ID   LPLA_YEAST              Reviewed;         409 AA.
AC   P47051;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Putative lipoate-protein ligase A;
DE            EC=2.7.7.63;
DE   AltName: Full=Altered inheritance rate of mitochondria protein 22;
GN   Name=AIM22; OrderedLocusNames=YJL046W; ORFNames=J1171;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=96208490; PubMed=8641269;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
RA   Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA   Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA   Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA   Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA   Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA   Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA   Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA   Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA   Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA   Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [3]
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
RT   using 5' SAGE.";
RL   Nucleic Acids Res. 33:2838-2851(2005).
CC   -!- FUNCTION: Catalyzes both the ATP-dependent activation of
CC       exogenously supplied lipoate to lipoyl-AMP and the transfer of the
CC       activated lipoyl onto the lipoyl domains of lipoate-dependent
CC       enzymes (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + lipoate = diphosphate + lipoyl-AMP.
CC   -!- CATALYTIC ACTIVITY: Lipoyl-AMP + protein = protein N(6)-
CC       (lipoyl)lysine + AMP.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoic acid: step 1/2.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoic acid: step 2/2.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group
CC       of lipoic acid is attached via an amide linkage to the epsilon-
CC       amino group of a specific lysine residue of lipoyl domains of
CC       lipoate-dependent enzymes (By similarity).
CC   -!- SIMILARITY: Belongs to the lplA family.
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DR   EMBL; Z49321; CAA89337.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY558080; AAS56406.1; ALT_INIT; Genomic_DNA.
DR   PIR; S56818; S56818.
DR   Ensembl; YJL046W; Saccharomyces cerevisiae.
DR   GenomeReviews; Y13136_GR; YJL046W.
DR   KEGG; sce:YJL046W; -.
DR   NMPDR; fig|4932.3.peg.3463; -.
DR   CYGD; YJL046w; -.
DR   SGD; S000003582; AIM22.
DR   HOGENOM; P47051; -.
DR   OMA; P47051; NYSYLTS.
DR   BRENDA; 2.7.7.63; 250.
DR   ArrayExpress; P47051; -.
DR   GermOnline; YJL046W; Saccharomyces cerevisiae.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR   InterPro; IPR004143; BPL_LipA_LipB.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   Pfam; PF03099; BPL_LipA_LipB; 1.
DR   TIGRFAMs; TIGR00545; lipoyltrans; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    409       Putative lipoate-protein ligase A.
FT                                /FTId=PRO_0000203066.
FT   NP_BIND     193    196       ATP (By similarity).
FT   BINDING     188    188       ATP (By similarity).
FT   BINDING     249    249       ATP (By similarity).
FT   BINDING     249    249       Lipoate (By similarity).
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
//