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P47051 (LPLA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Putative lipoate-protein ligase A

EC=2.7.7.63
Alternative name(s):
Altered inheritance rate of mitochondria protein 22
Gene names
Name:AIM22
Ordered Locus Names:YJL046W
ORF Names:J1171
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 lipoate: step 1/2.

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

Subunit structure

Monomer 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.

Sequence caution

The sequence AAS56406.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA89337.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein lipoylation

Inferred from mutant phenotype. Source: SGD

   Cellular componentmitochondrion

Inferred from direct assay. Source: SGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligase activity

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 – 409409Putative lipoate-protein ligase A
PRO_0000203066

Regions

Nucleotide binding193 – 1964ATP By similarity

Sites

Binding site1881ATP By similarity
Binding site2491ATP By similarity
Binding site2491Lipoate By similarity

Sequences

Sequence LengthMass (Da)Tools
P47051 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 72E9B6D036CDB1E9

FASTA40947,003
        10         20         30         40         50         60 
MSMMLSNWAL SPRYVGQRNL IHCTTLFHTL TRWAKDADDK YHDINSMYEN MFTPSNDNVS 

        70         80         90        100        110        120 
ILQDEGKSDY DTTKASSMEE DISAFNKDLY NFYNIGYAKQ IMSASQLENI VKAKGRFVIQ 

       130        140        150        160        170        180 
SLSTSPYYNL ALENYVFKNT PRAKRGPDNC RLLFYINDRC AVIGKNQNLW QEVDLAKLKS 

       190        200        210        220        230        240 
KNFELLRRFS GGGTVLHDLG NVNYSYLTSR EKFETKFFNK MIIKWLNSLN PELRLDLNER 

       250        260        270        280        290        300 
GDIIQDGFKI SGSAYKIAGG KAYHHATMLL NADLEQFSGL LEPSLPNNME WESSGVHSVK 

       310        320        330        340        350        360 
SKIKNVGIIT PNQFIAVVSE RFQKTFKVDG EIPIYYCDEF KSINDEIKDA MNTLQSEQWK 

       370        380        390        400 
YFSGPKFSVK IKDKGLTIKV EKGMIYDCDR NDLIGLEFKG FLENIDSYT 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE."
Zhang Z., Dietrich F.S.
Nucleic Acids Res. 33:2838-2851(2005) [PubMed: 15905473] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49321 Genomic DNA. Translation: CAA89337.1. Different initiation.
AY558080 Genomic DNA. Translation: AAS56406.1. Different initiation.
BK006943 Genomic DNA. Translation: DAA08754.1.
PIRS56818.
RefSeqNP_012489.2. NM_001181479.1.

3D structure databases

ProteinModelPortalP47051.
SMRP47051. Positions 116-392.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-2494178.
STRINGP47051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL046W; YJL046W; YJL046W.
GeneID853401.
KEGGsce:YJL046W.
NMPDRfig|4932.3.peg.3463.

Organism-specific databases

SGDS000003582. AIM22.

Phylogenomic databases

eggNOGfuNOG08946.
GeneTreeEFGT00050000006534.
HOGENOMHBG202206.
OMANYSYLTS.
OrthoDBEOG4Q886M.

Gene expression databases

ArrayExpressP47051.
GenevestigatorP47051.
GermOnlineYJL046W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004143. BPL_LipA_LipB.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
KOK03800.
PfamPF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00545. Lipoyltrans. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPLA_YEAST
AccessionPrimary (citable) accession number: P47051
Secondary accession number(s): D6VWD8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: June 16, 2009
Last modified: December 14, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families