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B6HFQ1

- LIPA_PENCW

UniProt

B6HFQ1 - LIPA_PENCW

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Protein

Lipoyl synthase, mitochondrial

Gene
Pc20g03200
Organism
Penicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-1255) (Penicillium notatum)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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.UniRule annotation

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi132 – 1321Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi137 – 1371Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi143 – 1431Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi167 – 1671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi170 – 1701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

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

BioCyciPCHR:PC20G03200-MONOMER.
UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
ORF Names:Pc20g03200
OrganismiPenicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-1255) (Penicillium notatum)
Taxonomic identifieri500485 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex
ProteomesiUP000000724: Contig Pc00c20

Subcellular locationi

Mitochondrion Reviewed prediction 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 – 3333Mitochondrion Reviewed predictionAdd
BLAST
Chaini34 – 416383Lipoyl synthase, mitochondrialUniRule annotationPRO_5000409605Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi500485.B6HFQ1.

Structurei

3D structure databases

ProteinModelPortaliB6HFQ1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiHPHIPTK.
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.

B6HFQ1-1 [UniParc]FASTAAdd to Basket

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MAAPTRSLRR LSSFRTTISP SLTVTAPIGC RSYATTDSSS ATNTPGTTRR    50
RATKFQDKLN AGPSFSDFVS GGQDEPLDPS EAYALKTALV GPAGRKKEMT 100
RLPEWLKTPI PDSKNYQRLK KDLRGLNLHT VCEEARCPNI SDCWGGSDKS 150
SATATIMLMG DTCTRGCRFC SVKTSRAPPP LDPHEPENTA EAISRWSLGY 200
VVLTSVDRDD LVDGGARHFA ETVIKIKQKK PSMLVECLTG DFRGDTEMAA 250
LVARSGLDVY AHNVETVEEL TPFVRDRRAT FQQSIRVLDS AKKAVPELVT 300
KTSLMLGLGE TDEQLWDALR QLRAVNVDVV TFGQYMRPTK RHMAVHEYVT 350
PDRFELWRQR ALDMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAGSGTA 400
ERTVDQTAAT TDEATR 416
Length:416
Mass (Da):45,966
Last modified:December 16, 2008 - v1
Checksum:iE9F9AE2F5E90A7CA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM920435 Genomic DNA. Translation: CAP85649.1.
RefSeqiXP_002562872.1. XM_002562826.1.

Genome annotation databases

GeneIDi8317549.
KEGGipcs:Pc20g03200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM920435 Genomic DNA. Translation: CAP85649.1 .
RefSeqi XP_002562872.1. XM_002562826.1.

3D structure databases

ProteinModelPortali B6HFQ1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 500485.B6HFQ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 8317549.
KEGGi pcs:Pc20g03200.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
KOi K03644.
OMAi HPHIPTK.
OrthoDBi EOG79KPR7.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .
BioCyci PCHR:PC20G03200-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 28089 / DSM 1075 / Wisconsin 54-1255.

Entry informationi

Entry nameiLIPA_PENCW
AccessioniPrimary (citable) accession number: B6HFQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 16, 2008
Last modified: June 11, 2014
This is version 42 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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