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Protein

Lipoyl synthase

Gene

lipA

Organism
Caulobacter crescentus (strain ATCC 19089 / CB15)
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: protein 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)DescriptionActionsGraphical viewLength
Metal bindingi64Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi69Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi75Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi90Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi94Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi97Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

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

BioCyciCAULO:CC1735-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:CC_1735
OrganismiCaulobacter crescentus (strain ATCC 19089 / CB15)
Taxonomic identifieri190650 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
Proteomesi
  • UP000001816 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001023011 – 325Lipoyl synthaseAdd BLAST325

Interactioni

Protein-protein interaction databases

STRINGi190650.CC_1735.

Structurei

3D structure databases

ProteinModelPortaliQ9A7I8.
SMRiQ9A7I8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235998.
KOiK03644.
OMAiNVCTRSC.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. 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.

Q9A7I8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVIDTLKA RGSEDRAARH PEKQNRPDTP VLRKPEWLRV RAPGSGQYNE
60 70 80 90 100
TKGIVREHKL HTVCEEAACP NIGECWSQKH ATMMIMGEIC TRACAFCNVT
110 120 130 140 150
TGLPTQLDPD EPRRVAEAVA KMGLKHVVIT SVDRDDLLDG GARHFAEVVT
160 170 180 190 200
SIRAAAPGTT IEILTPDFLR KDGAENVVID SKPDVFNHNL ETVPRLYLKI
210 220 230 240 250
RPGARYYNSL RLLDRVKQRD PSQFTKSGLM VGLGETKEEV MQVMDDMRSA
260 270 280 290 300
GVDFITIGQY LQPTRKHAAI DRFVTPEEFK AYEAIARAKG FLMVSSSPLT
310 320
RSSHHAGEDF AKLQAARRAL DARTA
Length:325
Mass (Da):36,161
Last modified:June 1, 2001 - v1
Checksum:i2A1606CD9C3B6400
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005673 Genomic DNA. Translation: AAK23711.1.
PIRiC87464.
RefSeqiNP_420543.1. NC_002696.2.
WP_010919603.1. NC_002696.2.

Genome annotation databases

EnsemblBacteriaiAAK23711; AAK23711; CC_1735.
GeneIDi942082.
KEGGiccr:CC_1735.
PATRICi21300486. VBICauCre124313_1759.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005673 Genomic DNA. Translation: AAK23711.1.
PIRiC87464.
RefSeqiNP_420543.1. NC_002696.2.
WP_010919603.1. NC_002696.2.

3D structure databases

ProteinModelPortaliQ9A7I8.
SMRiQ9A7I8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190650.CC_1735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK23711; AAK23711; CC_1735.
GeneIDi942082.
KEGGiccr:CC_1735.
PATRICi21300486. VBICauCre124313_1759.

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235998.
KOiK03644.
OMAiNVCTRSC.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciCAULO:CC1735-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPA_CAUCR
AccessioniPrimary (citable) accession number: Q9A7I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 107 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

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 one 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.