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Protein

Lipoyl synthase, mitochondrial

Gene

PABG_05724

Organism
Paracoccidioides brasiliensis (strain Pb03)
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 bindingi144 – 1441Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi149 – 1491Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi155 – 1551Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi175 – 1751Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi179 – 1791Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi182 – 1821Iron-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:PABG_05724
OrganismiParacoccidioides brasiliensis (strain Pb03)
Taxonomic identifieri482561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides
ProteomesiUP000002740 Componenti: 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 – 3131MitochondrionUniRule annotationAdd
BLAST
Chaini32 – 434403Lipoyl synthase, mitochondrialPRO_0000398277Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC0SDG9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiC0SDG9.
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]
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.

C0SDG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASARGLRT LQSAHSSTTV PRLQLAVSRC YATTTSPDPP ITNSSNSSNS
60 70 80 90 100
TPTPKQRITA FKDKLNAGPS FSDFVSGGGG GASNDRVPLD PAEAYALKTA
110 120 130 140 150
LVGPPGRKKQ IIRLPSWLKT PIPDTPNYRR IKSDLRGLNL HTVCEEARCP
160 170 180 190 200
NISDCWGGSS KSAATATIML MGDTCTRGCR FCSVKTSRTP PPLDPHEPEN
210 220 230 240 250
TAEALSRWGL GYVVMTSVDR DDLADGGARH VAETVRKVKQ KAPGILLECL
260 270 280 290 300
TGDYAGDLEM VALVATSGLD VFAHNVETVE ALTPFVRDRR ATFQQSLRVL
310 320 330 340 350
KAAKEARPEL ITKTSIMLGL GETETQLWET LRALRTVDVD VVTFGQYMRP
360 370 380 390 400
TKRHMAVHEY VRPGVFDLWK ERALEMGFLY CASGPLVRSS YKAGEAFIEN
410 420 430
VLKKRRGEGA DGGDGGNSTR REDVERLVAG GVVR
Length:434
Mass (Da):47,106
Last modified:May 5, 2009 - v1
Checksum:i02DABF6FB68CDDA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN305539 Genomic DNA. Translation: EEH23513.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN305539 Genomic DNA. Translation: EEH23513.1.

3D structure databases

ProteinModelPortaliC0SDG9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiC0SDG9.
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]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pb03.

Entry informationi

Entry nameiLIPA_PARBP
AccessioniPrimary (citable) accession number: C0SDG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 5, 2009
Last modified: April 1, 2015
This is version 35 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

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.