Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

LbrM19_V2.0670

Organism
Leishmania braziliensis
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 bindingi94 – 941Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi99 – 991Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi105 – 1051Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi126 – 1261Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi130 – 1301Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi133 – 1331Iron-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:LbrM19_V2.0670, LbrM_19_0670
OrganismiLeishmania braziliensis
Taxonomic identifieri5660 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmaniaLeishmania braziliensis species complex
ProteomesiUP000007258: Chromosome 19

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
Chaini? – 379Lipoyl synthase, mitochondrialPRO_0000398236
Transit peptidei1 – ?MitochondrionUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA4H9Z3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiA4H9Z3.
KOiK03644.
OMAiPAGNDNF.

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.

A4H9Z3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDVDKKDPQ YKQIFLERFR KKLQSDKTGM SDLESFVELP EGITPVAASI
60 70 80 90 100
GPIKRGSEPL PPWLKLNVPK GMTHRPRFNR IRRSMREKKL STVCEEAKCP
110 120 130 140 150
NIGECWGGGE DNGAATATIM VMGSHCTRGC RFCSVLTSRR PPPLDPDEPE
160 170 180 190 200
KVAAAVHEMG VDYIVMTMVD RDDLPDGGAS HVSRCIRTIK EQNPELMLEA
210 220 230 240 250
LVGDFHGDLK VVEQLAATPL SVYAHNIECV ERITPRVRDH RATYKQSLQT
260 270 280 290 300
LEHVTKWTNG KMLTKSSIML GLGEEEEEVR QTLRDLRTAG VSAVTLGQYL
310 320 330 340 350
QPSRTRLKVS RYAHPKEFEM WEKEAMSMGF LYCASGPMVR SSYRAGEYYI
360 370
KNIVKQRENA KGATTMEAVT AADAVAAGA
Length:379
Mass (Da):42,320
Last modified:May 1, 2007 - v1
Checksum:i6FEC94249B0FA50F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR798993 Genomic DNA. Translation: CAM38219.1.
RefSeqiXP_001564163.2. XM_001564113.2.

Genome annotation databases

GeneIDi5414704.
KEGGilbz:LBRM_19_0670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR798993 Genomic DNA. Translation: CAM38219.1.
RefSeqiXP_001564163.2. XM_001564113.2.

3D structure databases

ProteinModelPortaliA4H9Z3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5414704.
KEGGilbz:LBRM_19_0670.

Phylogenomic databases

InParanoidiA4H9Z3.
KOiK03644.
OMAiPAGNDNF.

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]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MHOM/BR/75/M2904.

Entry informationi

Entry nameiLIPA_LEIBR
AccessioniPrimary (citable) accession number: A4H9Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 2007
Last modified: March 4, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.