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Protein

Lipoyl synthase, mitochondrial

Gene

TSTA_101110

Organism
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
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: protein 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. no protein annotated in this organism
  2. Lipoyl synthase, mitochondrial (TSTA_101110)
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)DescriptionActionsGraphical viewLength
Metal bindingi146Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi151Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi157Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi177Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi181Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi184Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

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:TSTA_101110
OrganismiTalaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
Taxonomic identifieri441959 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces
Proteomesi
  • UP000001745 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:TSTA_101110.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34MitochondrionUniRule annotationAdd BLAST34
ChainiPRO_000039829435 – 422Lipoyl synthase, mitochondrialAdd BLAST388

Interactioni

Protein-protein interaction databases

STRINGi441959.XP_002486109.1.

Structurei

3D structure databases

ProteinModelPortaliB8MLU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
InParanoidiB8MLU5.
OrthoDBiEOG092C13O2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. 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.

B8MLU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASSTRLRC LYASSAPAWK KSPSQSIISL SRHYATTSST TPSLNPDESS
60 70 80 90 100
SSSSSTIPKR RKTTTFRDKL NAGPSFADFV TGGNGNNASL DPEEAYALEK
110 120 130 140 150
VMIPGPAGRK KEHTRLPSWL KTPIPDSTNY KRIKKDLRGL DLHTVCEEAR
160 170 180 190 200
CPNISDCWGG SDKSAATATI MLMGDTCTRG CRFCSVKTLR TPGPLDPHEP
210 220 230 240 250
ENTAEALSRW GLGDDLPDGG AHHFAETVIK IKQKAPGILV ECLTGDFAGD
260 270 280 290 300
LDMVSLVAKS GLDVYAHNVE TVEALTPHVR DRRATFKQSL RVLEAAKRAK
310 320 330 340 350
PSLITKTSMM LGFGETEDQL WDALRQLRAS NVDVVTFGQY MRPTKRHMAV
360 370 380 390 400
HEYVTPDKFE LWRQRALEMG FLYVASGPLV RSSYKAGEAF IENVLKKRRG
410 420
VGNTPGAEVA SAKDVPVDVL GK
Length:422
Mass (Da):46,127
Last modified:March 3, 2009 - v1
Checksum:i9F9C7823717AFD54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ962658 Genomic DNA. Translation: EED13871.1.
RefSeqiXP_002486109.1. XM_002486064.1.

Genome annotation databases

EnsemblFungiiEED13871; EED13871; TSTA_101110.
GeneIDi8101799.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ962658 Genomic DNA. Translation: EED13871.1.
RefSeqiXP_002486109.1. XM_002486064.1.

3D structure databases

ProteinModelPortaliB8MLU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi441959.XP_002486109.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEED13871; EED13871; TSTA_101110.
GeneIDi8101799.

Organism-specific databases

EuPathDBiFungiDB:TSTA_101110.

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
InParanoidiB8MLU5.
OrthoDBiEOG092C13O2.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPA_TALSN
AccessioniPrimary (citable) accession number: B8MLU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 3, 2009
Last modified: September 7, 2016
This is version 43 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

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 one 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.