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Protein

Lipoyl synthase, mitochondrial

Gene

NECHADRAFT_66689

Organism
Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) (Fusarium solani subsp. pisi)
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 bindingi124 – 1241Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi129 – 1291Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi135 – 1351Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi155 – 1551Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi159 – 1591Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi162 – 1621Iron-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:NECHADRAFT_66689
OrganismiNectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) (Fusarium solani subsp. pisi)
Taxonomic identifieri660122 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium solani species complex
ProteomesiUP000005206: 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
Transit peptidei1 – 2828MitochondrionUniRule annotationAdd
BLAST
Chaini29 – 412384Lipoyl synthase, mitochondrialPRO_0000398273Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC7Z527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiC7Z527.
KOiK03644.
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]
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.

C7Z527-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASIAPSLKR AHAPLRKALT ASSTIRAFAT VPPTSSETTK PKRKSYFKDT
60 70 80 90 100
TVAEFSDFLA TSSPAQPLSP AEAFTLRTAE VGPEGKKRTI TRLPEWLKTP
110 120 130 140 150
IPAGNDNFKS IKKDLRGLGL HTVCEEARCP NISECWGGSD KNAATATIML
160 170 180 190 200
MGDTCTRGCR FCSVKTNRKP AALDPHEPEN TAEALARWGL GYVVLTSVDR
210 220 230 240 250
DDLADGGAHH FAETIRRIKQ KKPSLLVEAL TGDFRGDLDM VKVVAESGLD
260 270 280 290 300
VYAHNVETVE DLTPYVRDRR ATFRQSLSVL KHVKEVKGKE GIITKTSLML
310 320 330 340 350
GLGEQEHEVM AALEDLRKAD VDVVTFGQYM RPTKRHLKVE KYVTPDEFEM
360 370 380 390 400
WNKRALDMGF LYCASGPLVR SSYKAGEAFI ENVLRKRSGE KAMARGTLAK
410
AVALDSETRS SI
Length:412
Mass (Da):45,389
Last modified:October 13, 2009 - v1
Checksum:i18E930BB46989CFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG698910 Genomic DNA. Translation: EEU40447.1.
RefSeqiXP_003046160.1. XM_003046114.1.

Genome annotation databases

EnsemblFungiiNechaT66689; NechaP66689; NechaG66689.
GeneIDi9678266.
KEGGinhe:NECHADRAFT_66689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG698910 Genomic DNA. Translation: EEU40447.1.
RefSeqiXP_003046160.1. XM_003046114.1.

3D structure databases

ProteinModelPortaliC7Z527.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiNechaT66689; NechaP66689; NechaG66689.
GeneIDi9678266.
KEGGinhe:NECHADRAFT_66689.

Phylogenomic databases

InParanoidiC7Z527.
KOiK03644.
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]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI.

Entry informationi

Entry nameiLIPA_NECH7
AccessioniPrimary (citable) accession number: C7Z527
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 13, 2009
Last modified: March 4, 2015
This is version 38 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.