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Q477G5

- LIPA_CUPPJ

UniProt

Q477G5 - LIPA_CUPPJ

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Protein

Lipoyl synthase

Gene

lipA

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
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

[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 bindingi78 – 781Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi83 – 831Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi89 – 891Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi104 – 1041Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi108 – 1081Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi111 – 1111Iron-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

BioCyciCPIN264198:GIW3-86-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:Reut_A0086
OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Taxonomic identifieri264198 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000002697: Chromosome 1

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 – 331331Lipoyl synthasePRO_0000325299Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi264198.Reut_A0086.

Structurei

3D structure databases

ProteinModelPortaliQ477G5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
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.

Q477G5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDALIASSS EAPQSPAEQY DPTRKQKSAD KTARIPIKIV PAEKLKKPDW
60 70 80 90 100
IRVKAATGNS RFYEIKDILR ANNLVTVCEE ASCPNIGECF GKGTATFMIM
110 120 130 140 150
GDKCTRRCPF CDVGHGRPDP LDVNEPGNLA RTIAQLKLNY VVITSVDRDD
160 170 180 190 200
LRDGGAQHYV DCISQTRELS PATRIEVLVP DFRGRLDKAL DILQACPPDV
210 220 230 240 250
MNHNMETVPR LYKQARPGAD YAHSLKLLQE FKRRNPNVPT KSGLMVGLGE
260 270 280 290 300
TDEEILEVMR DMRAHDIDML TIGQYLAPSN HHLPVLRYVH PDTFKMFEEE
310 320 330
AYKMGFTHAA VGAMVRSSYH ADQQAHQAGF A
Length:331
Mass (Da):36,979
Last modified:September 13, 2005 - v1
Checksum:iD0A3DAB597D58ADC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA. Translation: AAZ59468.1.
RefSeqiYP_294312.1. NC_007347.1.

Genome annotation databases

EnsemblBacteriaiAAZ59468; AAZ59468; Reut_A0086.
GeneIDi3611152.
KEGGireu:Reut_A0086.
PATRICi20225605. VBIRalEut24049_0681.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA. Translation: AAZ59468.1 .
RefSeqi YP_294312.1. NC_007347.1.

3D structure databases

ProteinModelPortali Q477G5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264198.Reut_A0086.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ59468 ; AAZ59468 ; Reut_A0086 .
GeneIDi 3611152.
KEGGi reu:Reut_A0086.
PATRICi 20225605. VBIRalEut24049_0681.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235997.
KOi K03644.
OMAi HPHIPTK.
OrthoDBi EOG6038ZS.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .
BioCyci CPIN264198:GIW3-86-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. "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JMP134 / LMG 1197.

Entry informationi

Entry nameiLIPA_CUPPJ
AccessioniPrimary (citable) accession number: Q477G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: September 13, 2005
Last modified: November 26, 2014
This is version 65 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