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Q6CLS2

- LIPA_KLULA

UniProt

Q6CLS2 - LIPA_KLULA

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Protein

Lipoyl synthase, mitochondrial

Gene

KLLA0F00836g

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
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.

Cofactori

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 bindingi104 – 1041Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi109 – 1091Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi115 – 1151Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi135 – 1351Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi139 – 1391Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi142 – 1421Iron-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

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
Ordered Locus Names:KLLA0F00836g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Chromosome F

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 370Lipoyl synthase, mitochondrialPRO_0000398268
Transit peptidei1 – ?MitochondrionUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi28985.Q6CLS2.

Structurei

3D structure databases

ProteinModelPortaliQ6CLS2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiQ6CLS2.
KOiK03644.
OMAiHPHIPTK.
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.

Q6CLS2 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKPGIRSVQ KRFITETVVR STQPSVSRRR KTTHFTDKLN KGPSFEDFVN
60 70 80 90 100
GNAQKFTLDP LEKARQNSEE VQRLPTWLKV PIAKGSNFHK LKNDVKELKL
110 120 130 140 150
STVCEEAKCP NIGECWGGGD KSKATATIML LGDTCTRGCR FCSVKTNRKP
160 170 180 190 200
SAPDPTEPEN TAEAISRWGL GYVVLTTVDR DDLVDGGAYH LAETVQKIKQ
210 220 230 240 250
KAPNILVETL SGDFRGDLEM VKVMALSGLD VYAHNMETVE ALTPHVRDRR
260 270 280 290 300
ATYRQSLSVL ECAKKTVPTL VTKTSVMLGL GETDEQVLQT MKDLRAIGCD
310 320 330 340 350
VITFGQYMRP TKRHMKVVEY VTPEKFDYWK QKALELGFLY CASGPLVRSS
360 370
YKAGESFIEN VLRGRSRARI
Length:370
Mass (Da):41,470
Last modified:August 16, 2004 - v1
Checksum:i86A501949025496B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382126 Genomic DNA. Translation: CAG97824.1.
RefSeqiXP_455117.1. XM_455117.1.

Genome annotation databases

GeneIDi2895837.
KEGGikla:KLLA0F00836g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382126 Genomic DNA. Translation: CAG97824.1 .
RefSeqi XP_455117.1. XM_455117.1.

3D structure databases

ProteinModelPortali Q6CLS2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 28985.Q6CLS2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2895837.
KEGGi kla:KLLA0F00836g.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
InParanoidi Q6CLS2.
KOi K03644.
OMAi HPHIPTK.
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...

Entry informationi

Entry nameiLIPA_KLULA
AccessioniPrimary (citable) accession number: Q6CLS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 72 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3