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Protein

Lipoyl synthase

Gene

lipA

Organism
Macrococcus caseolyticus (strain JCSC5402)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 + 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.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 the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation 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 pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi41Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi46Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi52Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi68Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi72Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi75Iron-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

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:MCCL_0553
OrganismiMacrococcus caseolyticus (strain JCSC5402)
Taxonomic identifieri458233 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeMacrococcus
Proteomesi
  • UP000001383 Componenti: Chromosome

Subcellular locationi

B9EAJ9:
  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001246371 – 304Lipoyl synthaseAdd BLAST304

Interactioni

Protein-protein interaction databases

STRINGi458233.MCCL_0553.

Structurei

3D structure databases

ProteinModelPortaliB9EAJ9.
SMRiB9EAJ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235998.
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.
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.

B9EAJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKNEEILR KPEWLKIKLN TNKSYTGLKK MMREHNLNTV CEEAKCPNIH
60 70 80 90 100
ECWGERKTAT IMILGAICTR ACRFCAVKTG LPNELDLNEP ERVAESVRLM
110 120 130 140 150
NLKHVVITAV ARDDLKDGGA HVYAETIRKV REVNPYTTIE VLPSDMGGSI
160 170 180 190 200
ENWETLMAAK PDILNHNIET VRRLTPRVRA RATYDRSLEV LRRSKELYPD
210 220 230 240 250
IPTKSSLMVG LGETTEEIYE VMDDLRANDV DIMTIGQYLQ PSRKHLKVQK
260 270 280 290 300
YYTPLEFGKL RKVAMEKGFK HCQAGPMVRS SYHADEQVNE AAKEKHRLGE

LSSK
Length:304
Mass (Da):34,754
Last modified:March 24, 2009 - v1
Checksum:i865505AFB68C2ED5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009484 Genomic DNA. Translation: BAH17260.1.
RefSeqiWP_012656461.1. NC_011999.1.

Genome annotation databases

EnsemblBacteriaiBAH17260; BAH17260; MCCL_0553.
KEGGimcl:MCCL_0553.

Similar proteinsi

Entry informationi

Entry nameiLIPA_MACCJ
AccessioniPrimary (citable) accession number: B9EAJ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: October 25, 2017
This is version 59 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