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Q3LSN5

- LIAS2_PEA

UniProt

Q3LSN5 - LIAS2_PEA

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Protein
Lipoyl synthase 2, mitochondrial
Gene
LIP1-2
Organism
Pisum sativum (Garden pea)
Status
Reviewed - 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 By similarity.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.UniRule annotation

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi120 – 1201Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi140 – 1401Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi144 – 1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi147 – 1471Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

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
Complete GO annotation...

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 2, mitochondrial (EC:2.8.1.8)
Alternative name(s):
Lipoate synthase 2
Short name:
LS 2
Short name:
Lip-syn 2
Lipoic acid synthase 2
Gene namesi
Name:LIP1-2
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

Mitochondrion By similarity 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 2, mitochondrialUniRule annotationPRO_0000398852
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Structurei

3D structure databases

ProteinModelPortaliQ3LSN5.

Family & Domainsi

Sequence similaritiesi

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.

Q3LSN5-1 [UniParc]FASTAAdd to Basket

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MMYSRFRTVA GNLNCAAKRL SSSSTTTTTT SAPSELQQNL AALRARLAME    50
SPSLSDFISL KSDNAYSVEV GTKKKPLPKP KWMKESIPGG EKYVQIKKKL 100
RELKLHTVCE EAKCPNLGEC WSGGETGTAT ATIMILGDTC TRGCRFCNVK 150
TSRTPPPPDP DEPTNVAEAI ASWGLDYVVI TSVDRDDLPD QGSGHFTETV 200
QKLKALKPSM LIEALVPDFR GNAECVEKVS KSGLDVFAHN IETVEELQSA 250
VRDHRANFKQ SLDVLMMAKE YAPAGTLTKT SIMLGCGETP DQIVKTMEKV 300
RAAGVDVMTF GQHMRPSKRH MPVSEYITPE AFEKYQTLGM EMGFRYVASG 350
PMVRSSYKAG EFYIKSMIDS DRAASS 376
Length:376
Mass (Da):41,294
Last modified:October 25, 2005 - v1
Checksum:i3613E2F6A0492FAA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ181623 mRNA. Translation: ABA29155.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ181623 mRNA. Translation: ABA29155.1 .

3D structure databases

ProteinModelPortali Q3LSN5.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

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 nameiLIAS2_PEA
AccessioniPrimary (citable) accession number: Q3LSN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 25, 2005
Last modified: February 19, 2014
This is version 38 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

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