LIPB_YEAST
ID LIPB_YEAST Reviewed; 328 AA.
AC Q06005; D6VYN7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Octanoyltransferase, mitochondrial;
DE EC=2.3.1.181;
DE AltName: Full=Lipoate biosynthesis protein;
DE AltName: Full=Lipoate-protein ligase;
DE AltName: Full=Lipoyl ligase;
DE AltName: Full=Lipoyl/octanoyl transferase;
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
DE Flags: Precursor;
GN Name=LIP2; OrderedLocusNames=YLR239C; ORFNames=L8083.16;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC dependent enzymes. Lipoyl-ACP can also act as a substrate although
CC octanoyl-ACP is likely to be the physiological substrate (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC acid is attached via an amide linkage to the epsilon-amino group of a
CC specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000305}.
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DR EMBL; U19027; AAB67419.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09553.1; -; Genomic_DNA.
DR PIR; S51458; S51458.
DR RefSeq; NP_013340.1; NM_001182126.1.
DR AlphaFoldDB; Q06005; -.
DR SMR; Q06005; -.
DR BioGRID; 31506; 391.
DR DIP; DIP-2776N; -.
DR IntAct; Q06005; 2.
DR MINT; Q06005; -.
DR STRING; 4932.YLR239C; -.
DR MaxQB; Q06005; -.
DR PaxDb; Q06005; -.
DR PRIDE; Q06005; -.
DR EnsemblFungi; YLR239C_mRNA; YLR239C; YLR239C.
DR GeneID; 850940; -.
DR KEGG; sce:YLR239C; -.
DR SGD; S000004229; LIP2.
DR VEuPathDB; FungiDB:YLR239C; -.
DR eggNOG; KOG0325; Eukaryota.
DR GeneTree; ENSGT00390000006450; -.
DR HOGENOM; CLU_035168_0_1_1; -.
DR InParanoid; Q06005; -.
DR OMA; RCHIRVL; -.
DR BioCyc; MetaCyc:YLR239C-MON; -.
DR BioCyc; YEAST:YLR239C-MON; -.
DR UniPathway; UPA00538; UER00592.
DR PRO; PR:Q06005; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06005; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016874; F:ligase activity; IMP:SGD.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009249; P:protein lipoylation; IMP:SGD.
DR CDD; cd16444; LipB; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..328
FT /note="Octanoyltransferase, mitochondrial"
FT /id="PRO_0000017859"
FT DOMAIN 108..312
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 272
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 162..169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241..243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254..256
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 238
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000250"
SQ SEQUENCE 328 AA; 37237 MW; 0CD9FBD8EAC07081 CRC64;
MSRCIRQSVC TNFNVCRRQC FSTYASALKE MTHPIKPSAQ TLRHLQFTQR IPFQKGLEIQ
ETLVRANLDI KDIQSKIERK LIQLDEEYKG TATINDNEKR ILDKVMAMKP NPIILTFEFE
PTYTGGKRIK KTMTPDQIAA YESFIPETQK DNPRPKFVQV ERGGQVTFHG PGQIVIYIIL
DLKTFQSFPA KCLVSCIEQA TIRTLKNTKM CDDTDKPLNL DAMTTKDTGV WVENGKKKVA
SVGIHVRRSI TSHGVAINVN TDLSYMNSFE MCGLKNTLTT SIMEQRPDAV VNVQSVAISF
VKEMTKLLGI KTLERMQIDD VNILKKNP
