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Protein

Lipoyl synthase, mitochondrial

Gene

HCBG_07690

Organism
Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum)
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

Pathwayi

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

  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:HCBG_07690
OrganismiAjellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic identifieri447093 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeHistoplasma
ProteomesiUP000001631 Componenti: 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 – 3737MitochondrionUniRule annotationAdd
BLAST
Chaini38 – 430393Lipoyl synthase, mitochondrialPRO_0000398246Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC0NXP6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiC0NXP6.
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.

C0NXP6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSAGKLRT LYSAHSSLSS LPPSARPTLQ LATLRSYATT TPHDSPIGNT
60 70 80 90 100
SNTPPTVKRP ATAFKDKLNA GPAFSDFVSG KKDEPLDPAE AYALKTALVG
110 120 130 140 150
PPGRKKEITR LPPWLKTAIP DSSNYKRIKN DLRGLNLHTV CEEARCPNIA
160 170 180 190 200
DCWGGSSKSA ATATIMLMGD TCTRGCRFCS VKTSNKPPPL DPHEPDNTAE
210 220 230 240 250
ALSRWGLGYV VLTSVDRDDL ADGGARHFAE TVMKIKQKAP NILVECLTGD
260 270 280 290 300
YAGDLDMVAL VANSGLDVFA HNVETVEALT PFVRDRRASF QQSLRVLKAA
310 320 330 340 350
KAAKPELITK TSLMLGLGET EAQLWDALRA LRAINVDVVT FGQYMRPTKR
360 370 380 390 400
HMAVHEYVRP DVFDLWKERA LEMGFLYCAS GPLVRSSYKA GEAFIENVLK
410 420 430
KRRGENAGSV NEKVTTSENV KKLVAGEAMM
Length:430
Mass (Da):46,821
Last modified:May 4, 2009 - v1
Checksum:iC0C098FB51E28C50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG663376 Genomic DNA. Translation: EEH03564.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG663376 Genomic DNA. Translation: EEH03564.1.

3D structure databases

ProteinModelPortaliC0NXP6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiC0NXP6.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: G186AR / H82 / ATCC MYA-2454 / RMSCC 2432.

Entry informationi

Entry nameiLIPA_AJECG
AccessioniPrimary (citable) accession number: C0NXP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 4, 2010
Last sequence update: May 4, 2009
Last modified: March 31, 2015
This is version 38 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.