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Protein

Lipoyl synthase, mitochondrial

Gene

PITG_14852

Organism
Phytophthora infestans (strain T30-4) (Potato late blight fungus)
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 = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.

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 bindingi116 – 1161Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi121 – 1211Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi127 – 1271Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi147 – 1471Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi151 – 1511Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi154 – 1541Iron-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:PITG_14852
OrganismiPhytophthora infestans (strain T30-4) (Potato late blight fungus)
Taxonomic identifieri403677 [NCBI]
Taxonomic lineageiEukaryotaStramenopilesOomycetesPeronosporalesPhytophthora
ProteomesiUP000006643: Partially assembled 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 – 1919MitochondrionUniRule annotationAdd
BLAST
Chaini20 – 383364Lipoyl synthase, mitochondrialPRO_0000398245Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliD0NP70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998.
InParanoidiD0NP70.
KOiK03644.
OMAiEEYVTPE.

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.

D0NP70-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHASTLTRCM RVAQNARCLS TAAASVQVTH SERGARLAAL RERLAEETRQ
60 70 80 90 100
GPTFAEQALS LEDFAFEADA APGTKPSRKP NASNRKPKWL KAQPTQGANY
110 120 130 140 150
ERLRKSVKSL GLSTVCEEAK CPNIGECWGG GKDGIATATI MLMGDTCTRG
160 170 180 190 200
CSFCAVKTSR KPKPLDIEEP NKVAEAIAAW GLDYIVFTSV DRDDYEDLGA
210 220 230 240 250
GHFAKTVSTL RAKLPEILIE CLTPDFQGHD NLIDQVATSG LDVFAHNMET
260 270 280 290 300
VERLQRRVRD YRANYKQSLH VLERAKVAAP HLVTKTSLML GVGERNEDLF
310 320 330 340 350
QTLRDLRNSG VDVVTFGQYL RPSTKHMPVK SYVTPEAFAE WQKVAEQMGF
360 370 380
LYVASGPMVR SSYKAGEFFM KNLLKNRKTQ VVA
Length:383
Mass (Da):42,420
Last modified:December 15, 2009 - v1
Checksum:i6D29FBE4DC34315F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS028150 Genomic DNA. Translation: EEY62412.1.
RefSeqiXP_002899048.1. XM_002899002.1.
UniGeneiPin.6624.

Genome annotation databases

EnsemblProtistsiPITG_14852T0; PITG_14852T0; PITG_14852.
GeneIDi9467967.
KEGGipif:PITG_14852.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS028150 Genomic DNA. Translation: EEY62412.1.
RefSeqiXP_002899048.1. XM_002899002.1.
UniGeneiPin.6624.

3D structure databases

ProteinModelPortaliD0NP70.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiPITG_14852T0; PITG_14852T0; PITG_14852.
GeneIDi9467967.
KEGGipif:PITG_14852.

Phylogenomic databases

HOGENOMiHOG000235998.
InParanoidiD0NP70.
KOiK03644.
OMAiEEYVTPE.

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. "Genome sequence and analysis of the Irish potato famine pathogen Phytophthora infestans."
    The Broad Institute Genome Sequencing Platform
    Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M., Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O., Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A., Baxter L., Beynon J.
    , Boevink P.C., Bollmann S.R., Bos J.I., Bulone V., Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S., Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S., Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K., Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D., Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L., Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J., Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M., Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S., Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D., Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J., Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S., Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P., Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S., Nusbaum C.
    Nature 461:393-398(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: T30-4.

Entry informationi

Entry nameiLIPA_PHYIT
AccessioniPrimary (citable) accession number: D0NP70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 15, 2009
Last modified: January 7, 2015
This is version 32 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.