Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase

Gene

lipA

Organism
Salmonella newport (strain SL254)
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 bindingi68 – 681Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi79 – 791Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi94 – 941Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi98 – 981Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi101 – 1011Iron-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

BioCyciSENT423368:GHJB-679-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:SNSL254_A0688
OrganismiSalmonella newport (strain SL254)
Taxonomic identifieri423368 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000008824 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 – 321321Lipoyl synthasePRO_1000099632Add
BLAST

Proteomic databases

PRIDEiB4SYJ0.

Interactioni

Protein-protein interaction databases

STRINGi423368.SNSL254_A0688.

Structurei

3D structure databases

ProteinModelPortaliB4SYJ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
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.

B4SYJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKPIVMERG VKYRDADKMA LIPVKNVVTE RDALLRKPEW MKIKLPADST
60 70 80 90 100
RIQGIKAAMR KNGLHSVCEE ASCPNLAECF NHGTATFMIL GAICTRRCPF
110 120 130 140 150
CDVAHGRPVA PDAEEPQKLA QTIADMALRY VVITSVDRDD LRDGGAQHFA
160 170 180 190 200
DCITAIRAKS PEIKIETLVP DFRGRMDRAL DILNATPPDV FNHNLENVPR
210 220 230 240 250
IYRQVRPGAD YNWSLKLLER FKEAHPEIPT KSGLMVGLGE TNAEIIEVMR
260 270 280 290 300
DLRRHGVTML TLGQYLQPSR HHLPVQRYVS PEEFDEMKAE ALAMGFTHAA
310 320
CGPFVRSSYH ADLQAKGMEV K
Length:321
Mass (Da):36,042
Last modified:September 22, 2008 - v1
Checksum:iF57DF09996E9309C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001113 Genomic DNA. Translation: ACF62738.1.
RefSeqiYP_002039874.1. NC_011080.1.

Genome annotation databases

EnsemblBacteriaiACF62738; ACF62738; SNSL254_A0688.
PATRICi18519800. VBISalEnt114557_0818.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001113 Genomic DNA. Translation: ACF62738.1.
RefSeqiYP_002039874.1. NC_011080.1.

3D structure databases

ProteinModelPortaliB4SYJ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi423368.SNSL254_A0688.

Proteomic databases

PRIDEiB4SYJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF62738; ACF62738; SNSL254_A0688.
PATRICi18519800. VBISalEnt114557_0818.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciSENT423368:GHJB-679-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. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
    Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
    J. Bacteriol. 193:3556-3568(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SL254.

Entry informationi

Entry nameiLIPA_SALNS
AccessioniPrimary (citable) accession number: B4SYJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2009
Last sequence update: September 22, 2008
Last modified: March 3, 2015
This is version 49 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.