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A5DGI1

- LIPA_PICGU

UniProt

A5DGI1 - LIPA_PICGU

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Protein
Lipoyl synthase, mitochondrial
Gene
PGUG_02382
Organism
Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
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 By similarity.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 By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi112 – 1121Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi118 – 1181Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi137 – 1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi144 – 1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

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

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrial (EC:2.8.1.8)
Alternative name(s):
Lipoate synthase
Short name:
LS
Short name:
Lip-syn
Lipoic acid synthase
Gene namesi
ORF Names:PGUG_02382
OrganismiMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Taxonomic identifieri294746 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeMeyerozyma
ProteomesiUP000001997: Unassembled WGS sequence

Subcellular locationi

Mitochondrion By similarity UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 385Lipoyl synthase, mitochondrialUniRule annotationPRO_0000398281
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Interactioni

Protein-protein interaction databases

STRINGi4929.A5DGI1.

Structurei

3D structure databases

ProteinModelPortaliA5DGI1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
KOiK03644.
OrthoDBiEOG79KPR7.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

A5DGI1-1 [UniParc]FASTAAdd to Basket

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MVPVRGQITA FRCSQNPTKT IWRTLATAEP PKPKRKRTMF TDKLNQGPSF    50
ADFVSGKASN MTIDPLEAAR QDPDQRLPSW LKVPIPKGKS FHTLKKDVRE 100
LKLATVCEEA KCPNIGECWG GKKSEATATI MLMGDTCTRG CRFCSVKTSR 150
KPAPPDPMEP ENTAEAISRW GLGYVVLTTV DRDDLVDGGA HHLAETVRKI 200
KEKAPQILVE VLGGDFRGDL DMASVLARSG LDVYAHNIET VEDLTPHVRD 250
RRATYRQSLS ILQRAKETKP SLVTKTSMML GFGETDEQIM QTLRDLREIK 300
CDVVTFGQYM RPTKRHMKVV EYVTPEKFDY WRDTALKMGF LYVASGPLVR 350
SSYKAGEAFI ENVIRKRNHN VGETPRLESA SAAQL 385
Length:385
Mass (Da):43,175
Last modified:July 22, 2008 - v2
Checksum:iF348661FA3522D91
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH408157 Genomic DNA. Translation: EDK38284.2.
RefSeqiXP_001484653.1. XM_001484603.1.

Genome annotation databases

GeneIDi5126776.
KEGGipgu:PGUG_02382.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH408157 Genomic DNA. Translation: EDK38284.2 .
RefSeqi XP_001484653.1. XM_001484603.1.

3D structure databases

ProteinModelPortali A5DGI1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4929.A5DGI1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5126776.
KEGGi pgu:PGUG_02382.

Phylogenomic databases

eggNOGi COG0320.
KOi K03644.
OrthoDBi EOG79KPR7.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324.

Entry informationi

Entry nameiLIPA_PICGU
AccessioniPrimary (citable) accession number: A5DGI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 22, 2008
Last modified: June 11, 2014
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

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