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Protein

Lipoyl synthase

Gene

lipA

Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
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.

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.

Cofactori

[4Fe-4S] clusterNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

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].
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 bindingi47Iron-sulfur 1 (4Fe-4S)1
Metal bindingi52Iron-sulfur 1 (4Fe-4S)1
Metal bindingi58Iron-sulfur 1 (4Fe-4S)1
Metal bindingi73Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi77Iron-sulfur 2 (4Fe-4S-S-AdoMet)1
Metal bindingi80Iron-sulfur 2 (4Fe-4S-S-AdoMet)1

GO - Molecular functioni

GO - Biological processi

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 synthase (EC:2.8.1.8)
Alternative name(s):
Lip-syn
Short name:
LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene namesi
Name:lipA
Ordered Locus Names:CT_558
OrganismiChlamydia trachomatis (strain D/UW-3/Cx)
Taxonomic identifieri272561 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000431 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001023061 – 311Lipoyl synthaseAdd BLAST311

Structurei

3D structure databases

ProteinModelPortaliO84562.
SMRiO84562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
InParanoidiO84562.
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.

O84562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDSESPIPK KSIPARFPKW LRQKLPLGRV FAQTDNTIKN KGLPTVCEEA
60 70 80 90 100
SCPNRTHCWS RHTATYLALG DACTRRCGFC DIDFTRNPLP PDPEEGAKIA
110 120 130 140 150
ESAKALGLKH IVITMVSRDD LEDGGASALV HIIETLHTEL PTATIEVLAS
160 170 180 190 200
DFEGNIAALH HLLDAHIAIY NHNVETVERL TPFVRHKATY RRSLMMLENA
210 220 230 240 250
AKYLPNLMTK SGIMVGLGEQ ESEVKQTLKD LADHGVKIVT IGQYLRPSRR
260 270 280 290 300
HIPVKSYVSP ETFDYYRSVG ESLGLFIYAG PFVRSSFNAD SVFEAMRQRE
310
TSTSALLPNK D
Length:311
Mass (Da):34,661
Last modified:November 1, 1998 - v1
Checksum:i0B613421B1F330DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001273 Genomic DNA. Translation: AAC68160.1.
PIRiF71500.
RefSeqiNP_220073.1. NC_000117.1.
WP_010725252.1. NC_000117.1.

Genome annotation databases

EnsemblBacteriaiAAC68160; AAC68160; CT_558.
GeneIDi884334.
KEGGictr:CT_558.
PATRICifig|272561.5.peg.609.

Similar proteinsi

Entry informationi

Entry nameiLIPA_CHLTR
AccessioniPrimary (citable) accession number: O84562
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
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, Reference proteome

Documents

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