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Protein

Lipoyl synthase, mitochondrial

Gene

AFUB_042490

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
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 (AFUB_042370)
  2. Lipoyl synthase, mitochondrial (AFUB_042490)
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 bindingi131Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi136Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi142Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi162Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi166Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi169Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

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:AFUB_042490
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001699 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 – 31MitochondrionUniRule annotationAdd BLAST31
ChainiPRO_000039825432 – 414Lipoyl synthase, mitochondrialAdd BLAST383

Structurei

3D structure databases

ProteinModelPortaliB0XYY2
SMRiB0XYY2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998
OrthoDBiEOG092C13O2
PhylomeDBiB0XYY2

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.

B0XYY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSTSHFRS LCASRPLSRT AIVGHISCRS YATTEPSPSA TSTSTTTTAR
60 70 80 90 100
RRTTFKDKLN AGPSFADFVG NGNTPLDPSE AYALKTALVG PAGRKKEMTR
110 120 130 140 150
LPSWLKTPIP DSKNYQRLKK DLRGLNLHTV CEEARCPNIS DCWGGSDKSA
160 170 180 190 200
ATATIMLMGD TCTRGCRFCS VKTSRTPAPL DPHEPENTAE AISRWGLGYV
210 220 230 240 250
VLTSVDRDDL ADGGARHFAE TVMKIKQKAP SILVECLTGD YAGDLEMVKL
260 270 280 290 300
VARSGLDVYA HNVETVEALT PQVRDRRANF QQSIRVLEAA KNAQPSLITK
310 320 330 340 350
TSLMLGLGET DDQLWDALRQ LRAANVDVVT FGQYMRPTKR HMAVHEYVTP
360 370 380 390 400
DRFELWRQRA LDMGFLYCAS GPLVRSSYKA GEAFIENVLK KRRATSGGTE
410
TVGVRPVTVD EVTR
Length:414
Mass (Da):45,479
Last modified:April 8, 2008 - v1
Checksum:i2E3D2BEA2E111ECA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499596 Genomic DNA Translation: EDP53078.1

Genome annotation databases

EnsemblFungiiCADAFUBT00004238; CADAFUBP00004166; CADAFUBG00004238

Similar proteinsi

Entry informationi

Entry nameiLIPA_ASPFC
AccessioniPrimary (citable) accession number: B0XYY2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 8, 2008
Last modified: May 23, 2018
This is version 51 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

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