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B2AT43 (LIPA_PODAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoyl synthase, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase
Gene names
Ordered Locus Names:PODANS_1_14620
OrganismPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) [Complete proteome]
Taxonomic identifier515849 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_03123

Catalytic activity

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. HAMAP-Rule MF_03123

Cofactor

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

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_03123

Subcellular location

Mitochondrion Potential HAMAP-Rule MF_03123.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Potential
Chain30 – 426397Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398284

Sites

Metal binding1401Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1451Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1511Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1711Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1751Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1781Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B2AT43 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 09B7F18A38D991A2

FASTA42646,688
        10         20         30         40         50         60 
MASPAPLQRL QAPLRRSLAR AAVLSSRTYA TIPSPSDPGL TQSSPSPAAS TTPAKKAPRP 

        70         80         90        100        110        120 
SYFKDTTVAS FSEFVGSQSA PLSLSEAYEI KTAEVGPAGR KRTITRLPEW LKTPIPSSGA 

       130        140        150        160        170        180 
NPNFGKIKAD LRGLNLHTVC EEARCPNIGE CWGGNDKSAA TATIMLMGDT CTRGCRFCSV 

       190        200        210        220        230        240 
KTNRKPPPLD PHEPENTAEA LARWGLGYVV LTSVDRDDLA DGGARHFAET IRRIKQKKPT 

       250        260        270        280        290        300 
LLVEALTGDF MGDLDMVKIV AESGLDVYAH NVETVEGLTP YVRDRRATFR QSLKVLEHVK 

       310        320        330        340        350        360 
AVRGKEGIIT KTSIMLGLGE QEQEIWDTLR ELRKIDVDVV TFGQYMRPTK RHLKVEKYVT 

       370        380        390        400        410        420 
PDEFDLWKQR ALDMGFLYCA SGPLVRSSYK AGEAFIENVL RKRAGERAAA SASLDQVVAA 


EETKAL 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU633899 Genomic DNA. Translation: CAP67566.1.
RefSeqXP_001906895.1. XM_001906860.1.

3D structure databases

ProteinModelPortalB2AT43.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6191609.
KEGGpan:PODANSg3928.

Phylogenomic databases

KOK03644.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_PODAN
AccessionPrimary (citable) accession number: B2AT43
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways