ID   LPLA_YEAS6              Reviewed;         409 AA.
AC   B5VLD2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 41.
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; ORFNames=AWRI1631_101610;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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=EDZ71262.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; ABSV01001321; EDZ71262.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B5VLD2; -.
DR   SMR; B5VLD2; -.
DR   UniPathway; UPA00537; UER00594.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
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.
FT   CHAIN           1..409
FT                   /note="Putative lipoate-protein ligase A"
FT                   /id="PRO_0000377669"
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;  47032 MW;  FEDFE85D4D17E0DC CRC64;
     MSMMLSNWAL SPRYVGQRNL IHCTTLFHTL TRWAKDADDK YHDINSMYEN MFTPSNDNVS
     ILQDEGKSDY DTTKTSSMQE 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