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Protein

Lipoyl synthase 2

Gene

lipA2

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
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 N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(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 2 (lipA2), Lipoyl synthase 1 (lipA1)
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 bindingi67Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi72Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi78Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi93Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi97Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi100Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase 2UniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-syn 2UniRule annotation
Lipoate synthase 2UniRule annotation
Lipoic acid synthase 2UniRule annotation
Sulfur insertion protein lipA2
Gene namesi
Name:lipA2UniRule annotation
Synonyms:lipA
Ordered Locus Names:bll3717
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
Proteomesi
  • UP000002526 Componenti: Chromosome

Subcellular locationi

Q89NW6:
  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001022941 – 322Lipoyl synthase 2Add BLAST322

Interactioni

Protein-protein interaction databases

STRINGi224911.bll3717.

Structurei

3D structure databases

ProteinModelPortaliQ89NW6.
SMRiQ89NW6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0G. Bacteria.
COG0320. LUCA.
HOGENOMiHOG000235997.
InParanoidiQ89NW6.
KOiK03644.
OMAiIRCESKD.
OrthoDBiPOG091H069D.
PhylomeDBiQ89NW6.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
PfamiView protein in Pfam
PF04055. Radical_SAM. 1 hit.
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SFLDiSFLDG01058. lipoyl_synthase_like. 1 hit.
SFLDS00029. Radical_SAM. 1 hit.
SMARTiView protein in SMART
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q89NW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVILDLLNN DPRTTQRTER PRHPEKANRP DTPMESRPAW IRVKAPGSAQ
60 70 80 90 100
WTETQRIVRE NKLVTVCEEA SCPNIGECWA KKHATFMIMG DTCTRACAFC
110 120 130 140 150
NVRTGLPGPL DADEPGKVAD AVAKLGLEHV VVTSVDRDDL ADGGAAHFAA
160 170 180 190 200
TIAAIRAMSP ATSIEILTPD FLRKHGALET VVAARPDVLN HNLETVPSKY
210 220 230 240 250
LAVRPGARYF HSVRLLQRAK ELDPRIFTKS GIMVGLGEDR SEVLQLMDDL
260 270 280 290 300
RSADVDFLTI GQYLQPTRKH HAVMRFVPPD EFEAYEKTAY AKGFLMVSAT
310 320
PLTRSSHHAG DDFRKLRERR RA
Length:322
Mass (Da):35,885
Last modified:June 1, 2003 - v1
Checksum:iDC515282CE94A4E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000040 Genomic DNA. Translation: BAC48982.1.
RefSeqiNP_770357.1. NC_004463.1.
WP_011086498.1. NZ_CP011360.1.

Genome annotation databases

EnsemblBacteriaiBAC48982; BAC48982; BAC48982.
GeneIDi1052093.
KEGGibja:bll3717.
PATRICifig|224911.44.peg.3381.

Similar proteinsi

Entry informationi

Entry nameiLIPA2_BRADU
AccessioniPrimary (citable) accession number: Q89NW6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: June 1, 2003
Last modified: October 25, 2017
This is version 91 of the entry and version 1 of the sequence. See 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