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Protein

Lipoyl synthase

Gene

lipA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Free octanoate is not a substrate for LipA.3 Publications

Miscellaneous

The source of sulfurs is the LipA protein itself, most likely one 4Fe-4S cluster.

Catalytic activityi

Protein N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.1 Publication

Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.1 Publication

Enzyme regulationi

Inhibited by the AdoMet analog S-adenosyl homocysteine.

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].1 Publication
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 bindingi68Iron-sulfur 1 (4Fe-4S)1
Metal bindingi73Iron-sulfur 1 (4Fe-4S)1
Metal bindingi79Iron-sulfur 1 (4Fe-4S)1
Metal bindingi94Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi98Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi101Iron-sulfur 2 (4Fe-4S-S-AdoMet)1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoliWiki
  • alpha-ketoacid dehydrogenase activity Source: CACAO
  • lipoate synthase activity Source: EcoliWiki
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • lipoate biosynthetic process Source: EcoliWiki
  • protein lipoylation Source: EcoliWiki

Keywordsi

Molecular functionTransferase
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:EG11306-MONOMER.
MetaCyc:EG11306-MONOMER.
UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase (EC:2.8.1.81 Publication)
Alternative name(s):
Lip-syn
Short name:
LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene namesi
Name:lipA
Synonyms:lip
Ordered Locus Names:b0628, JW0623
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11306. lipA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi68 – 79CEEAS…NLAEC → AEEASAPNLAEA: Loss of 1 4Fe-4S cluster binding. Loss of activity. 1 PublicationAdd BLAST12
Mutagenesisi94 – 101CTRRCPFC → ATRRAPFA: Loss of 1 4Fe-4S cluster binding. Loss of activity. 1 Publication8

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001023131 – 321Lipoyl synthaseAdd BLAST321

Proteomic databases

PaxDbiP60716.
PRIDEiP60716.

Interactioni

Subunit structurei

Monomer or homodimer.

Protein-protein interaction databases

BioGridi4260638. 29 interactors.
DIPiDIP-48008N.
IntActiP60716. 13 interactors.
MINTiMINT-1310776.
STRINGi316385.ECDH10B_0697.

Structurei

3D structure databases

ProteinModelPortaliP60716.
SMRiP60716.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235997.
InParanoidiP60716.
KOiK03644.
PhylomeDBiP60716.

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.

P60716-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKPIVMERG VKYRDADKMA LIPVKNVATE REALLRKPEW MKIKLPADST
60 70 80 90 100
RIQGIKAAMR KNGLHSVCEE ASCPNLAECF NHGTATFMIL GAICTRRCPF
110 120 130 140 150
CDVAHGRPVA PDANEPVKLA QTIADMALRY VVITSVDRDD LRDGGAQHFA
160 170 180 190 200
DCITAIREKS PQIKIETLVP DFRGRMDRAL DILTATPPDV FNHNLENVPR
210 220 230 240 250
IYRQVRPGAD YNWSLKLLER FKEAHPEIPT KSGLMVGLGE TNEEIIEVMR
260 270 280 290 300
DLRRHGVTML TLGQYLQPSR HHLPVQRYVS PDEFDEMKAE ALAMGFTHAA
310 320
CGPFVRSSYH ADLQAKGMEV K
Length:321
Mass (Da):36,072
Last modified:April 13, 2004 - v1
Checksum:iBE7BF32A4E3AA358
GO

Sequence cautioni

The sequence AAA24072 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35L → V (PubMed:1577793).Curated1
Sequence conflicti35L → V (PubMed:8444795).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M82805 Genomic DNA. Translation: AAA24072.1. Different initiation.
L07636 Genomic DNA. Translation: AAA66345.1.
U82598 Genomic DNA. Translation: AAB40828.1.
U00096 Genomic DNA. Translation: AAC73729.1.
AP009048 Genomic DNA. Translation: BAA35271.1.
PIRiB64797.
RefSeqiNP_415161.1. NC_000913.3.
WP_000042632.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73729; AAC73729; b0628.
BAA35271; BAA35271; BAA35271.
GeneIDi945227.
KEGGiecj:JW0623.
eco:b0628.
PATRICifig|1411691.4.peg.1640.

Similar proteinsi

Entry informationi

Entry nameiLIPA_ECOLI
AccessioniPrimary (citable) accession number: P60716
Secondary accession number(s): P25845, P77595
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: August 30, 2017
This is version 119 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families