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Protein

Lipoyl synthase

Gene

lipA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi80 – 801Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi95 – 951Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi99 – 991Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi102 – 1021Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

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

BioCyciTTHE300852:GH8R-248-MONOMER.
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 annotation
Ordered Locus Names:TTHA0239
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Lipoyl synthasePRO_0000325318Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0239.

Structurei

3D structure databases

ProteinModelPortaliQ5SLQ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.
PhylomeDBiQ5SLQ4.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
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.

Q5SLQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPKFETVEL LSPTGEVVEL KVVKRGLAQA RPEPVDRNKP AWIKAPLPTG
60 70 80 90 100
PRYQALKAMV RELRLHTVCQ EALCPNIGEC WTHGTLTVMI LGDICTRACK
110 120 130 140 150
FCAVHTGNPK GLVDPEEPRR VAEAIARMGV RYVVLTSVDR DDLPDGGASH
160 170 180 190 200
FAATIRAIKE RAPGVLVEAL TPDFQGDLKA VETVLAANPE VYAQNLETVR
210 220 230 240 250
RLTPKVRDPR AGYEQTLKVL AHAKKVRPDI LTKSSLMLGL GETEEEILEA
260 270 280 290 300
MRDLRAAGVD ILTLGQYLRP TPAHLPVARY VPPEDFKRYE AWGYELGFRE
310 320
VFAGPLVRSS YRADRVFLEA TQR
Length:323
Mass (Da):35,909
Last modified:December 21, 2004 - v1
Checksum:iBA5EB201299570B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70062.1.
RefSeqiWP_011174105.1. NC_006461.1.
YP_143505.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70062; BAD70062; BAD70062.
GeneIDi3168651.
KEGGittj:TTHA0239.
PATRICi23955423. VBITheThe93045_0239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70062.1.
RefSeqiWP_011174105.1. NC_006461.1.
YP_143505.1. NC_006461.1.

3D structure databases

ProteinModelPortaliQ5SLQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70062; BAD70062; BAD70062.
GeneIDi3168651.
KEGGittj:TTHA0239.
PATRICi23955423. VBITheThe93045_0239.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.
PhylomeDBiQ5SLQ4.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciTTHE300852:GH8R-248-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
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...

Publicationsi

  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiLIPA_THET8
AccessioniPrimary (citable) accession number: Q5SLQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 21, 2004
Last modified: March 4, 2015
This is version 74 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.