UniProtKB - P60716 (LIPA_ECOLI)
Protein
Lipoyl synthase
Gene
lipA
Organism
Escherichia coli (strain K12)
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. Free octanoate is not a substrate for LipA.3 Publications
Miscellaneous
The source of sulfurs is the LipA protein itself, most likely one 4Fe-4S cluster.
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 annotation1 PublicationEC:2.8.1.8UniRule annotation1 Publication
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
Activity regulationi
Is physiologically inhibited by accumulation of the reaction product 5'-deoxyadenosine (PubMed:15911379). Inhibited by the AdoMet analog S-adenosyl homocysteine.1 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 annotation1 PublicationProteins known to be involved in the 2 steps of the subpathway in this organism are:
- Octanoyltransferase (lipB), Octanoyltransferase (lipB)
- Lipoyl synthase (lipA), Lipoyl synthase (lipA)
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 | 68 | Iron-sulfur 1 (4Fe-4S)UniRule annotation | 1 | |
Metal bindingi | 73 | Iron-sulfur 1 (4Fe-4S)UniRule annotation | 1 | |
Metal bindingi | 79 | Iron-sulfur 1 (4Fe-4S)UniRule annotation | 1 | |
Metal bindingi | 94 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation | 1 | |
Metal bindingi | 98 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation | 1 | |
Metal bindingi | 101 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation | 1 | |
Metal bindingi | 308 | Iron-sulfur 1 (4Fe-4S)UniRule annotation | 1 |
GO - Molecular functioni
- 4 iron, 4 sulfur cluster binding Source: EcoliWiki
- lipoate synthase activity Source: EcoliWiki
- 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
- lipoate biosynthetic process Source: EcoliWiki
- protein lipoylation Source: EcoliWiki
Keywordsi
Molecular function | Transferase |
Ligand | 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11306-MONOMER MetaCyc:EG11306-MONOMER |
UniPathwayi | UPA00538;UER00593 |
Names & Taxonomyi
Protein namesi | Recommended name: Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation1 Publication)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 Synonyms:lip Ordered Locus Names:b0628, JW0623 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 68 – 79 | CEEAS…NLAEC → AEEASAPNLAEA: Loss of 1 4Fe-4S cluster binding. Loss of activity. 1 PublicationAdd BLAST | 12 | |
Mutagenesisi | 94 – 101 | CTRRCPFC → ATRRAPFA: Loss of 1 4Fe-4S cluster binding. Loss of activity. 1 Publication | 8 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000102313 | 1 – 321 | Lipoyl synthaseAdd BLAST | 321 |
Proteomic databases
jPOSTi | P60716 |
PaxDbi | P60716 |
PRIDEi | P60716 |
Interactioni
Subunit structurei
Monomer or homodimer.
Protein-protein interaction databases
BioGRIDi | 4260638, 67 interactors 849612, 2 interactors |
DIPi | DIP-48008N |
IntActi | P60716, 13 interactors |
STRINGi | 511145.b0628 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 80 – 297 | Radical SAM corePROSITE-ProRule annotationAdd BLAST | 218 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0320, Bacteria |
HOGENOMi | CLU_033144_2_1_6 |
InParanoidi | P60716 |
PhylomeDBi | P60716 |
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 IPR031691, LIAS_N IPR003698, Lipoyl_synth IPR007197, rSAM |
PANTHERi | PTHR10949, PTHR10949, 1 hit |
Pfami | View protein in Pfam PF16881, LIAS_N, 1 hit 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.
P60716-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSKPIVMERG VKYRDADKMA LIPVKNVATE REALLRKPEW MKIKLPADST
60 70 80 90 100
RIQGIKAAMR KNGLHSVCEE ASCPNLAECF NHGTATFMIL GAICTRRCPF
110 120 130 140 150
CDVAHGRPVA PDANEPVKLA QTIADMALRY VVITSVDRDD LRDGGAQHFA
160 170 180 190 200
DCITAIREKS PQIKIETLVP DFRGRMDRAL DILTATPPDV FNHNLENVPR
210 220 230 240 250
IYRQVRPGAD YNWSLKLLER FKEAHPEIPT KSGLMVGLGE TNEEIIEVMR
260 270 280 290 300
DLRRHGVTML TLGQYLQPSR HHLPVQRYVS PDEFDEMKAE ALAMGFTHAA
310 320
CGPFVRSSYH ADLQAKGMEV K
Sequence cautioni
The sequence AAA24072 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 35 | L → V (PubMed:1577793).Curated | 1 | |
Sequence conflicti | 35 | L → V (PubMed:8444795).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M82805 Genomic DNA Translation: AAA24072.1 Different initiation. L07636 Genomic DNA Translation: AAA66345.1 U82598 Genomic DNA Translation: AAB40828.1 U00096 Genomic DNA Translation: AAC73729.1 AP009048 Genomic DNA Translation: BAA35271.1 |
PIRi | B64797 |
RefSeqi | NP_415161.1, NC_000913.3 WP_000042632.1, NZ_STEB01000031.1 |
Genome annotation databases
EnsemblBacteriai | AAC73729; AAC73729; b0628 BAA35271; BAA35271; BAA35271 |
GeneIDi | 58390045 945227 |
KEGGi | ecj:JW0623 eco:b0628 |
PATRICi | fig|1411691.4.peg.1640 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M82805 Genomic DNA Translation: AAA24072.1 Different initiation. L07636 Genomic DNA Translation: AAA66345.1 U82598 Genomic DNA Translation: AAB40828.1 U00096 Genomic DNA Translation: AAC73729.1 AP009048 Genomic DNA Translation: BAA35271.1 |
PIRi | B64797 |
RefSeqi | NP_415161.1, NC_000913.3 WP_000042632.1, NZ_STEB01000031.1 |
3D structure databases
SMRi | P60716 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4260638, 67 interactors 849612, 2 interactors |
DIPi | DIP-48008N |
IntActi | P60716, 13 interactors |
STRINGi | 511145.b0628 |
Proteomic databases
jPOSTi | P60716 |
PaxDbi | P60716 |
PRIDEi | P60716 |
Genome annotation databases
EnsemblBacteriai | AAC73729; AAC73729; b0628 BAA35271; BAA35271; BAA35271 |
GeneIDi | 58390045 945227 |
KEGGi | ecj:JW0623 eco:b0628 |
PATRICi | fig|1411691.4.peg.1640 |
Organism-specific databases
EchoBASEi | EB1283 |
Phylogenomic databases
eggNOGi | COG0320, Bacteria |
HOGENOMi | CLU_033144_2_1_6 |
InParanoidi | P60716 |
PhylomeDBi | P60716 |
Enzyme and pathway databases
UniPathwayi | UPA00538;UER00593 |
BioCyci | EcoCyc:EG11306-MONOMER MetaCyc:EG11306-MONOMER |
Miscellaneous databases
PROi | PR:P60716 |
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 IPR031691, LIAS_N IPR003698, Lipoyl_synth IPR007197, rSAM |
PANTHERi | PTHR10949, PTHR10949, 1 hit |
Pfami | View protein in Pfam PF16881, LIAS_N, 1 hit 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 | LIPA_ECOLI | |
Accessioni | P60716Primary (citable) accession number: P60716 Secondary accession number(s): P25845, P77595 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 13, 2004 |
Last sequence update: | April 13, 2004 | |
Last modified: | February 10, 2021 | |
This is version 144 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
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families