ID A0A0M0K194_9EUKA Unreviewed; 260 AA.
AC A0A0M0K194;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=lipoyl(octanoyl) transferase {ECO:0000256|ARBA:ARBA00012334};
DE EC=2.3.1.181 {ECO:0000256|ARBA:ARBA00012334};
DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000256|ARBA:ARBA00033331};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000256|ARBA:ARBA00031131};
GN ORFNames=Ctob_010306 {ECO:0000313|EMBL:KOO32574.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO32574.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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 -!- SIMILARITY: Belongs to the LipB family.
CC {ECO:0000256|ARBA:ARBA00007907}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO32574.1}.
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DR EMBL; JWZX01001735; KOO32574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0K194; -.
DR OrthoDB; 166876at2759; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000037460; 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 CDD; cd16444; LipB; 1.
DR HAMAP; MF_00013; LipB; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOO32574.1}.
FT DOMAIN 35..221
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 181
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-1"
FT BINDING 81..88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 150..152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 163..165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT SITE 147
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-3"
SQ SEQUENCE 260 AA; 27942 MW; CEDEC6F94FAEA0CF CRC64;
MTAPRRVVVQ RLSGLIGYED GLRLQHRLVQ RRKAGALADT LLLLEHAPVF TLGRLQASAA
NVLAAPEALA AAGASVVQSD RGGNVTFHGP GQLVAYPILD LAAGYRRDLH WYVERLEDVM
IGTAAQFGVS AVRGAPGHTG VWVGERKIGA IGVRVQRWLS SHGVALNADV DLSFFDMIVP
CGLHEAPQVT SLSRELGRTV SVGELRPRFE AAFAEAFECE LVDGAHVDEI EISGADLELS
RVTTKSVDPT RPPSPKMRAE
//
