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Protein

Lipoyl synthase, mitochondrial

Gene

lias

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 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.

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi111 – 1111Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi117 – 1171Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi137 – 1371Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi144 – 1441Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-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
Name:lias
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6251515. lias.

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 372Lipoyl synthase, mitochondrialPRO_0000398212
Transit peptidei1 – ?MitochondrionUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6GQ48.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG023328.
KOiK03644.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6GQ48-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRQCGLVRAA QLLRTCGLAE WHTPYRALSS LPDEKKELIK NGPDLQDFLS
60 70 80 90 100
GELVDKSSWA AYKGDLKRQK GERLRLPPWV KTEIPMGKNY NKLKNTLRNL
110 120 130 140 150
NLHTVCEEAR CPNIGECWGG GEYGTATATI MLMGDTCTRG CRFCSVKTAR
160 170 180 190 200
NPPPLDPDEP YNTSKAIAEW GLDYVVLTSV DRDDISDGGA EHIAQTVSML
210 220 230 240 250
KERNKTILIE CLTPDFRGNM KAVETVAKSG LDVYAHNVET VPALQRHVRD
260 270 280 290 300
PRANFDQSLN VLKHAKNVRP DLVSKTSIML GLGETDEQIY STMKALREAG
310 320 330 340 350
VDCLTLGQYM QPTKRHLKVE EYITPEKFKY WEKAGNELGF LYTASGPLVR
360 370
SSYKAGEFFL KNLIEKRKTK AI
Length:372
Mass (Da):41,803
Last modified:July 19, 2004 - v1
Checksum:i905039EBFE3CC48C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC072900 mRNA. Translation: AAH72900.1.
RefSeqiNP_001085534.1. NM_001092065.1.
UniGeneiXl.55041.

Genome annotation databases

GeneIDi443960.
KEGGixla:443960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC072900 mRNA. Translation: AAH72900.1.
RefSeqiNP_001085534.1. NM_001092065.1.
UniGeneiXl.55041.

3D structure databases

ProteinModelPortaliQ6GQ48.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi443960.
KEGGixla:443960.

Organism-specific databases

CTDi11019.
XenbaseiXB-GENE-6251515. lias.

Phylogenomic databases

HOVERGENiHBG023328.
KOiK03644.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.

Entry informationi

Entry nameiLIAS_XENLA
AccessioniPrimary (citable) accession number: Q6GQ48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 19, 2004
Last modified: January 7, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.