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Protein

Lipoyl synthase

Gene

lipA

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
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 bindingi43Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi48Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi54Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi69Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi73Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi76Iron-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

BioCyciDVUL882:G1GT1-933-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:DVU_0905
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003252471 – 298Lipoyl synthaseAdd BLAST298

Proteomic databases

PaxDbiQ72DM4

Interactioni

Protein-protein interaction databases

STRINGi882.DVU0905

Structurei

3D structure databases

ProteinModelPortaliQ72DM4
SMRiQ72DM4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G Bacteria
COG0320 LUCA
KOiK03644
OMAiGRCPNRG
OrthoDBiPOG091H069D
PhylomeDBiQ72DM4

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.

Q72DM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPDNSSPS LRIPPWLRVK LPCSHTFADT RALVEGLGLN TVCNSAKCPN
60 70 80 90 100
MFECFSSGTA TFLILGNVCT RNCAFCNITP GHVSPPDPDE PRRVAEAAAR
110 120 130 140 150
LALRHVVVTS VTRDDLDDGG AAHFAATITR LRAALPAATV EVLIPDFRGD
160 170 180 190 200
HAALRTVMAA APHIVNHNVE TPPAHYARIR PQADYRQSLE LLRRVKAAGG
210 220 230 240 250
VAKSGLMVGL GENDTEVEGV LADLADCGCD IVTIGQYMRP SRQHPPVERY
260 270 280 290
VHPDTFESFA ACGRGMGIPF VFSAPLVRSS YNAESAYNAL CTLRTEPA
Length:298
Mass (Da):32,017
Last modified:July 5, 2004 - v1
Checksum:i566B03D04879200B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017285 Genomic DNA Translation: AAS95385.1
RefSeqiWP_010938204.1, NC_002937.3
YP_010126.1, NC_002937.3

Genome annotation databases

EnsemblBacteriaiAAS95385; AAS95385; DVU_0905
GeneIDi2795415
KEGGidvu:DVU0905
PATRICifig|882.5.peg.849

Similar proteinsi

Entry informationi

Entry nameiLIPA_DESVH
AccessioniPrimary (citable) accession number: Q72DM4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: July 5, 2004
Last modified: May 23, 2018
This is version 91 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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