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Protein

Lipoyl synthase

Gene

lipA

Organism
Ruthia magnifica subsp. Calyptogena magnifica
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi67 – 671Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi88 – 881Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi92 – 921Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi95 – 951Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciCRUT413404:GHM7-563-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:Rmag_0543
OrganismiRuthia magnifica subsp. Calyptogena magnifica
Taxonomic identifieri413404 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbiontsCandidatus Ruthia
ProteomesiUP000002587 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Lipoyl synthasePRO_0000325307Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi413404.Rmag_0543.

Structurei

3D structure databases

ProteinModelPortaliA1AWI8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.

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.

A1AWI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQEIDIKSL KGKSKVVRLK IKPDSERLPI KKPNWIRIKH VASQKVEQLK
60 70 80 90 100
KTLRSQKLFT VCEEAQCPNL SECFNHGAAT FMIMGQICTR RCPFCDVAHG
110 120 130 140 150
KPKALDVDEP KHLANTIKKM QLKYVVITSV DRDDLRDGGA QHFKTCIDNI
160 170 180 190 200
RLSTPKVKIE ILTPDFRGRI DKVLEVFKSC SPNVFNHNLE TVPSLYQKVR
210 220 230 240 250
PGANYNYSLR LLKAFKQQHP FVITKSGLML GVGESEKQVI NVLKDLRKHN
260 270 280 290 300
VDMLTLGQYL QPSKHHLAVE AYIHPNQFDK YKKIALKLGF SQVASGPMVR
310
SSYHADLQIK GELIS
Length:315
Mass (Da):35,868
Last modified:January 22, 2007 - v1
Checksum:iED6FB43F399EF0C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000488 Genomic DNA. Translation: ABL02295.1.
RefSeqiWP_011737920.1. NC_008610.1.
YP_903766.1. NC_008610.1.

Genome annotation databases

EnsemblBacteriaiABL02295; ABL02295; Rmag_0543.
KEGGirma:Rmag_0543.
PATRICi32000775. VBICanRut45856_0606.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000488 Genomic DNA. Translation: ABL02295.1.
RefSeqiWP_011737920.1. NC_008610.1.
YP_903766.1. NC_008610.1.

3D structure databases

ProteinModelPortaliA1AWI8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi413404.Rmag_0543.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL02295; ABL02295; Rmag_0543.
KEGGirma:Rmag_0543.
PATRICi32000775. VBICanRut45856_0606.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciCRUT413404:GHM7-563-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiLIPA_RUTMC
AccessioniPrimary (citable) accession number: A1AWI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 17, 2008
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 63 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.