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Protein

Lipoyl synthase, mitochondrial

Gene

LIP1

Organism
Vitis vinifera (Grape)
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, mitochondrial (VIT_00s0445g00020), Lipoyl synthase, mitochondrial (LIP1), Lipoyl synthase, chloroplastic (LIP1P)
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 bindingi115Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi120Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi126Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi146Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi150Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi153Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

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, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
Name:LIP1UniRule annotation
ORF Names:VITISV_021769
OrganismiVitis vinifera (Grape)
Taxonomic identifieri29760 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeVitis

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

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003988571 – 393Lipoyl synthase, mitochondrialAdd BLAST393

Proteomic databases

PRIDEiA5CB81

Structurei

3D structure databases

ProteinModelPortaliA5CB81
SMRiA5CB81
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
KOiK03644

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00206 Lipoyl_synth, 1 hit
MF_03128 Lipoyl_synth_plantM, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR031691 LIAS_N
IPR003698 Lipoyl_synth
IPR027527 Lipoyl_synth_mt
IPR007197 rSAM
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.

A5CB81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYTRLSSLAL RHHRHNHNNS VLLLSSLISL RHCSSPPTNP EPPQTLASLR
60 70 80 90 100
HRLAVESPSL SDFVRLQTSD DYSVEVGTKK KPLSKPKWMK ESIPGGAKYT
110 120 130 140 150
QIKKKLRQLN LHTVCEEARC PNMGECWSGG ETGTATATIM ILGDTCTRGC
160 170 180 190 200
RFCNVKTSRT PPPPDPDEPS KVAEAIASWG LDYVVITSVD RDDLPDQGSG
210 220 230 240 250
HFAETVQKLK ILKPNMLIEA LVPDFRGDPG CVEKVSKSGL DVFAHNIETV
260 270 280 290 300
EELQSAVRDH RANFKQSLEV LKLAKEYADA GTLTKTSIML GCGETPDQVV
310 320 330 340 350
RTMEKVRAAG VDVMTFGQYM RPSKRHMPVS EYITPEAFEK YRILGMDMGF
360 370 380 390
RYVASGPMVR SSYKAGEFYI KSMIDADRAM SWASSSPSPL PAA
Length:393
Mass (Da):43,477
Last modified:June 12, 2007 - v1
Checksum:i18F30ED79ECD49A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM488835 Genomic DNA Translation: CAN73265.1
RefSeqiXP_002266132.2, XM_002266096.4
UniGeneiVvi.610

Genome annotation databases

GeneIDi100251365
KEGGivvi:100251365

Similar proteinsi

Entry informationi

Entry nameiLIAS_VITVI
AccessioniPrimary (citable) accession number: A5CB81
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 12, 2007
Last modified: May 23, 2018
This is version 57 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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