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
Staphylococcus haemolyticus (strain JCSC1435)
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 the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation 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 pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi46 – 461Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi52 – 521Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi68 – 681Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi72 – 721Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi75 – 751Iron-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

BioCyciSHAE279808:GJX7-2085-MONOMER.

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:SH2028
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543 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 – 306306Lipoyl synthasePRO_0000325313Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi279808.SH2028.

Structurei

3D structure databases

ProteinModelPortaliQ4L4T8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
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.

Q4L4T8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKNEEILR KPDWLKIKLN TNENYIGLKK MMREKNLHTV CEEAKCPNIH
60 70 80 90 100
ECWGARRTAT FMILGAVCTR ACRFCAVKTG LPNELDLNEP ERVAESVELM
110 120 130 140 150
NLKHVVITAV ARDDLRDAGS NVYAETVRKV RERNPFTTIE ILPSDMGGDY
160 170 180 190 200
EALETLMASK PDILNHNIET VRRLTPRVRA RATYERTLEF LRRSKELQPD
210 220 230 240 250
IPTKSSLMVG LGETIEEIYE TMDDLRANDV DILTIGQYLQ PSRKHLKVEK
260 270 280 290 300
YYTPLEFGKL RKVAMDKGFK HCEAGPMVRS SYHADEQVNE AAKEKHRLGE

EKLQQN
Length:306
Mass (Da):35,161
Last modified:March 18, 2008 - v2
Checksum:i1F3B0F228EE955F1
GO

Sequence cautioni

The sequence BAE05337.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05337.1. Different initiation.
RefSeqiWP_029376689.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05337; BAE05337; SH2028.
GeneIDi24247662.
KEGGisha:SH2028.
PATRICi19620157. VBIStaHae67511_1999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05337.1. Different initiation.
RefSeqiWP_029376689.1. NC_007168.1.

3D structure databases

ProteinModelPortaliQ4L4T8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279808.SH2028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE05337; BAE05337; SH2028.
GeneIDi24247662.
KEGGisha:SH2028.
PATRICi19620157. VBIStaHae67511_1999.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

BioCyciSHAE279808:GJX7-2085-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. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiLIPA_STAHJ
AccessioniPrimary (citable) accession number: Q4L4T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: July 22, 2015
This is version 73 of the entry and version 2 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.