ID A0A2C7A6K5_9PROT Unreviewed; 187 AA.
AC A0A2C7A6K5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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};
DE Flags: Fragment;
GN ORFNames=CR162_17730 {ECO:0000313|EMBL:PHK93619.1};
OS Pseudoroseomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1335062 {ECO:0000313|EMBL:PHK93619.1, ECO:0000313|Proteomes:UP000223527};
RN [1] {ECO:0000313|EMBL:PHK93619.1, ECO:0000313|Proteomes:UP000223527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YW11 {ECO:0000313|EMBL:PHK93619.1,
RC ECO:0000313|Proteomes:UP000223527};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024732}.
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 -!- 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:PHK93619.1}.
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DR EMBL; PDNU01000040; PHK93619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C7A6K5; -.
DR OrthoDB; 9787061at2; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000223527; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 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 Pfam; PF03099; BPL_LplA_LipB; 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 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Ligase {ECO:0000313|EMBL:PHK93619.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000223527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..187
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 151
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-1"
FT BINDING 38..45
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 120..122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT SITE 117
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PHK93619.1"
SQ SEQUENCE 187 AA; 20342 MW; 7B47826B6F84987E CRC64;
EAGERVWLVE HPPLYTAGTS STPEGLVDAR FPVFAAGRGG QWTYHGPGQR TAYVMLDLDR
AHGAVPARDI RAYVHGLEEW IIRALDRFNV RGERREGRVG IWVADKVPGG FVQRENKIAA
IGVRVTRWVS WHGIALNVEP DLSHFGGIVP CGIRQHGVTS LAALGIPVTM AEADSALKAS
WAEVFGG
//
