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Q99M04 (LIAS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoyl synthase, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Short name=mLIP1
Lipoic acid synthase
Gene names
Name:Lias
Synonyms:Lip1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 Probable. HAMAP-Rule MF_03123

Catalytic activity

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_03123

Cofactor

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_03123

Subcellular location

Mitochondrion Ref.1.

Tissue specificity

Expressed predominantly in heart, testis, and liver. Ref.1

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 373347Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000017724

Sites

Metal binding1051Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1101Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1161Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1401Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1431Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99M04 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6796340A54BC5B8E

FASTA37341,879
        10         20         30         40         50         60 
MALRCWDTAR SLGSRIFGRY AFTVRALSSL PDKKKEFLHN GPDLQDFVSG DLADKSTWDE 

        70         80         90        100        110        120 
YKGNLKRQKG ERLRLPPWLK TKIPMGKNYN KLKNTLRNLS LHTVCEEARC PNIGECWGGG 

       130        140        150        160        170        180 
EYATATATIM LMGDTCTRGC RFCSVKTARN PPPLDANEPD NTAKAIAEWG LDYVVLTSVD 

       190        200        210        220        230        240 
RDDVADGGAE HIAKTVSCLK ERNPKILVEC LTPDFRGDLR AVEKVALSGL DVYAHNVETV 

       250        260        270        280        290        300 
PELQRKVRDP RANFDQSLRV LRHAKEVQPD VVSKTSIMLG LGETDEQVYA TLKALRAADV 

       310        320        330        340        350        360 
DCLTLGQYMQ PTKRHLKVEE YVTPEKFKYW EKVGNELGFL YTASGPLVRS SYKAGEFFLK 

       370 
NLVARRKTKA SKV 

« Hide

References

« Hide 'large scale' references
[1]"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria."
Morikawa T., Yasuno R., Wada H.
FEBS Lett. 498:16-21(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Heart.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum and Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB057731 mRNA. Translation: BAB62009.1.
AK048744 mRNA. Translation: BAC33443.1.
AK049548 mRNA. Translation: BAC33804.1.
AK077192 mRNA. Translation: BAC36672.1.
BC002141 mRNA. Translation: AAH02141.1.
RefSeqNP_077791.1. NM_024471.4.
UniGeneMm.195776.

3D structure databases

ProteinModelPortalQ99M04.
SMRQ99M04. Positions 129-309.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ99M04.
PRIDEQ99M04.

Protocols and materials databases

DNASU79464.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031101; ENSMUSP00000031101; ENSMUSG00000029199.
GeneID79464.
KEGGmmu:79464.
UCSCuc008xnq.1. mouse.

Organism-specific databases

CTD11019.
MGIMGI:1934604. Lias.

Phylogenomic databases

eggNOGCOG0320.
GeneTreeENSGT00390000006234.
HOGENOMHOG000235998.
HOVERGENHBG023328.
InParanoidQ99M04.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG7P2XS7.
PhylomeDBQ99M04.
TreeFamTF300817.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Gene expression databases

ArrayExpressQ99M04.
BgeeQ99M04.
CleanExMM_LIAS.
GenevestigatorQ99M04.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Other

NextBio349935.
PROQ99M04.
SOURCESearch...

Entry information

Entry nameLIAS_MOUSE
AccessionPrimary (citable) accession number: Q99M04
Secondary accession number(s): Q543M1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot