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Protein

Lipoyl synthase, mitochondrial

Gene

AN9486

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: -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 + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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 (AN4781.2), Octanoyltransferase (ANIA_04781)
  2. Lipoyl synthase, mitochondrial (AN9486)
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 bindingi133Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi138Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi144Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi164Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi168Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi171Iron-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:AN9486
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome III
  • UP000005890 Componenti: Unassembled WGS sequence

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 – 33MitochondrionUniRule annotationAdd BLAST33
ChainiPRO_000039826734 – 413Lipoyl synthase, mitochondrialAdd BLAST380

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00005653

Structurei

3D structure databases

ProteinModelPortaliQ5AQE4
SMRiQ5AQE4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998
InParanoidiQ5AQE4
KOiK03644
OMAiPYCDIDF
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
PIRSFiPIRSF005963 Lipoyl_synth, 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.

Q5AQE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATNRFRA LYSSSRVATP QAGSASYLSY RGYATTDPSS ATGGASTAGK
60 70 80 90 100
RRTTFTDKLN AGPSFGDFVS GGRDNAPLDP SEAYALKTAL VGPAGRKKEM
110 120 130 140 150
TRLPSWLKTP IPDSKNYQRL KKDLRGLNLH TVCEEARCPN ISDCWGGGDK
160 170 180 190 200
AAATATIMLM GDTCTRGCRF CSVKTSRAPP PLDPHEPENT AEAISRWGLG
210 220 230 240 250
YVVLTSVDRD DLADGGARHF AETVIKIKQK APNILVECLT GDYAGDLEMV
260 270 280 290 300
GVVARSGLDV YAHNVETVEA LTPHVRDRRA TFQQSLRVLE AAKKAKPSLI
310 320 330 340 350
TKTSLMLGLG ETEEQLWDAL RQLRAVNVDV VTFGQYMRPT KRHMAVHEYV
360 370 380 390 400
TPDRFELWRQ RALDMGFLYC ASGPLVRSSY KAGEAFIENV LKKRRSGAPE
410
VSHNTVPVDE ATR
Length:413
Mass (Da):45,118
Last modified:April 26, 2005 - v1
Checksum:iE149F64B033A8735
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000201 Genomic DNA Translation: EAA66777.1
BN001303 Genomic DNA Translation: CBF76818.1
RefSeqiXP_868868.1, XM_863775.1

Genome annotation databases

EnsemblFungiiCADANIAT00005653; CADANIAP00005653; CADANIAG00005653
EAA66777; EAA66777; AN9486.2
GeneIDi3684084
KEGGiani:AN9486.2

Similar proteinsi

Entry informationi

Entry nameiLIPA_EMENI
AccessioniPrimary (citable) accession number: Q5AQE4
Secondary accession number(s): C8VAP9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 26, 2005
Last modified: May 23, 2018
This is version 82 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
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Main funding by: National Institutes of Health