LIPB_KLULA
ID LIPB_KLULA Reviewed; 332 AA.
AC O13476;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=LIPB; OrderedLocusNames=KLLA0D18777g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=9268025; DOI=10.1007/s004380050505;
RA Chen X.J.;
RT "Cloning and characterization of the lipoyl-protein ligase gene LIPB from
RT the yeast Kluyveromyces lactis: synergistic respiratory deficiency due to
RT mutations in LIPB and mitochondrial F1-ATPase subunits.";
RL Mol. Gen. Genet. 255:341-349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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: 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; X87623; CAA60954.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00989.1; -; Genomic_DNA.
DR RefSeq; XP_453893.1; XM_453893.1.
DR AlphaFoldDB; O13476; -.
DR SMR; O13476; -.
DR STRING; 28985.XP_453893.1; -.
DR EnsemblFungi; CAH00989; CAH00989; KLLA0_D18777g.
DR GeneID; 2892930; -.
DR KEGG; kla:KLLA0_D18777g; -.
DR eggNOG; KOG0325; Eukaryota.
DR HOGENOM; CLU_035168_0_1_1; -.
DR InParanoid; O13476; -.
DR OMA; RCHIRVL; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:EnsemblFungi.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009249; P:protein lipoylation; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Acyltransferase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..332
FT /note="Octanoyltransferase, mitochondrial"
FT /id="PRO_0000017858"
FT DOMAIN 115..318
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 278
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 169..176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247..249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 244
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 37625 MW; AE6C1CAA38FF9BD1 CRC64;
MSKLMLIGTN YWYPSKFGCT IFRKVRFQST LKCTSTARTQ PIDPSAKTIR HLQFVKEIPF
ETGIDIQEKF VRAHLDIKQL QSKIKREMTN LQKEHNAEIQ LNFHEQMILD NINQMKPNPI
VLTFQFEPTY TGGKRVKKQI TDEQIARYEG FIPSKQKYNK KPKFVQAERG GQVTFHGPGQ
IVAYIILDLK TFQNLPAKCL VSTIDNAAMN ALKVVPKFQG SDEPLNLITQ KTNDTGVWVS
NQEKIASIGI HVRRSVTSHG ICINVDPDLS YMNSFTMCGL SEKKATSIRE QVPDSSTSVN
DVAVAFVNQL AKLLGITTVE RIQLDDLPIY TD
