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Protein

Lipoyl synthase

Gene

lipA

Organism
Ochrobactrum intermedium LMG 3301
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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

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 bindingi70Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi75Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi81Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi96Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi100Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi103Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotation
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 annotationImported
ORF Names:OINT_1001247Imported
OrganismiOchrobactrum intermedium LMG 3301Imported
Taxonomic identifieri641118 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum
Proteomesi
  • UP000004386 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Protein-protein interaction databases

STRINGi641118.OINT_1001247

Structurei

3D structure databases

ProteinModelPortaliC4WJN6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini86 – 293Elp3InterPro annotationAdd BLAST208

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G Bacteria
COG0320 LUCA
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
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.

C4WJN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMARIGRES MVTVLDLVNQ GKRERHPEKA HRPDNVVLKK PDWIRVKAPV
60 70 80 90 100
SRGYSETRDI VRSNKLVTVC EEAGCPNIGE CWEKKHATFM IMGEICTRAC
110 120 130 140 150
AFCNVSTGIP TALDPNEPEN VAKAVKQMGL THVVITSVDR DDLADGGAQH
160 170 180 190 200
FAEVIQAIRE ATPATTIEIL TPDFLRKEGA LEIVVKARPD VFNHNLETVP
210 220 230 240 250
SKYLKVRPGA RYFHSIRLLQ RVKELDPTIF TKSGIMVGLG EERNEILQLM
260 270 280 290 300
DDLRSADVDF MTIGQYLQPT RKHHPVIRFV TPDEFKSFET IGRTKGFLLV
310 320 330
ASSPLTRSSH HAGDDFAKLR AAREAQIAAR A
Length:331
Mass (Da):37,045
Last modified:July 28, 2009 - v1
Checksum:i0AFEE18DAF550CD9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACQA01000001 Genomic DNA Translation: EEQ95848.1

Genome annotation databases

EnsemblBacteriaiEEQ95848; EEQ95848; OINT_1001247

Similar proteinsi

Entry informationi

Entry nameiC4WJN6_9RHIZ
AccessioniPrimary (citable) accession number: C4WJN6
Entry historyiIntegrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: July 18, 2018
This is version 58 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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