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Protein

Lipoyl synthase

Gene

lipA

Organism
bacterium BMS3Bbin05
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 + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [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. 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 bindingi31Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi36Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi42Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi57Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi61Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi64Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

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 annotationImported
ORF Names:BMS3Bbin05_02230Imported
Organismibacterium BMS3Bbin05Imported
Taxonomic identifieri2005728 [NCBI]
Taxonomic lineageiBacteria

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 255Elp3InterPro annotationAdd BLAST209

Sequence similaritiesi

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

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.
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.

A0A2H6I468-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLPPWLRTN TFSNLHRTKS ILRGHRLSTV CEEARCPNRG HCFSKPTATF
60 70 80 90 100
LILGDHCTRN CSFCSVNPGR PSPPDPEEPE RVARAVKEMG LKYVVVTSVT
110 120 130 140 150
RDDLPDGGAE QFALTVRAIR ESVAEARIEI LTPDFRGDSN SIKTVLDACP
160 170 180 190 200
DVFNHNIETV PHLYAKVRPQ ADYKRSLSVL RRAAGLSRGA LTKSGLMVGL
210 220 230 240 250
GESFEEVANV MKDLREAGCR MLTIGQYLRP EKNNIPVREY VHPDIFDKYK
260 270 280
DQAQRLGFRF VASAPLVRSS MNAEELFLHN D
Length:281
Mass (Da):31,550
Last modified:February 28, 2018 - v1
Checksum:i075D05315E30991B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BDTO01000080 Genomic DNA. Translation: GBE33291.1.

Similar proteinsi

Entry informationi

Entry nameiA0A2H6I468_9BACT
AccessioniPrimary (citable) accession number: A0A2H6I468
Entry historyiIntegrated into UniProtKB/TrEMBL: February 28, 2018
Last sequence update: February 28, 2018
Last modified: March 28, 2018
This is version 2 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

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