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Protein

Lipoyl synthase, mitochondrial

Gene

PAAG_05935

Organism
Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
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 bindingi150 – 1501Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi155 – 1551Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi161 – 1611Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi181 – 1811Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi185 – 1851Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi188 – 1881Iron-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:PAAG_05935
OrganismiParacoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Taxonomic identifieri502779 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides
ProteomesiUP000002059: Partially assembled WGS

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 – 3737MitochondrionUniRule annotationAdd
BLAST
Chaini38 – 439402Lipoyl synthase, mitochondrialPRO_0000398276Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC1H594.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK03644.
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.

C1H594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVASARGLRT LHSAHSSISA LPASTVPRLQ LAVSRCYATT TSPDCPITNS
60 70 80 90 100
SNSSNSTPTL TPKQRITAFK DKLNAGPSFS DFVSGGGASN DSVPLDPTEA
110 120 130 140 150
YSLKTALVGP PGKKKQIIRL PSWLKTPIPD SPNFRRIKSD LRGLNLHTVC
160 170 180 190 200
EEARCPNISD CWGGSSKSAA TATIMLMGDT CTRGCRFCSV KTSRTPPPLD
210 220 230 240 250
PHEPENTAEA LSRWGLGYVV MTSVDRDDLA DGGARHVAET VRKVKQKAPN
260 270 280 290 300
ILLECLTGDY AGDLEMVALV ATSGLDVFAH NVETVEALTP FVRDRRATFQ
310 320 330 340 350
QSLRVLKAAK EAKPELITKT SIMLGLGETE AQLWETLKAL RAVDVDVVTF
360 370 380 390 400
GQYMRPTKRH MAVHEYVRPD VFDSWKERAL EMGFLYCASG PLVRSSYKAG
410 420 430
EAFIENVLKK RRGEGADGSG GSSTRREDVE RLVAGGVVR
Length:439
Mass (Da):47,567
Last modified:May 26, 2009 - v1
Checksum:i3BAB21D357F78492
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN294007 Genomic DNA. Translation: EEH34888.1.
RefSeqiXP_002792147.1. XM_002792101.1.

Genome annotation databases

GeneIDi9095385.
KEGGipbl:PAAG_05935.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN294007 Genomic DNA. Translation: EEH34888.1.
RefSeqiXP_002792147.1. XM_002792101.1.

3D structure databases

ProteinModelPortaliC1H594.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9095385.
KEGGipbl:PAAG_05935.

Phylogenomic databases

KOiK03644.
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: ATCC MYA-826 / Pb01.

Entry informationi

Entry nameiLIPA_PARBA
AccessioniPrimary (citable) accession number: C1H594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 26, 2009
Last modified: March 4, 2015
This is version 38 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.