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Protein

Lipoyl synthase, mitochondrial

Gene

BRAFLDRAFT_125969

Organism
Branchiostoma floridae (Florida lancelet) (Amphioxus)
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 (BRAFLDRAFT_125969)
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 bindingi102Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi107Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi113Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi133Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi137Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi140Iron-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, 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
ORF Names:BRAFLDRAFT_125969
OrganismiBranchiostoma floridae (Florida lancelet) (Amphioxus)
Taxonomic identifieri7739 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCephalochordataBranchiostomidaeBranchiostoma
Proteomesi
  • UP000001554 Componenti: Partially assembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003982131 – 376Lipoyl synthase, mitochondrialAdd BLAST376

Interactioni

Protein-protein interaction databases

STRINGi7739.JGI125969

Structurei

3D structure databases

ProteinModelPortaliC3Y3G4
SMRiC3Y3G4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
InParanoidiC3Y3G4
KOiK03644
OMAiPYCDIDF

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00206 Lipoyl_synth, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR031691 LIAS_N
IPR003698 Lipoyl_synth
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.

C3Y3G4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATCLLMSTF TFIRCSVLKW GSGSSLPQEQ KEKITKGPGL GDFISGEVES
60 70 80 90 100
TDSWEDYMGK LRLEKGDKRL RLPPWLKKEI PIGKNYHSLK GTLRELNLAT
110 120 130 140 150
VCEEAKCPNI GECWGGGEDK TATATIMVMG DTCTRGCRFC SVKTARSPPP
160 170 180 190 200
LDPNEPVHTA EAISRWGVDY IVITSVDRDD VADGGSAHFS ECVKEIKKRI
210 220 230 240 250
PSMLVECLTP DFRGDMEAVA TVAQSGLDVF AHNIETVKRL TPFVRDPRAK
260 270 280 290 300
YDQSLQVLSH VKKTVPDMVT KSSIMLGLGE TDQEVRTAME DLRRAGVDCL
310 320 330 340 350
TLGQYMQPTK RHLKVQEYVT PTKFKHWEEV GGEMGFAYTA SGPLVRSSYR
360 370
AGEFYIKNLL NKKRTEATLD TSSQES
Length:376
Mass (Da):41,818
Last modified:July 28, 2009 - v1
Checksum:i9B44DD05AF6265F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG666483 Genomic DNA Translation: EEN65231.1
RefSeqiXP_002609221.1, XM_002609175.1
UniGeneiBfl.339

Genome annotation databases

GeneIDi7219245
KEGGibfo:BRAFLDRAFT_125969

Similar proteinsi

Entry informationi

Entry nameiLIAS_BRAFL
AccessioniPrimary (citable) accession number: C3Y3G4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: May 23, 2018
This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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