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Protein

Lipoyl synthase 2

Gene

lipA2

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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 bindingi50 – 501Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi55 – 551Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi61 – 611Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi76 – 761Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi80 – 801Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi83 – 831Iron-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 2UniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-syn 2UniRule annotation
Lipoate synthase 2UniRule annotation
Lipoic acid synthase 2UniRule annotation
Sulfur insertion protein lipA2
Gene namesi
Name:lipA2UniRule annotation
Ordered Locus Names:sll0868
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Lipoyl synthase 2PRO_0000102372Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi1148.sll0868.

Structurei

3D structure databases

ProteinModelPortaliP73572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
InParanoidiP73572.
KOiK03644.
OMAiCAFCQVE.
OrthoDBiEOG6038ZS.
PhylomeDBiP73572.

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.

P73572-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQQSFMNGS SLPREFPPRL PSWLKRPIGR ASELSTVQQI IKQRQIHTIC
60 70 80 90 100
EEGRCPNRGE CYANRTATFL LMGQICTRAC GFCQVEKGQA PMMLDQDEPR
110 120 130 140 150
KVAEAVQLLG LKYVVLTSVA RDDLTDGGAG WFVAVMERIR QDNPATQIEV
160 170 180 190 200
LTPDFWGGMG RERSQKERVL TVTKAKPVCY NHNLETVARL QGKVRRGAKY
210 220 230 240 250
QRSLDVLRWI KEFDPDIFTK SGLMLGHGET VDEVVETLKD LRSVGCDRLT
260 270 280 290 300
LGQYMQPSLD HLPVQKYWTP EEFDQLGEIA KDLGFSHVRS GPLVRSSYHA

GED
Length:303
Mass (Da):34,267
Last modified:February 1, 1997 - v1
Checksum:i9E259BDC3D262653
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17612.1.
PIRiS77278.
RefSeqiNP_440932.1. NC_000911.1.
YP_005650991.1. NC_017277.1.
YP_007450815.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA17612; BAA17612; BAA17612.
KEGGisyn:sll0868.
PATRICi23839136. VBISynSp132158_1132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17612.1.
PIRiS77278.
RefSeqiNP_440932.1. NC_000911.1.
YP_005650991.1. NC_017277.1.
YP_007450815.1. NC_020286.1.

3D structure databases

ProteinModelPortaliP73572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1148.sll0868.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17612; BAA17612; BAA17612.
KEGGisyn:sll0868.
PATRICi23839136. VBISynSp132158_1132.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
InParanoidiP73572.
KOiK03644.
OMAiCAFCQVE.
OrthoDBiEOG6038ZS.
PhylomeDBiP73572.

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. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.

Entry informationi

Entry nameiLIPA2_SYNY3
AccessioniPrimary (citable) accession number: P73572
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: April 1, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.