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Protein

Lipoyl synthase, mitochondrial

Gene

PICST_86231

Organism
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis)
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. Octanoyltransferase (LAB2)
  2. Lipoyl synthase, mitochondrial (PICST_86231)
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 bindingi117Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi122Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi128Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi147Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi151Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi154Iron-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:PICST_86231
OrganismiScheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis)
Taxonomic identifieri322104 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeScheffersomyces
Proteomesi
  • UP000002258 Componentsi: Chromosome 1, 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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 32MitochondrionUniRule annotationAdd BLAST32
ChainiPRO_000039828333 – 398Lipoyl synthase, mitochondrialAdd BLAST366

Interactioni

Protein-protein interaction databases

STRINGi322104.XP_001387968.2.

Structurei

3D structure databases

ProteinModelPortaliA3GGJ5.
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.
HOGENOMiHOG000235998.
InParanoidiA3GGJ5.
KOiK03644.
OMAiVQKYWTP.
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.

A3GGJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIALRVHNTR VVSRSLTVWT RPSPTLTLSR SLATESDALD KPKTRRRKTV
60 70 80 90 100
FTDALNSGPS FDDFVSGKAS EIMDPLEAAR KDPNQRLPSW LKVPIPKGKS
110 120 130 140 150
YHNVKKDVRE LKLATVCEEA KCPNIGECWG GKKSEATATI MLLGDTCTRG
160 170 180 190 200
CRFCSVKTNR NPAKPDPMEP ENTAEAISRW GLGYVVLTTV DRDDLADGGA
210 220 230 240 250
HHLAETVMKI KQKAPQILVE VLGGDFRGDL DMATVLAKSG LDVYAHNLET
260 270 280 290 300
VEALTPFVRD RRATYRQSLS VLQRAKETKS SLVTKTSLML GLGETDEQIL
310 320 330 340 350
QTLKDLREIN CDVVTFGQYM RPTKRHMKVV EYVTPEKFDY WRDTALEMGF
360 370 380 390
LYVASGPLVR SSYKAGEAFI ENVIRKRRHN VGEAPRLAQE IQPKIFRE
Length:398
Mass (Da):44,638
Last modified:June 16, 2009 - v2
Checksum:iA10E1466D9D973B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAVQ01000001 Genomic DNA. Translation: EAZ63945.2.
RefSeqiXP_001387968.2. XM_001387931.1.

Genome annotation databases

EnsemblFungiiEAZ63945; EAZ63945; PICST_86231.
GeneIDi4851394.
KEGGipic:PICST_86231.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAVQ01000001 Genomic DNA. Translation: EAZ63945.2.
RefSeqiXP_001387968.2. XM_001387931.1.

3D structure databases

ProteinModelPortaliA3GGJ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322104.XP_001387968.2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAZ63945; EAZ63945; PICST_86231.
GeneIDi4851394.
KEGGipic:PICST_86231.

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
HOGENOMiHOG000235998.
InParanoidiA3GGJ5.
KOiK03644.
OMAiVQKYWTP.
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_PICST
AccessioniPrimary (citable) accession number: A3GGJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 16, 2009
Last modified: September 7, 2016
This is version 66 of the entry and version 2 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.