Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

NCU00565

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
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 N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(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 (NCU00565)
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 bindingi142Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi147Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi153Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi173Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi177Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi180Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Ligand4Fe-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:NCU00565
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 1, Linkage Group I

Organism-specific databases

EuPathDBiFungiDB:NCU00565.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29MitochondrionUniRule annotationAdd BLAST29
ChainiPRO_000039827530 – 430Lipoyl synthase, mitochondrialAdd BLAST401

Structurei

3D structure databases

ProteinModelPortaliQ7SF84.
SMRiQ7SF84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998.
InParanoidiQ7SF84.
KOiK03644.
OrthoDBiEOG092C13O2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
PfamiView protein in Pfam
PF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
SFLDiSFLDG01058. lipoyl_synthase_like. 1 hit.
SFLDS00029. Radical_SAM. 1 hit.
SMARTiView protein in SMART
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7SF84-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPVPIQRL QAPLRRSLAR AAALSTRSYA TIPSGPSSQP TSQESSSAAS
60 70 80 90 100
ASAPATKPRP TYFKDTTLAS LDDFIANQSS AAPLAPSEAY TLRTAEVGPA
110 120 130 140 150
GKKRTITRLP EWLKTPIPSA GANPEFAKIK ADLRGLNLHT VCEEARCPNI
160 170 180 190 200
GECWGGSNKA AATATIMLMG DTCTRGCRFC SVKTSRKPPP LDPHEPENTA
210 220 230 240 250
EALARWGLGY VVLTSVDRDD LADGGARHFA ETIRRIKQKK PTLLVEALTG
260 270 280 290 300
DFAGDLDMVK IVAESGLDVY AHNVETVENL TPYVRDRRAT FRQSLKVLEH
310 320 330 340 350
VKKVRGKEGI ITKTSIMLGL GETEEELWEA LRELRKVDVD VVTFGQYMRP
360 370 380 390 400
TKRHLAVEKY ITPDEFELWR QRALDMGFLY CASGPLVRSS YKAGEAFIEN
410 420 430
VLRKRSGEKV VSEALGQAVA AEEATSVQSS
Length:430
Mass (Da):46,902
Last modified:December 15, 2003 - v1
Checksum:i74795BCD7AD9FCCE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002236 Genomic DNA. Translation: EAA35490.1.
RefSeqiXP_964726.1. XM_959633.3.

Genome annotation databases

EnsemblFungiiEAA35490; EAA35490; NCU00565.
GeneIDi3880875.
KEGGincr:NCU00565.

Similar proteinsi

Entry informationi

Entry nameiLIPA_NEUCR
AccessioniPrimary (citable) accession number: Q7SF84
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 15, 2003
Last modified: October 25, 2017
This is version 94 of the entry and version 1 of the sequence. See 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