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Protein

Lipoyl synthase, mitochondrial

Gene

Lias

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein 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 N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [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), 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi110 – 1101Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi116 – 1161Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi136 – 1361Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi140 – 1401Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi143 – 1431Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotation

Keywords - Ligandi

4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotationImported (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
Name:LiasUniRule annotationImported
ORF Names:mCG_10271Imported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1934604. Lias.

Subcellular locationi

  • Mitochondrion UniRule annotation

Keywords - Cellular componenti

MitochondrionUniRule annotation

Expressioni

Gene expression databases

BgeeiD3Z6I3.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031101.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 332207Elp3InterPro annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transit peptideUniRule annotation

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
HOGENOMiHOG000235998.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

D3Z6I3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRCWDTAR SLGSRIFGRY AFTVRALSSL PDKKKEFLHN GPDLQDFVSG
60 70 80 90 100
DLADKSTWDE YKGNLKRQKG ERLRLPPWLK TKIPMGKNYN KLKNTLRNLS
110 120 130 140 150
LHTVCEEARC PNIGECWGGG EYATATATIM LMGDTCTRGC RFCSVKTARN
160 170 180 190 200
PPPLDANEPD NTAKAIAEWG LDYVVLTSVD RDDVADGGAE HIAKTVSCLK
210 220 230 240 250
ERNPKILVEC LTPDFRGDLR AVEKVALSGL DVYAHNVETV PELQRKVRDP
260 270 280 290 300
RANFDQSLRV LRHAKEVQPD VVSKTSIMLG LGETDEQVYA TLKALRAADV
310 320 330 340 350
DCLTLGQYMQ PTKRHLKVEE YVTPEKFKYW EKVGNELGFL YTASGPLVRS
360 370
SYKAGEFFLK NLVARRKTKA SKV
Length:373
Mass (Da):41,879
Last modified:October 14, 2015 - v2
Checksum:i6796340A54BC5B8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC136513 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37739.1.
RefSeqiNP_077791.1. NM_024471.5.
UniGeneiMm.195776.

Genome annotation databases

EnsembliENSMUST00000122026; ENSMUSP00000113228; ENSMUSG00000029199.
GeneIDi79464.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC136513 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37739.1.
RefSeqiNP_077791.1. NM_024471.5.
UniGeneiMm.195776.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000122026; ENSMUSP00000113228; ENSMUSG00000029199.
GeneIDi79464.

Organism-specific databases

CTDi11019.
MGIiMGI:1934604. Lias.

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
HOGENOMiHOG000235998.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Miscellaneous databases

SOURCEiSearch...

Gene expression databases

BgeeiD3Z6I3.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A comparison of whole-genome shotgun-derived mouse chromosome 16 and the human genome."
    Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R., Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A., Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.
    , Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K., Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J., Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R., Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H., Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A., Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A., Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C., Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C., Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B., Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E., Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R., Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C., Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L., Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S., Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L., Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R., Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R., Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J., Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L., Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C., Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A., Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H., Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L., Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M., Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K., Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S., Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J., Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G., Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.
    Science 296:1661-1671(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (MAY-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: C57BL/6JImported.

Entry informationi

Entry nameiD3Z6I3_MOUSE
AccessioniPrimary (citable) accession number: D3Z6I3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: October 14, 2015
Last modified: June 8, 2016
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.