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P0CH67

- LIPA_CANAL

UniProt

P0CH67 - LIPA_CANAL

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Protein
Lipoyl synthase, mitochondrial
Gene
LAB5, LIS1, CaO19.10290, CaO19.2774
Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
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
Name:LAB5
Synonyms:LIS1
ORF Names:CaO19.10290, CaO19.2774
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0004271. orf19.2774.

Subcellular locationi

Mitochondrion Reviewed prediction 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
Transit peptidei1 – 2121Mitochondrion Reviewed prediction
Add
BLAST
Chaini22 – 386365Lipoyl synthase, mitochondrialUniRule annotation
PRO_0000398258Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP0CH67.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998.
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.

P0CH67-1 [UniParc]FASTAAdd to Basket

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MISRNSILLR RLYPTTIIRT LATDATESTS VKTKRRRTIF TDELNKGPSF    50
DDFVSGKAKD MLEDPLETAR KDPNAKLPSW LKVPIPKGKS FHNVKKDVRE 100
LKLATVCEEA KCPNIGECWG GKKSEATATI MLLGDTCTRG CRFCSVKTNR 150
KPAAPDPMEP ENTAEAISRW GLGYVVLTTV DRDDLVDGGA RHLAETVQKI 200
KQKAPQILVE VLGGDFRGDL SMVEILADSG LDVYAHNLET VEALTPHIRD 250
RRATYRQSLA VLERAKQTNS SLITKTSLML GFGETDDQVL QTLRDLREIG 300
CDVVTFGQYM RPTKRHMKVV EYIKPEKFDY WRDTALDMGF LYVASGPLVR 350
SSYKAGEAFI ENVLKKRKHN VGETPRLAQE IKPSIY 386
Length:386
Mass (Da):43,339
Last modified:October 5, 2010 - v1
Checksum:i84ACA0D6EAECC691
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000025 Genomic DNA. Translation: EAL01446.1.
AACQ01000023 Genomic DNA. Translation: EAL01684.1.
RefSeqiXP_720294.1. XM_715201.1.
XP_720524.1. XM_715431.1.

Genome annotation databases

GeneIDi3637893.
3638133.
KEGGical:CaO19.10290.
cal:CaO19.2774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000025 Genomic DNA. Translation: EAL01446.1 .
AACQ01000023 Genomic DNA. Translation: EAL01684.1 .
RefSeqi XP_720294.1. XM_715201.1.
XP_720524.1. XM_715431.1.

3D structure databases

ProteinModelPortali P0CH67.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3637893.
3638133.
KEGGi cal:CaO19.10290.
cal:CaO19.2774.

Organism-specific databases

CGDi CAL0004271. orf19.2774.

Phylogenomic databases

HOGENOMi HOG000235998.
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: SC5314 / ATCC MYA-2876.

Entry informationi

Entry nameiLIPA_CANAL
AccessioniPrimary (citable) accession number: P0CH67
Secondary accession number(s): Q5AF33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 5, 2010
Last modified: June 11, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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