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A8N1T1 (LIPA_COPC7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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
ORF Names:CC1G_03624
OrganismCoprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata) [Reference proteome]
Taxonomic identifier240176 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

Protein attributes

Sequence length390 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
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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 – 1818Mitochondrion Potential
Chain19 – 390372Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398264

Sites

Metal binding991Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1041Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1101Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A8N1T1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 2D13896927A3B057

FASTA39042,711
        10         20         30         40         50         60 
MALYRAPKLQ RSLLNRCLAT ASTTPAAAST SRTSTFRKTL EEGPTLDDFI AGDVPNNRVV 

        70         80         90        100        110        120 
LGNTSAPRLP SYLKTSIPTG ASFSKIKKDL RGLNLHTVCE EARCPNIGDC WGGKPGATEA 

       130        140        150        160        170        180 
EGRSAATATI MLMGDTCTRG CRFCSVKTSR TPPPLDPHEP ENTAEAISRW GLGYIVLTSV 

       190        200        210        220        230        240 
DRDDLADGGA RHFAETISKI KQKAPHILVE ALTGDFAGNL EHVSLVAKSG LDVYAHNIET 

       250        260        270        280        290        300 
VEALTPFVRD RRATFRQSLS VLKRAKEEGV KVTKTSIMLG VGETEDQVLD ALKELRKVDV 

       310        320        330        340        350        360 
DVVTFGQYMR PTKRHMKVDR YVEPAEFDRW KQVAEDLGFL YVASGPLVRS SYKAGEFYIE 

       370        380        390 
NVLKGKSVNK RVKNLTMESE LSEKSASASL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACS02000001 Genomic DNA. Translation: EAU92837.1.
RefSeqXP_001828830.1. XM_001828778.2.

3D structure databases

ProteinModelPortalA8N1T1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6005256.
KEGGcci:CC1G_03624.

Phylogenomic databases

KOK03644.
OrthoDBEOG79KPR7.

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_COPC7
AccessionPrimary (citable) accession number: A8N1T1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 33 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