthase 2, chloroplasticPRO_0000398868Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi3694.POPTR_0019s13380.1.

Structurei

3D structure databases

ProteinModelPortaliB9N2B0.
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.
InParanoidiB9N2B0.
KOiK03644.
OMAiAEPREAC.

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.

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.
KEGGipop:POPTR_0019s13380g.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliB9N2B0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3694.POPTR_0019s13380.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiB9N2B0.
KOiK03644.
OMAiAEPREAC.

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

« Hide 'large scale' publications
  1. "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."
    Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W., Brun A.
    , Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.
    Science 313:1596-1604(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Nisqually.
  2. Cited for: GENOME REANNOTATION.
    Strain: cv. Nisqually.

Entry informationi

Entry nameiLISC2_POPTR
AccessioniPrimary (citable) accession number: B9N2B0
Secondary accession number(s): U5FF64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 24, 2009
Last modified: July 22, 2015
This is version 50 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.