Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q492U9 (LPLA_BLOPB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:
Lipoate-protein ligase A

EC=2.7.7.63
Alternative name(s):
Lipoate--protein ligase
Gene names
Name:lplA
Ordered Locus Names:BPEN_368
OrganismBlochmannia pennsylvanicus (strain BPEN) [Complete proteome] [HAMAP]
Taxonomic identifier291272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes By similarity. HAMAP MF_01602

Catalytic activity

ATP + lipoate = diphosphate + lipoyl-AMP. HAMAP MF_01602

Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. HAMAP MF_01602

Pathway

Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. HAMAP MF_01602

Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.

Subunit structure

Monomer By similarity. HAMAP MF_01602

Subcellular location

Cytoplasm By similarity HAMAP MF_01602.

Miscellaneous

In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes By similarity. HAMAP MF_01602

Sequence similarities

Belongs to the lplA family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpeptidyl-lysine lipoylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate-protein ligase activity

Inferred from electronic annotation. Source: InterPro

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Lipoate-protein ligase A HAMAP MF_01602
PRO_0000311125

Regions

Nucleotide binding76 – 794ATP By similarity

Sites

Binding site711ATP By similarity
Binding site1351ATP By similarity
Binding site1351Lipoate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q492U9 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: A0790CCFE243EA82

FASTA33939,198
        10         20         30         40         50         60 
MCSLRLLLSD SYDPWFNLSL EEYIYKNIPK KQSILFLWRN QNTVVIGRAQ NAWKECNTRR 

        70         80         90        100        110        120 
MERDGIKLAR RNSGGGAVFH DLGNTCFTFI STQEHYDKSI SSNIVLNGLS YIGIKAIISG 

       130        140        150        160        170        180 
RNDIVIRTEN GEHRKISGSA YRETSGRKFH HGTLLLHVDI DKLDYYLNPD FKKLETKGIT 

       190        200        210        220        230        240 
SIRSRVANLN ELKPGINHQE VCLGLTEAFF QHYGMKVKPE ILSTDNFCKI PEFFKQFNKQ 

       250        260        270        280        290        300 
SDWNWNFGSA PAFTHQLDTR FDWGSVTLHC DIERGIIHRS HIFTDSLDPS PLEILAKKLV 

       310        320        330 
GIPYNNKSIL CCCKEWMQSW PQYKKELSEV SHWLIKTIS 

« Hide

References

[1]"Genome sequence of Blochmannia pennsylvanicus indicates parallel evolutionary trends among bacterial mutualists of insects."
Degnan P.H., Lazarus A.B., Wernegreen J.J.
Genome Res. 15:1023-1033(2005) [PubMed: 16077009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BPEN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000016 Genomic DNA. Translation: AAZ40993.1.
RefSeqYP_277868.1. NC_007292.1.

3D structure databases

HSSPHSSP built from PDB template 1X2G based on UniProtKB P32099.
ProteinModelPortalQ492U9.
SMRQ492U9. Positions 3-338.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ492U9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3563042.
GenomeReviewsGene locus BPEN_368 in contig CP000016_GR.
KEGGbpn:BPEN_368.
PATRIC31965637. VBICanBlo110049_0356.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0095.
HOGENOMHBG715377.
OMAYDRMENL.
PhylomeDBQ492U9.
ProtClustDBCLSK280831.

Enzyme and pathway databases

BioCycCBLO291272:BPEN_368-MONOMER.

Family and domain databases

HAMAPMF_01602. LplA.
[Tree]
InterProIPR004143. BPL_LipA_LipB.
IPR005107. CO_DH_flav_C.
IPR023741. Lipoate_ligase_A.
IPR019491. Lipoate_protein_ligase_C.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
Gene3DG3DSA:3.30.390.50. CO_DH_flav_C. 1 hit.
KOK03800.
PfamPF03099. BPL_LplA_LipB. 1 hit.
PF10437. Lip_prot_lig_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00545. Lipoyltrans. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPLA_BLOPB
AccessionPrimary (citable) accession number: Q492U9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families