LIPB_GLOVI
ID LIPB_GLOVI Reviewed; 222 AA.
AC Q7ND22;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
GN Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013}; OrderedLocusNames=gll4414;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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:0000255|HAMAP-Rule:MF_00013}.
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:0000255|HAMAP-Rule:MF_00013};
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:0000255|HAMAP-Rule:MF_00013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
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:0000255|HAMAP-Rule:MF_00013}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC Rule:MF_00013}.
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DR EMBL; BA000045; BAC92355.1; -; Genomic_DNA.
DR RefSeq; NP_927360.1; NC_005125.1.
DR RefSeq; WP_011144397.1; NC_005125.1.
DR AlphaFoldDB; Q7ND22; -.
DR SMR; Q7ND22; -.
DR STRING; 251221.35214989; -.
DR PRIDE; Q7ND22; -.
DR EnsemblBacteria; BAC92355; BAC92355; BAC92355.
DR KEGG; gvi:gll4414; -.
DR PATRIC; fig|251221.4.peg.4444; -.
DR eggNOG; COG0321; Bacteria.
DR HOGENOM; CLU_035168_1_0_3; -.
DR InParanoid; Q7ND22; -.
DR OMA; GEVTYHC; -.
DR OrthoDB; 1806796at2; -.
DR PhylomeDB; Q7ND22; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR CDD; cd16444; LipB; 1.
DR Gene3D; 3.30.930.10; -; 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 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; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Octanoyltransferase"
FT /id="PRO_0000062839"
FT DOMAIN 32..207
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 170
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 72..79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 139..141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 152..154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 136
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ SEQUENCE 222 AA; 24298 MW; 6B89EC6B726437D6 CRC64;
MGRCLLIEPG LVPYLTAWEW QRQLMATRIA HRDRPDVLML LEHPPVYTLG QGADAKHVLV
DPASIELYRT ERGGEVTYHG PGQLVGYPIL DLTGYRQDLH WYLRTLEQVL IEVLADFGVQ
GEREAGFTGV WAGGRKIAAL GIKVSRWVTM HGFALNVDPD LDAFARIVPC GLTRPVGSLV
QLCPGVSVEQ VQPVVACAFA RVFGVQCEPG ALEACLAVKP GC
