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Protein

Lipoyl synthase, mitochondrial

Gene

DEHA2G18854g

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
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 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

[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 bindingi112 – 1121Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi117 – 1171Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi123 – 1231Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi142 – 1421Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi146 – 1461Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi149 – 1491Iron-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:DEHA2G18854g
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
ProteomesiUP000000599: Chromosome G

Subcellular locationi

Mitochondrion 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 – 1414MitochondrionUniRule annotationAdd
BLAST
Chaini15 – 395381Lipoyl synthase, mitochondrialPRO_0000398266Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi4959.B5RUV1.

Structurei

3D structure databases

ProteinModelPortaliB5RUV1.
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.
InParanoidiB5RUV1.
KOiK03644.
OMAiEEYVTPE.
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.

B5RUV1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MISLRSISRS PAVQPARIYR TLATADTSGI NEQAKPKTKR KKTVFSDSLN
60 70 80 90 100
KGPSFEDFVN GKAADMLVDP LEAARQDPNQ RLPKWLKVPI PKGKSFNNLK
110 120 130 140 150
NDVRELKLAT VCEEAKCPNI GECWGGKKSE ATATIMLMGD TCTRGCRFCS
160 170 180 190 200
VKTSRAPAKP DPMEPENTAE AISRWGLGYV VLTTVDRDDL VDGGANHLAE
210 220 230 240 250
TVRKIKEKAP QILVEVLGGD FRGDLDMAAI LARSGLDVYA HNIETVEALT
260 270 280 290 300
PYVRDRRATY RQSLSILNKA KETKPSLVTK TSLMLGFGET DEQIMQTLKD
310 320 330 340 350
LREIKCDVVT FGQYMRPTKR HMKVVDYVKP EKFDYWRDTA LQMGFLYVAS
360 370 380 390
GPLVRSSYKA GEAFIENVIR KRRHNVGETP RLAQEVNPKI ISQSI
Length:395
Mass (Da):44,126
Last modified:November 4, 2008 - v1
Checksum:i0E99DCBC39A30A45
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382139 Genomic DNA. Translation: CAR65995.1.
RefSeqiXP_002770663.1. XM_002770617.1.

Genome annotation databases

GeneIDi8999246.
KEGGidha:DEHA2G18854g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382139 Genomic DNA. Translation: CAR65995.1.
RefSeqiXP_002770663.1. XM_002770617.1.

3D structure databases

ProteinModelPortaliB5RUV1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4959.B5RUV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8999246.
KEGGidha:DEHA2G18854g.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiB5RUV1.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG79KPR7.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPA_DEBHA
AccessioniPrimary (citable) accession number: B5RUV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: November 4, 2008
Last modified: January 7, 2015
This is version 45 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.