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Protein

Lipoyl synthase

Gene

lipA

Organism
Clostridium autoethanogenum DSM 10061
Status
Unreviewed-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 annotationSAAS 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 bindingi35Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi40Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi46Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi61Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi65Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi68Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotationImported
Ligand4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotation

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
ORF Names:CAETHG_1220Imported
OrganismiClostridium autoethanogenum DSM 10061Imported
Taxonomic identifieri1341692 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000017590 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliU5RRW1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 255Elp3InterPro annotationAdd BLAST205

Sequence similaritiesi

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

Phylogenomic databases

KOiK03644
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
SFLDiSFLDF00271 lipoyl_synthase, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

U5RRW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYKRKPEWLK IKIRGGQVSQ DVKDILKKYS LNTVCGEANC PNRMECFNKS
60 70 80 90 100
RATFMILGKN CTRNCTFCNV TKGKPEKVDK KEPFNVAQAV DKLELKYAVI
110 120 130 140 150
TSVTRDDLED GGASHFANVV EEIRKLNKNI TVEVLIPDFK GNETALKKVV
160 170 180 190 200
DSKPNVINHN VETTPALYKE VRPMAVYKRS LELLKRVKIM DNSILTKSGF
210 220 230 240 250
MLGLGEKEED IIEVLKDLRR ADCDIVTIGQ YLPPSSKHHP VVEYVHPDLF
260 270 280
KKYKEIALEL GFKFVSSSPL VRSSYHAEEM IES
Length:283
Mass (Da):32,198
Last modified:January 22, 2014 - v1
Checksum:i04AC86938D31B796
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP006763 Genomic DNA Translation: AGY75445.1
RefSeqiWP_013239950.1, NZ_CP012395.1

Genome annotation databases

EnsemblBacteriaiAGY75445; AGY75445; CAETHG_1220
GeneIDi33104214
KEGGicah:CAETHG_1220
PATRICifig|1341692.11.peg.1216

Similar proteinsi

Entry informationi

Entry nameiU5RRW1_9CLOT
AccessioniPrimary (citable) accession number: U5RRW1
Entry historyiIntegrated into UniProtKB/TrEMBL: January 22, 2014
Last sequence update: January 22, 2014
Last modified: July 18, 2018
This is version 33 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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