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Reviewed, UniProtKB/Swiss-Prot Q9Y9E6 (LPLA_AERPE)

Last modified June 16, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative lipoate-protein ligase A
      Short name=Lipoate--protein ligase
    EC=2.7.7.63
Gene names
Name: lplA
Synonyms: lipB
Ordered Locus Names: APE_2341
OrganismAeropyrum pernix [Complete proteome] [HAMAP]
Taxonomic identifier56636 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + lipoate = diphosphate + lipoyl-AMP.

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

Pathway

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

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

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence similarities

Belongs to the lplA family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein modification process

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

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Putative lipoate-protein ligase A
PRO_0000062902

Regions

Nucleotide binding73 – 764ATP By similarity

Sites

Binding site681ATP By similarity
Binding site1301ATP By similarity
Binding site1301Lipoate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Y9E6-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 1814419916955924

FASTA26428,890
        10         20         30         40         50         60 
MILKTTGGSP HFNIALEEAL LEESAEHGIA IARLWVNPDS IIVGYTSDVG REVNIEQARA 

        70         80         90        100        110        120 
EGVPVVRRIS GGGAVFHDLG NMNVSVYIPR RLGVDEAYAL VTSIILKTLH RLGIEGRVEN 

       130        140        150        160        170        180 
GNDVAVGPWK VSGSAAAIRA RATLAHATLL LTTDPSRIRR LVIPQLHRVE RGEVTPVKYN 

       190        200        210        220        230        240 
PNSLERITGE RMEVWQAARL LEESVKHALG EPENVGRDIL QEAVIRAREL CKTKYSQKGF 

       250        260 
WSPLGLGACR EPQVAPMTSP SYVL 

« Hide

References

[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K1.

Cross-references

Sequence databases

BA000002 Genomic DNA. Translation: BAA81354.1.
PIRB72462.
RefSeqNP_148553.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1445362.
GenomeReviewsGene locus APE_2341 in contig BA000002_GR.
KEGGape:APE_2341.
NMPDRfig|272557.1.peg.1661.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9Y9E6.
OMAQ9Y9E6. NSLERIT.

Enzyme and pathway databases

BRENDA2.7.7.63. 256344.

Family and domain databases

InterProIPR004143. BPL_LipA_LipB.
[Graphical view]
PfamPF03099. BPL_LipA_LipB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPLA_AERPE
AccessionPrimary (citable) accession number: Q9Y9E6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents