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Protein

Lipoyl synthase 2

Gene

lipA2

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(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. Octanoyltransferase (lipB)
  2. Lipoyl synthase 2 (lipA2), Lipoyl synthase 1 (lipA1)
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 bindingi37Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi42Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi48Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi63Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi67Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi70Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase 2UniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-syn 2UniRule annotation
Lipoate synthase 2UniRule annotation
Lipoic acid synthase 2UniRule annotation
Sulfur insertion protein lipA2
Gene namesi
Name:lipA2UniRule annotation
Ordered Locus Names:tll0574
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001023671 – 290Lipoyl synthase 2Add BLAST290

Interactioni

Protein-protein interaction databases

STRINGi197221.tll0574.

Structurei

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 16Combined sources8
Helixi23 – 31Combined sources9
Turni37 – 39Combined sources3
Turni43 – 48Combined sources6
Helixi49 – 51Combined sources3
Beta strandi53 – 59Combined sources7
Beta strandi61 – 65Combined sources5
Beta strandi72 – 74Combined sources3
Helixi85 – 96Combined sources12
Beta strandi99 – 105Combined sources7
Turni112 – 115Combined sources4
Helixi116 – 129Combined sources14
Beta strandi134 – 138Combined sources5
Helixi151 – 159Combined sources9
Beta strandi164 – 167Combined sources4
Helixi174 – 176Combined sources3
Helixi177 – 180Combined sources4
Helixi186 – 199Combined sources14
Beta strandi205 – 211Combined sources7
Helixi217 – 229Combined sources13
Beta strandi234 – 239Combined sources6
Helixi256 – 269Combined sources14
Beta strandi272 – 277Combined sources6
Turni282 – 287Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4U0OX-ray1.60B1-290[»]
4U0PX-ray1.62B1-290[»]
ProteinModelPortaliQ8DLC2.
SMRiQ8DLC2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235998.
KOiK03644.
OMAiGICTRRC.
OrthoDBiPOG091H069D.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8DLC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSRPLPSW LRKPLGKASE ISTVQRLVRQ YGIHTICEEG RCPNRGECYG
60 70 80 90 100
QKTATFLLLG PTCTRACAFC QVEKGHAPAA VDPEEPTKIA AAVATLGLRY
110 120 130 140 150
VVLTSVARDD LPDQGAGQFV ATMAAIRQRC PGTEIEVLSP DFRMDRGRLS
160 170 180 190 200
QRDCIAQIVA AQPACYNHNL ETVRRLQGPV RRGATYESSL RVLATVKELN
210 220 230 240 250
PDIPTKSGLM LGLGETEAEI IETLKDLRRV GCDRLTLGQY LPPSLSHLPV
260 270 280 290
VKYWTPEEFN TLGNIARELG FSHVRSGPLV RSSYHAAEGG
Length:290
Mass (Da):31,735
Last modified:March 1, 2003 - v1
Checksum:i60BE127E2B9A59D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08126.1.
RefSeqiNP_681364.1. NC_004113.1.
WP_011056422.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC08126; BAC08126; BAC08126.
GeneIDi1012525.
KEGGitel:tll0574.
PATRICi23926408. VBITheElo119873_0606.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08126.1.
RefSeqiNP_681364.1. NC_004113.1.
WP_011056422.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4U0OX-ray1.60B1-290[»]
4U0PX-ray1.62B1-290[»]
ProteinModelPortaliQ8DLC2.
SMRiQ8DLC2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi197221.tll0574.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC08126; BAC08126; BAC08126.
GeneIDi1012525.
KEGGitel:tll0574.
PATRICi23926408. VBITheElo119873_0606.

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235998.
KOiK03644.
OMAiGICTRRC.
OrthoDBiPOG091H069D.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPA2_THEEB
AccessioniPrimary (citable) accession number: Q8DLC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.