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B4RBV1 (LIPA_PHEZH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:PHZ_c1737
OrganismPhenylobacterium zucineum (strain HLK1) [Complete proteome] [HAMAP]
Taxonomic identifier450851 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaePhenylobacterium

Protein attributes

Sequence length319 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]: step 2/2. 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 – 319319Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000099619

Sites

Metal binding581Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding631Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding691Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding841Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding881Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding911Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B4RBV1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 3BF30B60C5EF6761

FASTA31935,207
        10         20         30         40         50         60 
MAVVIDTVGA RPRHPEKQAN PDTPVLRKPE WLRVRAPGSA NYMATREVVK SNRLVTVCEE 

        70         80         90        100        110        120 
AGCPNIGECW DKSHATFMIM GEVCTRACAF CNVATGKPLA LDPDEPARVG EATAKMGLKH 

       130        140        150        160        170        180 
VVVTSVDRDD LADGGAWHFV ETIRAIRAAS PATTIEILTP DFARKPVAAL ESVIDARPDV 

       190        200        210        220        230        240 
FNHNLETVPR LYLSIRPGAR YYHSLRLLER VKERDPTQFT KSGIMVGLGE SKEEVMQVMD 

       250        260        270        280        290        300 
DMRSAGVDFI TIGQYLQPTR KHAPIDRFVH PDEFRALEEI ARAKGFLMVS ASPLTRSSHH 

       310 
AGEDFARLQA ARLAKESAA 

« Hide

References

[1]"Complete genome of Phenylobacterium zucineum - a novel facultative intracellular bacterium isolated from human erythroleukemia cell line K562."
Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.
BMC Genomics 9:386-386(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000747 Genomic DNA. Translation: ACG78148.1.
RefSeqYP_002130577.1. NC_011144.1.

3D structure databases

ProteinModelPortalB4RBV1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING450851.PHZ_c1737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG78148; ACG78148; PHZ_c1737.
GeneID6791250.
KEGGpzu:PHZ_c1737.
PATRIC22926410. VBIPheZuc44517_2277.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMATIRAVRH.
OrthoDBEOG6038ZS.

Enzyme and pathway databases

BioCycPZUC450851:GHUG-1764-MONOMER.
UniPathwayUPA00538; UER00593.

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_PHEZH
AccessionPrimary (citable) accession number: B4RBV1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 42 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