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Protein

Lipoyl synthase

Gene

lipA

Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1) (Rochalimaea henselae)
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. 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 bindingi59Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi64Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi70Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi85Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi89Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi92Iron-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

BioCyciBHEN283166:G1GJ7-600-MONOMER
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:BH05790
OrganismiBartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1) (Rochalimaea henselae)
Taxonomic identifieri283166 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
Proteomesi
  • UP000000421 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000121891 – 320Lipoyl synthaseAdd BLAST320

Proteomic databases

PaxDbiQ6G401
PRIDEiQ6G401

Interactioni

Protein-protein interaction databases

STRINGi283166.BH05790

Structurei

3D structure databases

ProteinModelPortaliQ6G401
SMRiQ6G401
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.

Q6G401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTVVDRVTD RRLRHPEKAH RPDTSVQKKP DWIRVKAPTS QVYKETHGIV
60 70 80 90 100
RAHKLVTVCE EAGCPNIGEC WSQRHASFMI LGEICTRACA FCNVATGIPF
110 120 130 140 150
AVDENEPERV ADAVARMELK HVVITSVDRD DLADGGAEHF AKVIYAIRRK
160 170 180 190 200
APKTTIEVLT PDFRHKDGAL EIVVAAKPDV FNHNLETVPS KYLKVRPGAR
210 220 230 240 250
YFHSIRLLQR VKELDPTIFT KSGIMVGLGE ERNEILQLMD DLRSADVDFM
260 270 280 290 300
TIGQYLQPTR KHHPVIRFVP PEEFESFAKI GKVKGFLHMA SNPLTRSSHH
310 320
AGDDFAILQK ARDEKFALQR
Length:320
Mass (Da):36,202
Last modified:July 19, 2004 - v1
Checksum:i307FD4D4111224D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX897699 Genomic DNA Translation: CAF27387.1
RefSeqiWP_011180508.1, NZ_LRIJ02000001.1

Genome annotation databases

EnsemblBacteriaiCAF27387; CAF27387; BH05790
GeneIDi29621134
KEGGibhe:BH05790

Similar proteinsi

Entry informationi

Entry nameiLIPA_BARHE
AccessioniPrimary (citable) accession number: Q6G401
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: May 23, 2018
This is version 86 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

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