UniProtKB - Q8DLC2 (LIPA2_THEEB)
Protein
Lipoyl synthase 2
Gene
lipA2
Organism
Thermosynechococcus elongatus (strain BP-1)
Status
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
- [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S]2+ cluster] + 4 H+ + N6-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N6-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe3+ + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]UniRule annotationEC:2.8.1.8UniRule annotation
Cofactori
[4Fe-4S] clusterUniRule annotation1 PublicationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation1 Publication
: protein lipoylation via endogenous pathway Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotationProteins known to be involved in the 2 steps of the subpathway in this organism are:
- Octanoyltransferase (lipB)
- Lipoyl synthase 1 (lipA1), Lipoyl synthase 2 (lipA2)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 37 | Iron-sulfur 1 (4Fe-4S)UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 42 | Iron-sulfur 1 (4Fe-4S)UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 48 | Iron-sulfur 1 (4Fe-4S)UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 63 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 67 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 70 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 283 | Iron-sulfur 1 (4Fe-4S)UniRule annotationCombined sources1 Publication | 1 |
GO - Molecular functioni
- 4 iron, 4 sulfur cluster binding Source: UniProtKB-UniRule
- lipoate synthase activity Source: UniProtKB-UniRule
- lipoyl synthase activity (acting on glycine-cleavage complex H protein Source: UniProtKB-EC
- lipoyl synthase activity (acting on pyruvate dehydrogenase E2 protein) Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- protein lipoylation Source: UniProtKB-UniRule
Keywordsi
Molecular function | Transferase |
Ligand | 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine |
Enzyme and pathway databases
UniPathwayi | UPA00538;UER00593 |
Names & Taxonomyi
Protein namesi | Recommended name: Lipoyl synthase 21 PublicationUniRule annotation (EC:2.8.1.8UniRule annotation)Alternative name(s): Lip-syn 2UniRule annotation Short name: LS 2UniRule annotation Lipoate synthase 2UniRule annotation Lipoic acid synthase 2UniRule annotation Sulfur insertion protein LipA 2UniRule annotation |
Gene namesi | Name:lipA21 PublicationUniRule annotation Ordered Locus Names:tll0574 |
Organismi | Thermosynechococcus elongatus (strain BP-1) |
Taxonomic identifieri | 197221 [NCBI] |
Taxonomic lineagei | Bacteria › Cyanobacteria › Synechococcales › Synechococcaceae › Thermosynechococcus › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000102367 | 1 – 290 | Lipoyl synthase 2Add BLAST | 290 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q8DLC2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 49 – 272 | Radical SAM corePROSITE-ProRule annotationAdd BLAST | 224 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0320, Bacteria |
OMAi | GRCPNRG |
OrthoDBi | 1184806at2 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00206, Lipoyl_synth, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR006638, Elp3/MiaB/NifB IPR003698, Lipoyl_synth IPR007197, rSAM |
PANTHERi | PTHR10949, PTHR10949, 1 hit |
Pfami | View protein in Pfam PF04055, Radical_SAM, 1 hit |
PIRSFi | PIRSF005963, Lipoyl_synth, 1 hit |
SFLDi | SFLDF00271, lipoyl_synthase, 1 hit |
SMARTi | View protein in SMART SM00729, Elp3, 1 hit |
TIGRFAMsi | TIGR00510, lipA, 1 hit |
PROSITEi | View protein in PROSITE PS51918, RADICAL_SAM, 1 hit |
i Sequence
Sequence statusi: Complete.
Q8DLC2-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000039 Genomic DNA Translation: BAC08126.1 |
RefSeqi | NP_681364.1, NC_004113.1 WP_011056422.1, NC_004113.1 |
Genome annotation databases
EnsemblBacteriai | BAC08126; BAC08126; BAC08126 |
KEGGi | tel:tll0574 |
PATRICi | fig|197221.4.peg.606 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000039 Genomic DNA Translation: BAC08126.1 |
RefSeqi | NP_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 entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4U0O | X-ray | 1.60 | B | 1-290 | [»] | |
4U0P | X-ray | 1.62 | B | 1-290 | [»] | |
SMRi | Q8DLC2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 197221.22294295 |
Genome annotation databases
EnsemblBacteriai | BAC08126; BAC08126; BAC08126 |
KEGGi | tel:tll0574 |
PATRICi | fig|197221.4.peg.606 |
Phylogenomic databases
eggNOGi | COG0320, Bacteria |
OMAi | GRCPNRG |
OrthoDBi | 1184806at2 |
Enzyme and pathway databases
UniPathwayi | UPA00538;UER00593 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00206, Lipoyl_synth, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR006638, Elp3/MiaB/NifB IPR003698, Lipoyl_synth IPR007197, rSAM |
PANTHERi | PTHR10949, PTHR10949, 1 hit |
Pfami | View protein in Pfam PF04055, Radical_SAM, 1 hit |
PIRSFi | PIRSF005963, Lipoyl_synth, 1 hit |
SFLDi | SFLDF00271, lipoyl_synthase, 1 hit |
SMARTi | View protein in SMART SM00729, Elp3, 1 hit |
TIGRFAMsi | TIGR00510, lipA, 1 hit |
PROSITEi | View protein in PROSITE PS51918, RADICAL_SAM, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LIPA2_THEEB | |
Accessioni | Q8DLC2Primary (citable) accession number: Q8DLC2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 10, 2004 |
Last sequence update: | March 1, 2003 | |
Last modified: | December 2, 2020 | |
This is version 104 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families