Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase

Gene

lipA

Organism
Ruthia magnifica subsp. Calyptogena magnifica
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. Octanoyltransferase (lipB)
  2. Lipoyl synthase (lipA)
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 bindingi62Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi67Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi73Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi88Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi92Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi95Iron-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

BioCyciCRUT413404:G1G7M-555-MONOMER
UniPathwayiUPA00538; UER00593

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-synUniRule annotation
Short name:
LSUniRule annotation
Lipoate synthaseUniRule annotation
Lipoic acid synthaseUniRule annotation
Sulfur insertion protein LipAUniRule annotation
Gene namesi
Name:lipAUniRule annotation
Ordered Locus Names:Rmag_0543
OrganismiRuthia magnifica subsp. Calyptogena magnifica
Taxonomic identifieri413404 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbiontsCandidatus Ruthia
Proteomesi
  • UP000002587 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003253071 – 315Lipoyl synthaseAdd BLAST315

Interactioni

Protein-protein interaction databases

STRINGi413404.Rmag_0543

Structurei

3D structure databases

ProteinModelPortaliA1AWI8
SMRiA1AWI8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G Bacteria
COG0320 LUCA
HOGENOMiHOG000235997
KOiK03644
OMAiPYCDIDF
OrthoDBiPOG091H069D

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
IPR003698 Lipoyl_synth
IPR007197 rSAM
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.

A1AWI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQEIDIKSL KGKSKVVRLK IKPDSERLPI KKPNWIRIKH VASQKVEQLK
60 70 80 90 100
KTLRSQKLFT VCEEAQCPNL SECFNHGAAT FMIMGQICTR RCPFCDVAHG
110 120 130 140 150
KPKALDVDEP KHLANTIKKM QLKYVVITSV DRDDLRDGGA QHFKTCIDNI
160 170 180 190 200
RLSTPKVKIE ILTPDFRGRI DKVLEVFKSC SPNVFNHNLE TVPSLYQKVR
210 220 230 240 250
PGANYNYSLR LLKAFKQQHP FVITKSGLML GVGESEKQVI NVLKDLRKHN
260 270 280 290 300
VDMLTLGQYL QPSKHHLAVE AYIHPNQFDK YKKIALKLGF SQVASGPMVR
310
SSYHADLQIK GELIS
Length:315
Mass (Da):35,868
Last modified:January 23, 2007 - v1
Checksum:iED6FB43F399EF0C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000488 Genomic DNA Translation: ABL02295.1
RefSeqiWP_011737920.1, NC_008610.1

Genome annotation databases

EnsemblBacteriaiABL02295; ABL02295; Rmag_0543
KEGGirma:Rmag_0543

Similar proteinsi

Entry informationi

Entry nameiLIPA_RUTMC
AccessioniPrimary (citable) accession number: A1AWI8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health