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B9J3H2

- LIPA_BACCQ

UniProt

B9J3H2 - LIPA_BACCQ

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Protein
Lipoyl synthase
Gene
lipA, BCQ_4790
Organism
Bacillus cereus (strain Q1)
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 By similarity.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

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathwayi

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi45 – 451Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi51 – 511Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi67 – 671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi71 – 711Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi74 – 741Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

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
Complete GO annotation...

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

BioCyciBCER361100:GJ7M-4777-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase (EC:2.8.1.8)
Alternative name(s):
Lip-syn
Short name:
LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene namesi
Name:lipA
Ordered Locus Names:BCQ_4790
OrganismiBacillus cereus (strain Q1)
Taxonomic identifieri361100 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000441: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction 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 – 298298Lipoyl synthaseUniRule annotation
PRO_1000124621Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi361100.BCQ_4790.

Structurei

3D structure databases

ProteinModelPortaliB9J3H2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiHPHIPTK.
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.

B9J3H2-1 [UniParc]FASTAAdd to Basket

« Hide

MTKQTEYKRK PEWLKIKLNT NENYTGLKKM MRSKNLHTVC EEAKCPNIHE    50
CWAVRKTATF MILGAVCTRA CRFCAVKTGL PTELDLQEPE RVADSVVQMG 100
LKHVVITAVA RDDLKDGGAA VFAETVRAVR RKNPFTSIEV LPSDMGGVEE 150
NLKMLMDAKP DILNHNIETV RRLSDRVRAR AKYDRSLEFL RRAKEMQPDI 200
PTKSSIMVGL GETREDLIEA MDDLRANNVD ILTLGQYLQP SKKHLPVLKY 250
YPPAEFAELK EIALSKGFSH CEAGPLVRSS YHADEQVRSA KENTAEAK 298
Length:298
Mass (Da):33,688
Last modified:March 24, 2009 - v1
Checksum:i64FB54F922A98774
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000227 Genomic DNA. Translation: ACM15191.1.
RefSeqiYP_002532480.1. NC_011969.1.

Genome annotation databases

EnsemblBacteriaiACM15191; ACM15191; BCQ_4790.
GeneIDi7376408.
KEGGibcq:BCQ_4790.
PATRICi18917377. VBIBacCer120424_4828.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000227 Genomic DNA. Translation: ACM15191.1 .
RefSeqi YP_002532480.1. NC_011969.1.

3D structure databases

ProteinModelPortali B9J3H2.
ModBasei Search...

Protein-protein interaction databases

STRINGi 361100.BCQ_4790.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM15191 ; ACM15191 ; BCQ_4790 .
GeneIDi 7376408.
KEGGi bcq:BCQ_4790.
PATRICi 18917377. VBIBacCer120424_4828.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
KOi K03644.
OMAi HPHIPTK.
OrthoDBi EOG6038ZS.

Enzyme and pathway databases

BioCyci BCER361100:GJ7M-4777-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. "Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
    Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
    J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Q1.

Entry informationi

Entry nameiLIPA_BACCQ
AccessioniPrimary (citable) accession number: B9J3H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 40 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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