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Protein

Lipoyl synthase, mitochondrial

Gene

BDBG_06713

Organism
Ajellomyces dermatitidis (strain SLH14081) (Blastomyces dermatitidis)
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 + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

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

Pathway:iprotein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Octanoyltransferase (BDBG_06737)
  2. Lipoyl synthase, mitochondrial (BDBG_06713)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi141 – 1411Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi146 – 1461Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi152 – 1521Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi172 – 1721Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi176 – 1761Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi179 – 1791Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

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:BDBG_06713
OrganismiAjellomyces dermatitidis (strain SLH14081) (Blastomyces dermatitidis)
Taxonomic identifieri559298 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeBlastomyces
ProteomesiUP000002038 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionUniRule annotationAdd
BLAST
Chaini38 – 430393Lipoyl synthase, mitochondrialPRO_0000398249Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi559298.XP_002623274.1.

Structurei

3D structure databases

ProteinModelPortaliC5JVC1.
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]
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.

C5JVC1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTGKLRT LFSAHSSLSA RPSSALPALR LTILRSYATT TPPDSSISNP
60 70 80 90 100
SNPSTTVKRP PTAFKDKLNA GPAFSDFVSG KKDEPLDPAE AYALKTALVG
110 120 130 140 150
PAGRKKEITR LPSWLKTPIP DSSNYKRIKN DLRGLNLHTV CEEARCPNIS
160 170 180 190 200
DCWGGSSKSA ATATIMLMGD TCTRGCRFCS VKTSNKPPPL DPHEPENTAE
210 220 230 240 250
ALSRWGLGYV VLTSVDRDDL ADGGARHFAE TVLKIKQKAP NILVECLTGD
260 270 280 290 300
YAGDLEMVAL VANSGLDVYA HNVETVEALT PFVRDRRATF QQSLRVLKAA
310 320 330 340 350
KATKPELITK TSLMLGLGET EAQLWDTLRA LRAIDVDVVT FGQYMRPTKR
360 370 380 390 400
HMAVHEYVRP DVFDMWKERA LEMGFLYCAS GPLVRSSYKA GEAFIENVLK
410 420 430
KKRGKNVGSA SGKGTTSENV EKLVAGEAVR
Length:430
Mass (Da):46,760
Last modified:July 28, 2009 - v1
Checksum:i029D26CA5B9FA368
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG657461 Genomic DNA. Translation: EEQ71522.1.
RefSeqiXP_002623274.1. XM_002623228.1.

Genome annotation databases

GeneIDi8503147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG657461 Genomic DNA. Translation: EEQ71522.1.
RefSeqiXP_002623274.1. XM_002623228.1.

3D structure databases

ProteinModelPortaliC5JVC1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi559298.XP_002623274.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8503147.

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]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Blastomyces dermatitidis strain SLH14081."
    Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N., Sykes S.
    , Galagan J.E., Nusbaum C., Birren B.W.
    Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SLH14081.

Entry informationi

Entry nameiLIPA_AJEDS
AccessioniPrimary (citable) accession number: C5JVC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: June 24, 2015
This is version 36 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

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.