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Protein

Lipoyl synthase, mitochondrial

Gene

LIAS

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

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. Putative lipoyltransferase 2, mitochondrial (LIPT2)
  2. Lipoyl synthase, mitochondrial (LIAS), Lipoyl synthase, mitochondrial (LIAS)
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 bindingi106Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi111Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi117Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi137Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi141Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi144Iron-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

ReactomeiR-BTA-389661 Glyoxylate metabolism and glycine degradation
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
Name:LIASUniRule annotation
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 6

Organism-specific databases

VGNCiVGNC:30879 LIAS

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome 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 – 27MitochondrionUniRule annotationAdd BLAST27
ChainiPRO_000033231028 – 372Lipoyl synthase, mitochondrialAdd BLAST345

Proteomic databases

PaxDbiQ5BIP7
PRIDEiQ5BIP7

Expressioni

Gene expression databases

BgeeiENSBTAG00000014520
ExpressionAtlasiQ5BIP7 baseline and differential

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019299

Structurei

3D structure databases

ProteinModelPortaliQ5BIP7
SMRiQ5BIP7
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
GeneTreeiENSGT00390000006234
HOGENOMiHOG000235998
HOVERGENiHBG023328
InParanoidiQ5BIP7
KOiK03644
OMAiPYCDIDF
OrthoDBiEOG091G0AXJ
TreeFamiTF300817

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.

Q5BIP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRCGGAVR TVGPRVFGRY VFSPVREVSF LPDEKKEFLQ SGPDLQEFIS
60 70 80 90 100
GNLADKSTWD EYKGNLKRQK GERLRLPPWL KTEIPMGKNY NKLKNTLRNL
110 120 130 140 150
NLHTVCEEAR CPNIGECWGG GEYATATATI MLMGDTCTRG CRFCSVKTAR
160 170 180 190 200
NPPPLDANEP YNTAKAIAEW GLDYVVLTSV DRDDMPDGGA EHFAKTVSYL
210 220 230 240 250
KERNPKILVE CLTPDFRGDL KAIEKVALSG LDVYAHNVET VPELQRKVRD
260 270 280 290 300
PRANFDQSLR VLKHAKEVRP DVISKTSIML GLGENDEQVY ATMKALREAD
310 320 330 340 350
VDCLTLGQYM QPTKRHLKVE EYITPEKFKY WEKVGNELGF HYTASGPLVR
360 370
SSYKAGEFFL KNLVAKRKTK AL
Length:372
Mass (Da):42,035
Last modified:April 12, 2005 - v1
Checksum:iAA6C54F92133B3A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021177 mRNA Translation: AAX31359.1
RefSeqiNP_001017944.1, NM_001017944.1
UniGeneiBt.9756

Genome annotation databases

EnsembliENSBTAT00000019299; ENSBTAP00000019299; ENSBTAG00000014520
GeneIDi530865
KEGGibta:530865

Similar proteinsi

Entry informationi

Entry nameiLIAS_BOVIN
AccessioniPrimary (citable) accession number: Q5BIP7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 12, 2005
Last modified: May 23, 2018
This is version 84 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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