LPLA_YEAST
ID LPLA_YEAST Reviewed; 409 AA.
AC P47051; D6VWD8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative lipoate-protein ligase A;
DE EC=6.3.1.20;
DE AltName: Full=Altered inheritance rate of mitochondria protein 22;
GN Name=AIM22; OrderedLocusNames=YJL046W; ORFNames=J1171;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=15905473; DOI=10.1093/nar/gki583;
RA Zhang Z., Dietrich F.S.;
RT "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT SAGE.";
RL Nucleic Acids Res. 33:2838-2851(2005).
CC -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC onto the lipoyl domains of lipoate-dependent enzymes. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-
CC N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate +
CC H(+); Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:456215; EC=6.3.1.20;
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group of
CC lipoic acid is attached via an amide linkage to the epsilon-amino group
CC of a specific lysine residue of lipoyl domains of lipoate-dependent
CC enzymes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS56406.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA89337.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z49321; CAA89337.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY558080; AAS56406.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006943; DAA08754.1; -; Genomic_DNA.
DR PIR; S56818; S56818.
DR RefSeq; NP_012489.2; NM_001181479.1.
DR AlphaFoldDB; P47051; -.
DR SMR; P47051; -.
DR BioGRID; 33709; 343.
DR MINT; P47051; -.
DR STRING; 4932.YJL046W; -.
DR MaxQB; P47051; -.
DR PaxDb; P47051; -.
DR PRIDE; P47051; -.
DR EnsemblFungi; YJL046W_mRNA; YJL046W; YJL046W.
DR GeneID; 853401; -.
DR KEGG; sce:YJL046W; -.
DR SGD; S000003582; AIM22.
DR VEuPathDB; FungiDB:YJL046W; -.
DR eggNOG; KOG3159; Eukaryota.
DR GeneTree; ENSGT00390000008846; -.
DR HOGENOM; CLU_022986_2_0_1; -.
DR InParanoid; P47051; -.
DR OMA; KCAVIGK; -.
DR BioCyc; MetaCyc:G3O-31510-MON; -.
DR BioCyc; YEAST:G3O-31510-MON; -.
DR Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR UniPathway; UPA00537; UER00594.
DR UniPathway; UPA00537; UER00595.
DR PRO; PR:P47051; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47051; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; ISA:SGD.
DR GO; GO:0017118; F:lipoyltransferase activity; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IMP:SGD.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR PANTHER; PTHR12561; PTHR12561; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..409
FT /note="Putative lipoate-protein ligase A"
FT /id="PRO_0000203066"
FT DOMAIN 146..330
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 193..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 47003 MW; 72E9B6D036CDB1E9 CRC64;
MSMMLSNWAL SPRYVGQRNL IHCTTLFHTL TRWAKDADDK YHDINSMYEN MFTPSNDNVS
ILQDEGKSDY DTTKASSMEE DISAFNKDLY NFYNIGYAKQ IMSASQLENI VKAKGRFVIQ
SLSTSPYYNL ALENYVFKNT PRAKRGPDNC RLLFYINDRC AVIGKNQNLW QEVDLAKLKS
KNFELLRRFS GGGTVLHDLG NVNYSYLTSR EKFETKFFNK MIIKWLNSLN PELRLDLNER
GDIIQDGFKI SGSAYKIAGG KAYHHATMLL NADLEQFSGL LEPSLPNNME WESSGVHSVK
SKIKNVGIIT PNQFIAVVSE RFQKTFKVDG EIPIYYCDEF KSINDEIKDA MNTLQSEQWK
YFSGPKFSVK IKDKGLTIKV EKGMIYDCDR NDLIGLEFKG FLENIDSYT
