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Protein

Lipoyl synthase, mitochondrial

Gene

SMAC_01256

Organism
Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
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. no protein annotated in this organism
  2. Lipoyl synthase, mitochondrial (SMAC_01256)
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 bindingi157Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi162Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi168Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi188Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi192Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi195Iron-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:SMAC_01256
OrganismiSordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
Taxonomic identifieri771870 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeSordaria
Proteomesi
  • UP000001881 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:SMAC_01256

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 – 40MitochondrionUniRule annotationAdd BLAST40
ChainiPRO_000039829341 – 445Lipoyl synthase, mitochondrialAdd BLAST405

Proteomic databases

PRIDEiD1Z4I6

Interactioni

Protein-protein interaction databases

STRINGi771870.XP_003352422.1

Structurei

3D structure databases

ProteinModelPortaliD1Z4I6
SMRiD1Z4I6
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
InParanoidiD1Z4I6
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.

D1Z4I6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPGSWRVIT HYGFTGPIQR LQAPLRRSLA RAAALSTRSY ATIPSAPSSQ
60 70 80 90 100
PTSQESSPAA SASASASAPA TKPRPTYFKD TTLASLDDFI ANQSSAAPLA
110 120 130 140 150
PSEAYTLRTA QVGPAGKKRT ITRLPEWLKT PIPSAGANPE FAKIKADLRG
160 170 180 190 200
LNLHTVCEEA RCPNIGECWG GSNKAAATAT IMLMGDTCTR GCRFCSVKTS
210 220 230 240 250
RKPPPLDPHE PENTAEALAR WGLGYVVLTS VDRDDLADGG ARHFAETIRR
260 270 280 290 300
IKQKKPTLLV EALTGDFMGD LDMVKIVADS GLDVYAHNVE TVENLTPYVR
310 320 330 340 350
DRRATFRQSL KVLEHVKNVR GKEGIITKTS IMLGLGETEE ELWDALRELR
360 370 380 390 400
KVDVDVVTFG QYMRPTKRHL AVEKYITPDE FELWRQRALD MGFLYCASGP
410 420 430 440
LVRSSYKAGE AFIENVLKKR ASERVVSEAL GQAVAAEEAT SAKSA
Length:445
Mass (Da):48,591
Last modified:February 9, 2010 - v1
Checksum:iCC87656ED8D9D672
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CABT02000004 Genomic DNA Translation: CCC07689.1
RefSeqiXP_003352422.1, XM_003352374.1

Genome annotation databases

EnsemblFungiiCCC07689; CCC07689; SMAC_01256
GeneIDi10810058
KEGGismp:SMAC_01256

Similar proteinsi

Entry informationi

Entry nameiLIPA_SORMK
AccessioniPrimary (citable) accession number: D1Z4I6
Secondary accession number(s): F7VQA7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 9, 2010
Last modified: May 23, 2018
This is version 48 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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