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Protein

Lipoyl synthase

Gene

lipA

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
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. no protein annotated in this organism
  2. Lipoyl synthase (lipA), Lipoyl synthase (lipA), 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 bindingi52Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi57Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi63Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi78Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi82Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi85Iron-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:CPn_0832, CP_1038, CpB0861
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000583 Componenti: Chromosome
  • UP000000801 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001023041 – 307Lipoyl synthaseAdd BLAST307

Interactioni

Protein-protein interaction databases

STRINGi182082.CpB0861

Structurei

3D structure databases

ProteinModelPortaliQ9Z774
SMRiQ9Z774
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
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.

Q9Z774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCRPTLNTD QPRVRKKLPE RFPKWLQRPL PQGSAFHATD ATIKRSGMPT
60 70 80 90 100
VCEEALCPNR AECWSRKTAT YLALGDVCTR SCGFCNIGHS KTPPALDPTE
110 120 130 140 150
PERIALSAKE LGLKHVVITM VARDDLEDGG AQGLVDIIQK LREELPQATT
160 170 180 190 200
EVLASDFQGN VSALHTLLDS GITIYNHNVE TVARLSPLVR HKATYARSMF
210 220 230 240 250
MLEQAANYLP DLKIKSGIMV GLGEMEGEVK QTLQDLASIG VRIVTIGQYL
260 270 280 290 300
RPSRKHLQVK SYVTPETFDY YRRVGEAMGL FVYAGPFVRS SFNADMILAS

VQDKASA
Length:307
Mass (Da):33,993
Last modified:May 1, 1999 - v1
Checksum:iF893D50F7BC90062
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA Translation: AAD18969.1
AE002161 Genomic DNA Translation: AAF38813.1
BA000008 Genomic DNA Translation: BAA99040.1
AB035942 Genomic DNA Translation: BAA88650.1
AE009440 Genomic DNA Translation: AAP98790.1
PIRiB72031
F86594
RefSeqiNP_225027.1, NC_000922.1
WP_010883469.1, NZ_LN847257.1

Genome annotation databases

EnsemblBacteriaiAAD18969; AAD18969; CPn_0832
AAF38813; AAF38813; CP_1038
AAP98790; AAP98790; CpB0861
BAA99040; BAA99040; BAA99040
GeneIDi894731
KEGGicpa:CP_1038
cpj:lipA
cpn:CPn0832
cpt:CpB0861
PATRICifig|115713.3.peg.911

Similar proteinsi

Entry informationi

Entry nameiLIPA_CHLPN
AccessioniPrimary (citable) accession number: Q9Z774
Secondary accession number(s): Q9JQ18
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 23, 2018
This is version 130 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
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Main funding by: National Institutes of Health