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A4HY57

- LIPA_LEIIN

UniProt

A4HY57 - LIPA_LEIIN

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Protein
Lipoyl synthase, mitochondrial
Gene
LinJ19.0190, LinJ_19_0350
Organism
Leishmania infantum
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 bindingi127 – 1271Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi132 – 1321Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi138 – 1381Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi159 – 1591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi166 – 1661Iron-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

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:LinJ19.0190, LinJ_19_0350
OrganismiLeishmania infantum
Taxonomic identifieri5671 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
ProteomesiUP000008153: Chromosome 19

Subcellular locationi

Mitochondrion By similarity 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? – 412Lipoyl synthase, mitochondrialUniRule annotationPRO_0000398237
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Interactioni

Protein-protein interaction databases

STRINGi5671.LinJ19.0190.

Structurei

3D structure databases

ProteinModelPortaliA4HY57.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiEWLRRPI.

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.

A4HY57-1 [UniParc]FASTAAdd to Basket

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MCLTAAPSRV SPVAAAAAAA ADVAGSSEST VNLMADVDKK DPQYKQIFLE    50
RFRKKLQSDK TGMNDLESFV ELPEGVAPSA ASIGPIKRGS EPLPPWLKLK 100
VPKGMTHRPR FNRIRRSMRE KNLSTVCEEA KCPNIGECWG GSDDEGTATA 150
TIMVMGSHCT RGCRFCSVLT SRRPPPLDPE EPEKVAAAVH EMGVDYIVMT 200
MVDRDDLPDG GASHVCRCIH TIKEKNPALM LEALVGDFHG DLKLVEQLAV 250
TPLSVYAHNI ECVERITPRV RDRRASYKQS LQTLEHVTKS TNGKMLTKSS 300
IMLGLGEEEK EVRQTLRDLR TAGVSAVTLG QYLQPSRTRL KVSRYAHPKE 350
FEMWEKEAMD MGFLYCASGP MVRSSYRAGE YYIKSILKQR QSAEGGKATA 400
AATAANAGAA IA 412
Length:412
Mass (Da):45,132
Last modified:May 1, 2007 - v1
Checksum:iCC21574ED808D2C6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FR796451 Genomic DNA. Translation: CAM67240.1.
RefSeqiXP_001464998.1. XM_001464961.1.

Genome annotation databases

GeneIDi5068408.
KEGGilif:LINJ_19_0350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FR796451 Genomic DNA. Translation: CAM67240.1 .
RefSeqi XP_001464998.1. XM_001464961.1.

3D structure databases

ProteinModelPortali A4HY57.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5671.LinJ19.0190.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5068408.
KEGGi lif:LINJ_19_0350.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
KOi K03644.
OMAi EWLRRPI.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .

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: JPCM5.

Entry informationi

Entry nameiLIPA_LEIIN
AccessioniPrimary (citable) accession number: A4HY57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 2007
Last modified: June 11, 2014
This is version 47 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

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