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Protein

Lipoyl synthase, mitochondrial

Gene

PODANS_1_14620

Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
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 bindingi140 – 1401Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi145 – 1451Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi151 – 1511Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi171 – 1711Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi175 – 1751Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi178 – 1781Iron-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
Ordered Locus Names:PODANS_1_14620
OrganismiPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Taxonomic identifieri515849 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora
ProteomesiUP000001197 Componenti: Chromosome 1

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 – 2929MitochondrionUniRule annotationAdd
BLAST
Chaini30 – 426397Lipoyl synthase, mitochondrialPRO_0000398284Add
BLAST

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

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]
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.

B2AT43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPAPLQRL QAPLRRSLAR AAVLSSRTYA TIPSPSDPGL TQSSPSPAAS
60 70 80 90 100
TTPAKKAPRP SYFKDTTVAS FSEFVGSQSA PLSLSEAYEI KTAEVGPAGR
110 120 130 140 150
KRTITRLPEW LKTPIPSSGA NPNFGKIKAD LRGLNLHTVC EEARCPNIGE
160 170 180 190 200
CWGGNDKSAA TATIMLMGDT CTRGCRFCSV KTNRKPPPLD PHEPENTAEA
210 220 230 240 250
LARWGLGYVV LTSVDRDDLA DGGARHFAET IRRIKQKKPT LLVEALTGDF
260 270 280 290 300
MGDLDMVKIV AESGLDVYAH NVETVEGLTP YVRDRRATFR QSLKVLEHVK
310 320 330 340 350
AVRGKEGIIT KTSIMLGLGE QEQEIWDTLR ELRKIDVDVV TFGQYMRPTK
360 370 380 390 400
RHLKVEKYVT PDEFDLWKQR ALDMGFLYCA SGPLVRSSYK AGEAFIENVL
410 420
RKRAGERAAA SASLDQVVAA EETKAL
Length:426
Mass (Da):46,688
Last modified:May 19, 2008 - v1
Checksum:i09B7F18A38D991A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633899 Genomic DNA. Translation: CAP67566.1.
RefSeqiXP_001906895.1. XM_001906860.1.

Genome annotation databases

GeneIDi6191609.
KEGGipan:PODANSg3928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633899 Genomic DNA. Translation: CAP67566.1.
RefSeqiXP_001906895.1. XM_001906860.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6191609.
KEGGipan:PODANSg3928.

Phylogenomic databases

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

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: S / ATCC MYA-4624 / DSM 980 / FGSC 10383.

Entry informationi

Entry nameiLIPA_PODAN
AccessioniPrimary (citable) accession number: B2AT43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 4, 2010
Last sequence update: May 19, 2008
Last modified: March 31, 2015
This is version 45 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.