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Protein

Lipoyl synthase

Gene

lipA

Organism
Brucella suis biovar 1 (strain 1330)
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 bindingi60 – 601Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi65 – 651Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi71 – 711Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi86 – 861Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi90 – 901Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi93 – 931Iron-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

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:BR1124, BS1330_I1120
OrganismiBrucella suis biovar 1 (strain 1330)
Taxonomic identifieri204722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000007104 Componenti: Chromosome I UP000000824 Componenti: Chromosome I

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 – 322322Lipoyl synthasePRO_0000102296Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi204722.BR1124.

Structurei

3D structure databases

ProteinModelPortaliP65282.
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.

P65282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTVLNTVNQ SGRLRHPEKA HRPDNEVLKK PDWIRVKAPV SRGYGETREI
60 70 80 90 100
VRSNKLVTVC EEAGCPNIGE CWEKKHATFM IMGEICTRAC AFCNISTGIP
110 120 130 140 150
NALDPNEPEN IAKAVKQMGL THVVITSVDR DDLADGGAHH FAEVIKAVRE
160 170 180 190 200
AAPATTIEIL TPDFLRKEGA LEIVVKARPD VFNHNLETVP SKYLKVRPGA
210 220 230 240 250
RYFHSIRLLQ RVKELDPTIF TKSGIMVGLG EERNEILQLM DDLRSADVDF
260 270 280 290 300
MTIGQYLQPT RKHHPVIRFV KPDEFKSFET IGKTKGFLLV ASSPLTRSSH
310 320
HAGEDFAKLK AAREALYASR AS
Length:322
Mass (Da):35,957
Last modified:October 10, 2004 - v1
Checksum:i7A018D4FE62D1F99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN30044.1.
CP002997 Genomic DNA. Translation: AEM18462.1.
RefSeqiNP_698129.1. NC_004310.3.
YP_005615954.1. NC_017251.1.

Genome annotation databases

EnsemblBacteriaiAAN30044; AAN30044; BR1124.
AEM18462; AEM18462; BS1330_I1120.
KEGGibms:BR1124.
bsi:BS1330_I1120.
PATRICi17790581. VBIBruSui107850_1144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN30044.1.
CP002997 Genomic DNA. Translation: AEM18462.1.
RefSeqiNP_698129.1. NC_004310.3.
YP_005615954.1. NC_017251.1.

3D structure databases

ProteinModelPortaliP65282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi204722.BR1124.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN30044; AAN30044; BR1124.
AEM18462; AEM18462; BS1330_I1120.
KEGGibms:BR1124.
bsi:BS1330_I1120.
PATRICi17790581. VBIBruSui107850_1144.

Phylogenomic databases

eggNOGiCOG0320.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.

Entry informationi

Entry nameiLIPA_BRUSU
AccessioniPrimary (citable) accession number: P65282
Secondary accession number(s): G0KA46, Q8YHE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2004
Last sequence update: October 10, 2004
Last modified: March 31, 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. Brucella suis
    Brucella suis (strain 1330): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.