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Protein

Lipoyl synthase

Gene

lipA

Organism
Bacteroides fragilis (strain YCH46)
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 bindingi39 – 391Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi44 – 441Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi50 – 501Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi65 – 651Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi69 – 691Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi72 – 721Iron-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

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:BF0976
OrganismiBacteroides fragilis (strain YCH46)
Taxonomic identifieri295405 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000002197 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 – 288288Lipoyl synthasePRO_0000325233Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ64XQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG118519.
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.

Q64XQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNDKRVRKP EWLKISIGAN ERYTETKRIV ESHCLHTICS SGRCPNMGEC
60 70 80 90 100
WGKGTATFMI AGDICTRSCK FCNTQTGRPL PLDPDEPAHV AESIALMKLS
110 120 130 140 150
HAVITSVDRD DLPDLGAAHW AQTIREIKRL NPETTTEVLI PDFQGRKELI
160 170 180 190 200
DQVIKACPEI ISHNMETVKR ISPQVRSAAN YHTSLEVIRQ IAESGITAKS
210 220 230 240 250
GIMVGLGETP AEVEELMDDL ISVGCKILTI GQYLQPTHKH FPVAAYITPE
260 270 280
QFAVYKETGL KKGFEQVESA PLVRSSYHAE KHIRFNNK
Length:288
Mass (Da):32,092
Last modified:October 25, 2004 - v1
Checksum:i546C89DE515F08D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006841 Genomic DNA. Translation: BAD47726.1.
RefSeqiWP_008767975.1. NC_006347.1.
YP_098260.1. NC_006347.1.

Genome annotation databases

EnsemblBacteriaiBAD47726; BAD47726; BF0976.
GeneIDi3081276.
KEGGibfr:BF0976.
PATRICi21047706. VBIBacFra17906_0976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006841 Genomic DNA. Translation: BAD47726.1.
RefSeqiWP_008767975.1. NC_006347.1.
YP_098260.1. NC_006347.1.

3D structure databases

ProteinModelPortaliQ64XQ0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD47726; BAD47726; BF0976.
GeneIDi3081276.
KEGGibfr:BF0976.
PATRICi21047706. VBIBacFra17906_0976.

Phylogenomic databases

eggNOGiNOG118519.
HOGENOMiHOG000235997.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

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. "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
    Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
    Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: YCH46.

Entry informationi

Entry nameiLIPA_BACFR
AccessioniPrimary (citable) accession number: Q64XQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 25, 2004
Last modified: June 24, 2015
This is version 73 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

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.