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Protein

Lipoyl synthase

Gene

lipA

Organism
Chlamydia muridarum (strain MoPn / Nigg)
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. no protein annotated in this organism
  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 bindingi48Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi53Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi59Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi74Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi78Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi81Iron-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:TC_0847
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000800 Componenti: Chromosome

Subcellular locationi

Q9PJI2:
  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001023031 – 308Lipoyl synthaseAdd BLAST308

Interactioni

Protein-protein interaction databases

STRINGi243161.CmurN_010100004363.

Structurei

3D structure databases

ProteinModelPortaliQ9PJI2.
SMRiQ9PJI2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
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.

Q9PJI2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSPESSTP KQSIPARFPK WLRQKLPLGK VFSRTDGTIK NKGLPTVCEE
60 70 80 90 100
ASCPNRTHCW SRHTATYLAL GDACTRRCGF CDIDFTKKPL PPDPQEGEKI
110 120 130 140 150
AASAKALGLK HIVITMVSRD DLEDGGADAL ARIITTLHIE LPEATIEVLA
160 170 180 190 200
SDFEGNIDAL HHLLDARIAI YNHNVETVER LSPLVRHKAT YRRSLMMLEQ
210 220 230 240 250
AAQYLPDLMI KSGIMVGLGE QESEIKQTLK DLADHGVKIV TIGQYLRPSR
260 270 280 290 300
RHIPVKSYVS PETFDYYRSV GEALGLFIYA GPFVRSSFNA DAVFEAMSQR

ERLSASIQ
Length:308
Mass (Da):34,278
Last modified:October 1, 2000 - v1
Checksum:i617846CB79C12A92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002160 Genomic DNA. Translation: AAF39645.1.
PIRiC81658.
RefSeqiWP_010231744.1. NZ_ACOV01000004.1.

Genome annotation databases

EnsemblBacteriaiAAF39645; AAF39645; TC_0847.
GeneIDi1246215.
KEGGicmu:TC_0847.

Similar proteinsi

Entry informationi

Entry nameiLIPA_CHLMU
AccessioniPrimary (citable) accession number: Q9PJI2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: October 25, 2017
This is version 111 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

Documents

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