LIPB_SCHPO
ID LIPB_SCHPO Reviewed; 219 AA.
AC O36017;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable octanoyltransferase;
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;
GN ORFNames=SPAC4F10.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 -!- 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; CU329670; CAB11708.1; -; Genomic_DNA.
DR PIR; T38809; T38809.
DR RefSeq; NP_594748.1; NM_001020175.2.
DR AlphaFoldDB; O36017; -.
DR SMR; O36017; -.
DR BioGRID; 280054; 2.
DR STRING; 4896.SPAC4F10.05c.1; -.
DR MaxQB; O36017; -.
DR PaxDb; O36017; -.
DR EnsemblFungi; SPAC4F10.05c.1; SPAC4F10.05c.1:pep; SPAC4F10.05c.
DR GeneID; 2543640; -.
DR KEGG; spo:SPAC4F10.05c; -.
DR PomBase; SPAC4F10.05c; -.
DR VEuPathDB; FungiDB:SPAC4F10.05c; -.
DR eggNOG; KOG0325; Eukaryota.
DR HOGENOM; CLU_035168_0_1_1; -.
DR InParanoid; O36017; -.
DR OMA; ENWIIRT; -.
DR PhylomeDB; O36017; -.
DR UniPathway; UPA00538; UER00592.
DR PRO; PR:O36017; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; ISS:PomBase.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..219
FT /note="Probable octanoyltransferase"
FT /id="PRO_0000062908"
FT DOMAIN 43..219
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 182
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 83..90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151..153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 148
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000250"
SQ SEQUENCE 219 AA; 24497 MW; E401E923A0AE00C9 CRC64;
MNKIQHISFI TKKNPLVSYE RVGALQNRFV QHYLNYKANK VEQPPKPTII TSQVCPVYTL
GRRESSINFT KGFPKAKVVK ALRGGQTTFH GPGQILAYPI IDLKSFGLSP REYVSRLEQA
IIATCKSFGI EKAHTTKNTG VWVTENDKIA AIGIHLRRNI TSHGLALNVS TDLKYFNYIV
GCGLYGKNTT SFKDQGVFTD LKSVEKVLVN NLDSFLMSK
