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Protein

Lipoyl synthase, mitochondrial

Gene

Bm1_23910

Organism
Brugia malayi (Filarial nematode worm)
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 bindingi89 – 891Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi94 – 941Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi100 – 1001Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi120 – 1201Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi124 – 1241Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi127 – 1271Iron-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:Bm1_23910
OrganismiBrugia malayi (Filarial nematode worm)
Taxonomic identifieri6279 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia

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? – 357Lipoyl synthase, mitochondrialPRO_0000398227
Transit peptidei1 – ?MitochondrionUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA8PF69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiA8PF69.
KOiK03644.

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.

A8PF69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISFTTRISR VTFSSKRVAL PDGPSLHDFI ETGNSNDAVE KYGIQMKLEA
60 70 80 90 100
NAKRLRLPPW LKRSIPSVDN TNFTHLKKQV KKLKLATVCE EARCPNIEEC
110 120 130 140 150
WSGSNNVPST ATIMLMGDTC TRGCKFCSVK TSLKPPPLNP EEPINTAKAI
160 170 180 190 200
ADWGINYVVL TSVDRDDIED GGASHIAATV KHLKQECPNI LVECLVPDFR
210 220 230 240 250
GSLSSVETIA SSGLDVYAHN METVRRLTPW VRDPRATYDQ SLKVLEYAKK
260 270 280 290 300
FRADIVTKTS LMLGLGETDE EVLTTLHDLR KIGVDALTFG QYMQPTKRHL
310 320 330 340 350
LVKEWITPEK FEEWREVGDX LGFLYTASGP LVRSSYKAGE YFLGKVVKNR

KQGVQEN
Length:357
Mass (Da):39,992
Last modified:January 14, 2008 - v1
Checksum:iD2D111962123E37C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS239138 Genomic DNA. Translation: EDP34906.1.
RefSeqiXP_001896239.1. XM_001896204.1.

Genome annotation databases

GeneIDi6099682.
KEGGibmy:Bm1_23910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS239138 Genomic DNA. Translation: EDP34906.1.
RefSeqiXP_001896239.1. XM_001896204.1.

3D structure databases

ProteinModelPortaliA8PF69.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6099682.
KEGGibmy:Bm1_23910.

Organism-specific databases

CTDi6099682.

Phylogenomic databases

InParanoidiA8PF69.
KOiK03644.

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. "Draft genome of the filarial nematode parasite Brugia malayi."
    Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E., Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T., Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.
    , Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M., Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J., Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F., Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W., Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M., McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J., Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E., Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G., Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B., Blaxter M.L., Scott A.L.
    Science 317:1756-1760(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiLIAS_BRUMA
AccessioniPrimary (citable) accession number: A8PF69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 4, 2010
Last sequence update: January 14, 2008
Last modified: March 31, 2015
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.