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Protein

Lipoyl synthase

Gene

lipA

Organism
Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
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 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 bindingi55Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi60Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi66Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi81Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi85Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi88Iron-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:Bcav_1858
OrganismiBeutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
Taxonomic identifieri471853 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesBeutenbergiaceaeBeutenbergia
Proteomesi
  • UP000007962 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002041431 – 332Lipoyl synthaseAdd BLAST332

Interactioni

Protein-protein interaction databases

STRINGi471853.Bcav_1858.

Structurei

3D structure databases

ProteinModelPortaliC5C4Y6.
SMRiC5C4Y6.
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.
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.
SMARTiView protein in SMART
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

C5C4Y6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIAPEGRRL LRVEARNAAV PIEKKPPWIK TRATMGPEYT ELRSLVRREG
60 70 80 90 100
LHTVCEEAGC PNIFECWEDR EATFLIGGDQ CTRRCDFCQI DTGKPADFDA
110 120 130 140 150
DEPRRVAESV QAMGLRYSTV TGVARDDLAD GGAWLYAETV RQIHALNPGT
160 170 180 190 200
GVELLIPDFN AEPDQLAEVF SSRPEVLAHN LETVPRVFKR IRPGFRYARS
210 220 230 240 250
LSVLTAARDA GLVTKSNLIL GMGETTAEAV EALADLHAAG CDLVTITQYL
260 270 280 290 300
RPSPRHHPVE RWVKPEEFVE LSDEAERIGF LGVMAGPLVR SSYRAGRLWG
310 320 330
QAMARRGLEV PPALAHLTEP TTSRQEAASL LR
Length:332
Mass (Da):36,752
Last modified:July 28, 2009 - v1
Checksum:i8CF73DE278E01168
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001618 Genomic DNA. Translation: ACQ80114.1.
RefSeqiWP_015882354.1. NC_012669.1.

Genome annotation databases

EnsemblBacteriaiACQ80114; ACQ80114; Bcav_1858.
KEGGibcv:Bcav_1858.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiLIPA_BEUC1
AccessioniPrimary (citable) accession number: C5C4Y6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: June 7, 2017
This is version 56 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