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Protein

Lipoyl synthase, mitochondrial

Gene

MCYG_08114

Organism
Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis)
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 bindingi129 – 1291Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi134 – 1341Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi140 – 1401Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi160 – 1601Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi164 – 1641Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi167 – 1671Iron-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
ORF Names:MCYG_08114
OrganismiArthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis)
Taxonomic identifieri554155 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeArthroderma
ProteomesiUP000002035: Unassembled WGS sequence

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 – 2929MitochondrionUniRule annotationAdd
BLAST
Chaini30 – 410381Lipoyl synthase, mitochondrialPRO_0000398272Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC5FZJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

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.

C5FZJ2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASTTVCSAA RIRVASSQVL RSIANTRTYA TTSPESSIPE TKPTAKRTPT
60 70 80 90 100
TFKDKLNKGP SFSDFIGGAT EPPLSPDEAY ALKTALVGPA GKKKEITRLP
110 120 130 140 150
SWLKTPIPDS SSYKKIKNDL RGLNLHTVCE EARCPNISEC WGGGSKAAAT
160 170 180 190 200
ATIMLMGDTC TRGCRFCSVK TSRTPPPLDP HEPENTAEAL SRWGLGYVVL
210 220 230 240 250
TAVDRDDLVD GGARHFAETV RRIKGKAPNI LVECLTGDFS GDMEMVSLMA
260 270 280 290 300
ESGMDVFAHN VETVEALTPF VRDRRASFQQ SLSVLRGAKA ANPELITKTS
310 320 330 340 350
LMLGLGETKE QVLDALKQLR ASQVDVVTFG QYMRPTKRHM AVHEYVRPDV
360 370 380 390 400
FDMWKEKAME MGFLYCASGP LVRSSYKAGE AFIENVLKKR AKERIGGAVE
410
DSVKGKDVLL
Length:410
Mass (Da):44,727
Last modified:July 28, 2009 - v1
Checksum:iB3FAF375C58B00DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS995708 Genomic DNA. Translation: EEQ35295.1.
RefSeqiXP_002843031.1. XM_002842985.1.

Genome annotation databases

GeneIDi9226245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS995708 Genomic DNA. Translation: EEQ35295.1.
RefSeqiXP_002843031.1. XM_002842985.1.

3D structure databases

ProteinModelPortaliC5FZJ2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9226245.

Phylogenomic databases

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4605 / CBS 113480.

Entry informationi

Entry nameiLIPA_ARTOC
AccessioniPrimary (citable) accession number: C5FZJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: January 7, 2015
This is version 37 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.