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Protein

Lipoyl synthase, mitochondrial

Gene

AFLA_100710

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
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 (AFLA_100850)
  2. Lipoyl synthase, mitochondrial (AFLA_100710)
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 bindingi132Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi137Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi143Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi163Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi167Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi170Iron-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:AFLA_100710
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001875 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AFLA_100710

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 – 32MitochondrionUniRule annotationAdd BLAST32
ChainiPRO_000039825233 – 415Lipoyl synthase, mitochondrialAdd BLAST383

Proteomic databases

PRIDEiB8NUL8

Interactioni

Protein-protein interaction databases

STRINGi5059.CADAFLAP00011808

Structurei

3D structure databases

SMRiB8NUL8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998
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.

B8NUL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTNRLRF LYSSARTVPQ TGSITPISRR TYATTEPSPS ATGAPATARK
60 70 80 90 100
RTNFTDKLNA GPSFADFVSG GEDNTPLEPS EAYALKTAMV GPAGRKKEMT
110 120 130 140 150
RLPSWLKTPI PDSKNYQRLK KDLRGLNLHT VCEEARCPNI SDCWGGSDKS
160 170 180 190 200
AATATIMLMG DTCTRGCRFC SVKTNRRPPP LDPHEPENTA EAISRWSLGY
210 220 230 240 250
VVLTSVDRDD LADGGARHFA ETVIKIKQKK PSMLVECLTG DYLGDLEMVK
260 270 280 290 300
LVARSGLDVY AHNVETVEAL TPFVRDRRAT FQQSLRVLEA AKQARPDLIT
310 320 330 340 350
KTSLMLGFGE TEEQLWDALR QLRSVGVDVV TFGQYMRPTK RHMPVHEYVT
360 370 380 390 400
PDQFELWRQR ALDMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAAGTAG
410
ESVTDSKAAV DEATR
Length:415
Mass (Da):45,848
Last modified:March 3, 2009 - v1
Checksum:i6BFF144A44D5C296
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963484 Genomic DNA Translation: EED46407.1
RefSeqiXP_002383943.1, XM_002383902.1

Genome annotation databases

EnsemblFungiiEED46407; EED46407; AFLA_100710
GeneIDi7912952
KEGGiafv:AFLA_100710

Similar proteinsi

Entry informationi

Entry nameiLIPA_ASPFN
AccessioniPrimary (citable) accession number: B8NUL8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 3, 2009
Last modified: May 23, 2018
This is version 56 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

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