Skip Header

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

Q5WYF5

- LIPA_LEGPL

UniProt

Q5WYF5 - LIPA_LEGPL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lipoyl synthase

Gene

lipA

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - 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 = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

Cofactori

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 bindingi72 – 721Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi77 – 771Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi83 – 831Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi98 – 981Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi102 – 1021Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi105 – 1051Iron-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

BioCyciLPNE297245:GJD4-840-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:lpl0781
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517: Chromosome

Organism-specific databases

LegioListilpl0781.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Lipoyl synthasePRO_0000325268Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi297245.lpl0781.

Structurei

3D structure databases

ProteinModelPortaliQ5WYF5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiHPHIPTK.
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.

Q5WYF5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKLIDIPIV VESGQKYKTS QGVTAIKDGI KSSGQDHERL PKPKWLRIVN
60 70 80 90 100
HTTPAYSQVK EQVQKHRLAT VCEEAKCPNI SECWSHGTAT IMLMGAVCTR
110 120 130 140 150
ACRFCSVDTG NPHGWLDAEE PENTAETVAL MNLDYVVLTS VNRDDLPDGG
160 170 180 190 200
ANHYAKTIRA IKKRSPRTKV EALTPDFQGS ERDVAVLLDS GLDVFAQNVE
210 220 230 240 250
TVERLTHPVR DNRAGYQQTL NVLAFAKKYR PDVLTKTSLM LGLGETDEEI
260 270 280 290 300
IRTMDDLRAH HVDILTLGQY LQPTKNHLPI ARYVTPETFS ELRQIGLKKG
310 320
FFEVASGPLV RSSYRADRVF KRDNLGLDV
Length:329
Mass (Da):36,754
Last modified:November 23, 2004 - v1
Checksum:iED7555CFA828FC7B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH15015.1.
RefSeqiYP_126143.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH15015; CAH15015; lpl0781.
GeneIDi3115445.
KEGGilpf:lpl0781.
PATRICi22315117. VBILegPne33733_0893.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH15015.1 .
RefSeqi YP_126143.1. NC_006369.1.

3D structure databases

ProteinModelPortali Q5WYF5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 297245.lpl0781.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH15015 ; CAH15015 ; lpl0781 .
GeneIDi 3115445.
KEGGi lpf:lpl0781.
PATRICi 22315117. VBILegPne33733_0893.

Organism-specific databases

LegioListi lpl0781.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
KOi K03644.
OMAi HPHIPTK.
OrthoDBi EOG6038ZS.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .
BioCyci LPNE297245:GJD4-840-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiLIPA_LEGPL
AccessioniPrimary (citable) accession number: Q5WYF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 23, 2004
Last modified: October 29, 2014
This is version 70 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