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B7G3Y9

- LIPA2_PHATC

UniProt

B7G3Y9 - LIPA2_PHATC

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Protein

Lipoyl synthase 2, mitochondrial

Gene

PHATRDRAFT_28652

Organism
Phaeodactylum tricornutum (strain CCAP 1055/1)
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.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

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 bindingi46 – 461Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi51 – 511Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi57 – 571Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi72 – 721Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi76 – 761Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi79 – 791Iron-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 2, mitochondrial (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthase 2UniRule annotation
Short name:
LS 2UniRule annotation
Short name:
Lip-syn 2UniRule annotation
Lipoic acid synthase 2UniRule annotation
Gene namesi
ORF Names:PHATRDRAFT_28652
OrganismiPhaeodactylum tricornutum (strain CCAP 1055/1)
Taxonomic identifieri556484 [NCBI]
Taxonomic lineageiEukaryotaStramenopilesBacillariophytaBacillariophyceaeBacillariophycidaeNaviculalesPhaeodactylaceaePhaeodactylum
ProteomesiUP000000759: Chromosome 13, UP000000759: Unassembled WGS sequence

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 314Lipoyl synthase 2, mitochondrialPRO_0000398244
Transit peptidei1 – ?MitochondrionUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi2850.JGI28652.

Structurei

3D structure databases

ProteinModelPortaliB7G3Y9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiB7G3Y9.
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.

B7G3Y9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPKGRPSWFK VPAPSQGTQS TYSTASYSRY AQVKDSLQKL DLHTVCEEAQ
60 70 80 90 100
CPNIGECWNG GTGTIMLLGD TCTRGCMFCA VNTDSKPPPP DPFEPFKTAE
110 120 130 140 150
AVVAWGVDYI VLTSVDRDDI ADGGAQHFAQ TVQLLKQNKP NLLVECLVSD
160 170 180 190 200
FQGMLDSVET LALSGLDVYA HNVETVERLQ PFVRDARANY QQSLSTLQHA
210 220 230 240 250
KVVKPELYTK TSIMLGLGET EEEVTQTMTD LRAIGVDVVT FGQYLRPTEH
260 270 280 290 300
HLSVVEYVTP EKFDHYRQVG ENMGFKYVAS GPMVRSSYKA GEFYLEHMIK
310
KERTEAAIDI GENA
Length:314
Mass (Da):34,862
Last modified:February 10, 2009 - v1
Checksum:i70E379E29A535340
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CM000615 Genomic DNA. Translation: EEC46905.1.
RefSeqiXP_002181691.1. XM_002181655.1.
UniGeneiPtc.241.

Genome annotation databases

EnsemblProtistsiPhatr28652; Phatr28652; Phatr28652.
GeneIDi7202486.
KEGGipti:PHATRDRAFT_28652.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CM000615 Genomic DNA. Translation: EEC46905.1 .
RefSeqi XP_002181691.1. XM_002181655.1.
UniGenei Ptc.241.

3D structure databases

ProteinModelPortali B7G3Y9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 2850.JGI28652.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblProtistsi Phatr28652 ; Phatr28652 ; Phatr28652 .
GeneIDi 7202486.
KEGGi pti:PHATRDRAFT_28652.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
InParanoidi B7G3Y9.
KOi K03644.

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

« Hide 'large scale' publications
  1. "The Phaeodactylum genome reveals the evolutionary history of diatom genomes."
    Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A., Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.
    , Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y., Grigoriev I.V.
    Nature 456:239-244(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CCAP 1055/1.
  2. Cited for: GENOME REANNOTATION.
    Strain: CCAP 1055/1.

Entry informationi

Entry nameiLIPA2_PHATC
AccessioniPrimary (citable) accession number: B7G3Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 10, 2009
Last modified: October 29, 2014
This is version 34 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