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Protein

Lipoyl synthase 1, mitochondrial

Gene

LIP1-1

Organism
Pisum sativum (Garden pea)
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 + 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi120 – 1201Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi140 – 1401Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi144 – 1441Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi147 – 1471Iron-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 1, mitochondrial (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthase 1UniRule annotation
Short name:
LS 1UniRule annotation
Short name:
Lip-syn 1UniRule annotation
Lipoic acid synthase 1UniRule annotation
Gene namesi
Name:LIP1-1UniRule annotation
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

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? – 376Lipoyl synthase 1, mitochondrialPRO_0000398851
Transit peptidei1 – ?MitochondrionUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ3LSN4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
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.

Q3LSN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMYSRFRTVA GNLNCAAKRL SSSSTTTTTT SAPSELQQNL AALRARLAME
60 70 80 90 100
SPSLSDFISL KSDNAYSVEV GTKKKPLPKP KWMKESIPGG EKYVQIKKKL
110 120 130 140 150
RELKLHTVCE EAKCPNLGEC WSGGETGTAT ATIMILGDTC TRGCRFCNVK
160 170 180 190 200
TSRTPPPPDP DEPTNVAEAI ASWGLDYVVI TSVDRDDLPD QGSGHFTETV
210 220 230 240 250
QKLKALKPST LIEALVPDFR GNAECVEKVS KSGLDVFAHN IETVEELQSA
260 270 280 290 300
VRDHRANFKQ SLDVLMMAKE YAPAGTLTKT SIMLGCGETP DQIVKTMEKV
310 320 330 340 350
RAAGVDVMTF GQYMRPSKRH MPVSEYITPE AFEKYQTLGM EMGFRYVASG
360 370
PMVRSSYKAG EFYIKSMIDS DRAASS
Length:376
Mass (Da):41,290
Last modified:October 25, 2005 - v1
Checksum:i484934B10E861BDB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ181624 mRNA. Translation: ABA29156.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ181624 mRNA. Translation: ABA29156.1.

3D structure databases

ProteinModelPortaliQ3LSN4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
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. Doss R.P., Price R.R.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiLIAS1_PEA
AccessioniPrimary (citable) accession number: Q3LSN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 25, 2005
Last modified: March 4, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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.