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Q9K7C9 (LIPA_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:lipA
Ordered Locus Names:BH3435
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00206

Catalytic activity

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. HAMAP-Rule MF_00206

Cofactor

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

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]. HAMAP-Rule MF_00206

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00206.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000102287

Sites

Metal binding401Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding451Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding511Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding711Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding741Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K7C9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0DF7334D2703A7D1

FASTA30334,533
        10         20         30         40         50         60 
MAKKEEYVRK PDWLKIKLNT NETYTGLKKM MREKNLHTVC EEAKCPNIHE CWAVRKTATF 

        70         80         90        100        110        120 
MILGDVCTRA CRFCAVKTGL PNELDLQEPE RVAESVEIMG LKHAVITAVA RDDLKDGGAG 

       130        140        150        160        170        180 
VFAETVRAVR RRNPFCTIEV LPSDMMGNDD NLKTLMDARP NILNHNIETV RRLTPRVRAR 

       190        200        210        220        230        240 
ATYERSLEFL RRAKEMQPDI PTKSSLMIGL GETKDEIIET MDDLRANNVD IMTIGQYLQP 

       250        260        270        280        290        300 
TKKHLKVQKY YHPDEFAELK EIALSKGFSH CEAGPLVRSS YHADEQVNEA QVREEARKAA 


AKS 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB07154.1.
PIRC84079.
RefSeqNP_244302.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9K7C9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH3435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB07154; BAB07154; BAB07154.
GeneID894530.
KEGGbha:BH3435.
PATRIC18944142. VBIBacHal18977_3569.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-3536-MONOMER.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_BACHD
AccessionPrimary (citable) accession number: Q9K7C9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways