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Protein

Lipoyl synthase

Gene

lipA

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
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:iprotein 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 bindingi37 – 371Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi42 – 421Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi48 – 481Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi63 – 631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi67 – 671Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi70 – 701Iron-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

BioCyciBTHE226186:GJXV-4270-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:BT_4192
OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifieri226186 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000001414 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 – 282282Lipoyl synthasePRO_0000102289Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi226186.BT_4192.

Structurei

3D structure databases

ProteinModelPortaliQ8A029.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiQ8A029.
KOiK03644.
OMAiNVCTRSC.
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.

Q8A029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADRVRKPEW LKINIGANDR YTETKRIVDS HCLHTICSSG RCPNMGECWG
60 70 80 90 100
KGTATFMIGG DICTRSCKFC NTQTGRPHPL DANEPTHVAE SIALMKLDHA
110 120 130 140 150
VVTSVDRDDL PDLGAGHWAH TIREIKRLNP QTTIEVLIPD FQGRMELVDL
160 170 180 190 200
VIEANPDIIS HNMETVRRIS PLVRSAANYD TSLQVIGHIA RSGTKSKSGI
210 220 230 240 250
MVGLGETPQE VETIMDDLLA VGCQILTIGQ YLQPTHRHYP VAEYVTPQQF
260 270 280
ATYKTIGLEK GFSIVESAPL VRSSYHAEKH IR
Length:282
Mass (Da):31,352
Last modified:June 1, 2003 - v1
Checksum:iF3E992E4F24F728C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO79297.1.
RefSeqiNP_813103.1. NC_004663.1.
WP_008764405.1. NC_004663.1.

Genome annotation databases

EnsemblBacteriaiAAO79297; AAO79297; BT_4192.
GeneIDi1072478.
KEGGibth:BT_4192.
PATRICi21063426. VBIBacThe70966_4260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO79297.1.
RefSeqiNP_813103.1. NC_004663.1.
WP_008764405.1. NC_004663.1.

3D structure databases

ProteinModelPortaliQ8A029.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226186.BT_4192.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO79297; AAO79297; BT_4192.
GeneIDi1072478.
KEGGibth:BT_4192.
PATRICi21063426. VBIBacThe70966_4260.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiQ8A029.
KOiK03644.
OMAiNVCTRSC.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciBTHE226186:GJXV-4270-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. "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
    Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
    Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Entry informationi

Entry nameiLIPA_BACTN
AccessioniPrimary (citable) accession number: Q8A029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 90 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.