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
Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1)
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 bindingi64Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi69Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi75Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi90Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi94Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi97Iron-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 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:Mrad2831_2176
OrganismiMethylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1)
Taxonomic identifieri426355 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
Proteomesi

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000996131 – 327Lipoyl synthaseAdd BLAST327

Interactioni

Protein-protein interaction databases

STRINGi426355.Mrad2831_2176

Structurei

3D structure databases

ProteinModelPortaliB1LWN4
SMRiB1LWN4
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.

B1LWN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVVLDTLKN DPRPVRLRHP EKAHRPDQPV QAKKPDWIRV KAPGSRAWSE
60 70 80 90 100
TQKIVREHGL VTVCEEAGCP NIGECWEKRH ATFMIMGDTC TRACAFCNVR
110 120 130 140 150
TGLPDALDLG EPDKIADSVA KLGLHHVVIT SVDRDDLRDG GAEHFARTIA
160 170 180 190 200
AIRRASPGTT VEILTPDFLR KDGALEVVVA AKPDVFNHNL ETVPAKYLTV
210 220 230 240 250
RPGARYFHSV RLLQRVKELD PAIFTKSGIM VGLGEERNEV LQLMDDLRSA
260 270 280 290 300
DVDFLTIGQY LQPSKKHHEV VRFVPPDEFK AYETTAYAKG FLLVSATPLT
310 320
RSSHHAGEDF ARLQAARLAK LSPALSA
Length:327
Mass (Da):36,245
Last modified:April 29, 2008 - v1
Checksum:iAA09B4FF34385F53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001001 Genomic DNA Translation: ACB24171.1
RefSeqiWP_012319150.1, NC_010505.1

Genome annotation databases

EnsemblBacteriaiACB24171; ACB24171; Mrad2831_2176
GeneIDi6138208
KEGGimrd:Mrad2831_2176

Entry informationi

Entry nameiLIPA_METRJ
AccessioniPrimary (citable) accession number: B1LWN4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: May 23, 2018
This is version 61 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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