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Protein

Lipoyl synthase

Gene

lipA

Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
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 bindingi68Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi73Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi79Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi94Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi98Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi101Iron-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:EcolC_3017
OrganismiEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Taxonomic identifieri481805 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000779551 – 321Lipoyl synthaseAdd BLAST321

Structurei

3D structure databases

ProteinModelPortaliB1IYI0
SMRiB1IYI0
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

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.

B1IYI0-1 [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 29, 2008 - v1
Checksum:iBE7BF32A4E3AA358
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000946 Genomic DNA Translation: ACA78642.1
RefSeqiWP_000042632.1, NC_010468.1

Genome annotation databases

EnsemblBacteriaiACA78642; ACA78642; EcolC_3017
KEGGiecl:EcolC_3017

Similar proteinsi

Entry informationi

Entry nameiLIPA_ECOLC
AccessioniPrimary (citable) accession number: B1IYI0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 29, 2008
Last modified: May 23, 2018
This is version 60 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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