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Protein

Lipoyl synthase

Gene

lipA

Organism
Anaplasma marginale (strain St. Maries)
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 bindingi34Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi39Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi45Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi60Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi64Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi67Iron-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

BioCyciAMAR234826:G1G47-620-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:AM820
OrganismiAnaplasma marginale (strain St. Maries)
Taxonomic identifieri234826 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003252281 – 295Lipoyl synthaseAdd BLAST295

Structurei

3D structure databases

ProteinModelPortaliQ5PAD4
SMRiQ5PAD4
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

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.

Q5PAD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENKPDWLRV RMPGGAVFDE VTELVRRYEL NTVCEEAACP NIGECWNKRH
60 70 80 90 100
ATIMIMGSVC TRACAFCNVK VGVPNALDPD EPERVGAAIS KLGLKHVVIT
110 120 130 140 150
SVDRDDLPDG GASHFAKCVR EIRKRDSSVT VEILTPDFLG KPCAIDIIAS
160 170 180 190 200
ARPDVYNHNL ETVPRLYSRV RPRAKYFNSL NLLKEVKDKS PGVFTKSGFM
210 220 230 240 250
LGLGESKEEV YQVMDDLRCA GVDFIVMGQY LQPTKNNIEV HRYVPPSEFE
260 270 280 290
QYKLMAYAKG FSMVAASPLA RSSYHAEDDF RKLKELRFAR AKVNE
Length:295
Mass (Da):33,168
Last modified:March 18, 2008 - v2
Checksum:i505E239CD512822D
GO

Sequence cautioni

The sequence AAV86746 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000030 Genomic DNA Translation: AAV86746.1 Different initiation.
RefSeqiWP_029209728.1, NZ_AFMU01000051.1

Genome annotation databases

EnsemblBacteriaiAAV86746; AAV86746; AM820
GeneIDi7398251
KEGGiama:AM820
PATRICifig|320483.3.peg.703

Similar proteinsi

Entry informationi

Entry nameiLIPA_ANAMM
AccessioniPrimary (citable) accession number: Q5PAD4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: May 23, 2018
This is version 84 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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