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Protein

Lipoyl synthase

Gene

lipA

Organism
Burkholderia mallei (Pseudomonas mallei)
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 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 bindingi76Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi81Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi87Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi102Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi106Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi109Iron-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:RY28_00205Imported
OrganismiBurkholderia mallei (Pseudomonas mallei)Imported
Taxonomic identifieri13373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000218037 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

SMRiA0A290Y604
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini92 – 301Elp3InterPro annotationAdd BLAST210

Sequence similaritiesi

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

Phylogenomic databases

KOiK03644

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
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.

A0A290Y604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDLTATPAP AEPAASAYDP TAKQKAQAKT ARIPIKIVPI EKLKKPEWIR
60 70 80 90 100
VKAATSSSRF NEIKTILREH NLHTVCEEAS CPNIGECFGK GTATFMIMGD
110 120 130 140 150
KCTRRCPFCD VGHGRPDPLD ADEPKNLART IAALKLKYVV ITSVDRDDLR
160 170 180 190 200
DGGAGHFVEC IREVREQSPA TRIEILTPDF RGRLDRALAI LNAAPPDVMN
210 220 230 240 250
HNLETVPRLY KEARPGSDYA HSLKLLKDFK ALHPDVATKS GLMVGLGETT
260 270 280 290 300
DEILQVMRDL RAHDVDMLTI GQYLQPSEHH LPVREYVHPD TFKMYEEEAY
310 320
KMGFTHAAVG AMVRSSYHAD LQAHGAGVV
Length:329
Mass (Da):36,459
Last modified:December 20, 2017 - v1
Checksum:i209EA922ADB5BC9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP009929 Genomic DNA Translation: ATE31262.1
RefSeqiWP_004189177.1, NZ_MKIU01000244.1

Genome annotation databases

KEGGibmab:BM45_2756
bmae:DM78_2923
bmaf:DM51_3032
bmai:DM57_2069
bmal:DM55_787
bmaq:DM76_768

Similar proteinsi

Entry informationi

Entry nameiA0A290Y604_BURML
AccessioniPrimary (citable) accession number: A0A290Y604
Entry historyiIntegrated into UniProtKB/TrEMBL: December 20, 2017
Last sequence update: December 20, 2017
Last modified: July 18, 2018
This is version 6 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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