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Protein

Lipoyl synthase, mitochondrial

Gene

LELG_04389

Organism
Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 bindingi150 – 1501Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi155 – 1551Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi161 – 1611Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi180 – 1801Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi184 – 1841Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi187 – 1871Iron-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
ORF Names:LELG_04389
OrganismiLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
Taxonomic identifieri379508 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeLodderomyces
ProteomesiUP000001996: Unassembled WGS sequence

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? – 432Lipoyl synthase, mitochondrialPRO_0000398271
Transit peptidei1 – ?MitochondrionUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi36914.A5E450.

Structurei

3D structure databases

ProteinModelPortaliA5E450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiA5E450.
KOiK03644.
OMAiCAFCQVE.
OrthoDBiEOG79KPR7.

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]
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.

A5E450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPRSINILK LRPTTQVTTT ALRALATEAK TTLGATPGST STSTSTSTAT
60 70 80 90 100
TTTLESTSTS TSGDATETTI KETKSIKRKR TFFTDELNKG PSFDDFVSGK
110 120 130 140 150
AKDMLEDPLE LARKDPNAKL PLWLKVPIPK GKSFHNVKND VRELKLSTVC
160 170 180 190 200
EEAKCPNIGE CWGGKKSEAT ATIMLLGDTC TRGCRFCSVK TNRKPGKPDP
210 220 230 240 250
MEPENTAEAI SRWGLGYVVL TTVDRDDLID GGANHLKETV QKIKFKAPQI
260 270 280 290 300
LVEVLGGDFR GDLEMVKILA NSGLDVYAHN METVEALTPH IRDRRATYRQ
310 320 330 340 350
SLAVLRTAKE TKPSLITKTS LMLGFGETDD QIRQTLKDLR EVGCDVVTFG
360 370 380 390 400
QYMRPTKRHM KVVEYVTPEK FDYWRDVALE MGFLYVASGP LVRSSYKAGE
410 420 430
AFIENVLKKR KHNVGESPRM LQEVKPSIFK RA
Length:432
Mass (Da):47,959
Last modified:June 12, 2007 - v1
Checksum:i6371CA6B2C363D7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH981529 Genomic DNA. Translation: EDK46208.1.
RefSeqiXP_001524417.1. XM_001524367.1.

Genome annotation databases

GeneIDi5231419.
KEGGilel:LELG_04389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH981529 Genomic DNA. Translation: EDK46208.1.
RefSeqiXP_001524417.1. XM_001524367.1.

3D structure databases

ProteinModelPortaliA5E450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi36914.A5E450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5231419.
KEGGilel:LELG_04389.

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiA5E450.
KOiK03644.
OMAiCAFCQVE.
OrthoDBiEOG79KPR7.

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]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

Entry informationi

Entry nameiLIPA_LODEL
AccessioniPrimary (citable) accession number: A5E450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 12, 2007
Last modified: March 4, 2015
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.