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Q82AP7

- LIPA_STRAW

UniProt

Q82AP7 - LIPA_STRAW

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Protein

Lipoyl synthase

Gene

lipA

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
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.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 bindingi56 – 561Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi61 – 611Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi67 – 671Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi82 – 821Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi86 – 861Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi89 – 891Iron-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

BioCyciSAVE227882:GJU1-6090-MONOMER.
UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-synUniRule annotation
Short name:
LSUniRule annotation
Lipoate synthaseUniRule annotation
Lipoic acid synthaseUniRule annotation
Sulfur insertion protein LipAUniRule annotation
Gene namesi
Name:lipAUniRule annotation
Ordered Locus Names:SAV_6009
OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Taxonomic identifieri227882 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
ProteomesiUP000000428: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Lipoyl synthasePRO_0000102365Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi227882.SAV_6009.

Structurei

3D structure databases

ProteinModelPortaliQ82AP7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
KOiK03644.
OMAiWIKIRAK.
OrthoDBiEOG6038ZS.

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.

Q82AP7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAVAPDGRK MLRLEVRNAQ TPIERKPEWI KTRAKMGPEY TKMQNLVKSE
60 70 80 90 100
GLHTVCQEAG CPNIYECWED REATFLIGGD QCTRRCDFCQ IDTGKPEALD
110 120 130 140 150
RDEPRRVGES VVTMDLNYAT ITGVARDDLE DGGAWLYAET VRQIHAQTAG
160 170 180 190 200
REAGRTKVEL LAPDFNAEPD QLAEVFSARP EVFAHNVETV PRIFKRIRPG
210 220 230 240 250
FRYERSLKVI TEARDYGLVT KSNLILGMGE TREEVSEALR QLHDAGCELI
260 270 280 290 300
TITQYLRPSV RHHPVERWVK PHEFVELKEE AEEIGFSGVM SGPLVRSSYR
310 320
AGRLYQMAME LRQSAAPQGG AQVASQAV
Length:328
Mass (Da):36,964
Last modified:June 1, 2003 - v1
Checksum:i9DBEEFF550623CEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC73721.1.
RefSeqiNP_827186.1. NC_003155.4.

Genome annotation databases

EnsemblBacteriaiBAC73721; BAC73721; SAV_6009.
GeneIDi1211373.
KEGGisma:SAV_6009.
PATRICi23726046. VBIStrAve112782_6376.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC73721.1 .
RefSeqi NP_827186.1. NC_003155.4.

3D structure databases

ProteinModelPortali Q82AP7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 227882.SAV_6009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC73721 ; BAC73721 ; SAV_6009 .
GeneIDi 1211373.
KEGGi sma:SAV_6009.
PATRICi 23726046. VBIStrAve112782_6376.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235997.
KOi K03644.
OMAi WIKIRAK.
OrthoDBi EOG6038ZS.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .
BioCyci SAVE227882:GJU1-6090-MONOMER.

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. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
    Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
    Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
  2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
    Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
    Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Entry informationi

Entry nameiLIPA_STRAW
AccessioniPrimary (citable) accession number: Q82AP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 80 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

External Data

Dasty 3