ID M2XHM4_DOTSN Unreviewed; 245 AA.
AC M2XHM4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Octanoyltransferase {ECO:0000256|PIRNR:PIRNR016262};
DE EC=2.3.1.181 {ECO:0000256|PIRNR:PIRNR016262};
GN ORFNames=DOTSEDRAFT_180972 {ECO:0000313|EMBL:EME38947.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME38947.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME38947.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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.
CC {ECO:0000256|PIRNR:PIRNR016262}.
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 Evidence={ECO:0000256|PIRNR:PIRNR016262};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2. {ECO:0000256|ARBA:ARBA00004821,
CC ECO:0000256|PIRNR:PIRNR016262}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000256|ARBA:ARBA00007907,
CC ECO:0000256|PIRNR:PIRNR016262}.
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DR EMBL; KB446546; EME38947.1; -; Genomic_DNA.
DR AlphaFoldDB; M2XHM4; -.
DR STRING; 675120.M2XHM4; -.
DR EnsemblFungi; EME38947; EME38947; DOTSEDRAFT_180972.
DR eggNOG; KOG0325; Eukaryota.
DR HOGENOM; CLU_035168_0_1_1; -.
DR OMA; TEEPMWY; -.
DR OrthoDB; 166876at2759; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
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 NCBIfam; TIGR00214; lipB; 1.
DR PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR016262};
KW Reference proteome {ECO:0000313|Proteomes:UP000016933};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR016262}.
FT DOMAIN 39..229
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 187
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-1"
FT BINDING 88..95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 156..158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 169..171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT SITE 153
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-3"
SQ SEQUENCE 245 AA; 27245 MW; 07DF05D51610768D CRC64;
MILRHIHFPT PVPYTHADIL QQTLVKTLLT HKASPKTIPA PNPTILTAQF HPVYTCGRRE
VGTLSKNQIN YLTAPTPLGT ASFHESLRGG QTTFHGPGQL VAYPIIDLRR HGLSPKCYVN
YLEQCVMDIL IEGWSIKGIR TENPGIWIDQ ERKICAVGVH LRRNVTSHGI GLNLRTKMGW
FERIVACGLE GKRVVNLEMV AGKGEGDMEV EKVAEMFVRR FGEGLEGVNA IRRIGQEEAF
GQGEG
//
