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Database: UniProt
Entry: A0A0F3IV03_9PROT
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ID   A0A0F3IV03_9PROT        Unreviewed;       207 AA.
AC   A0A0F3IV03;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-NOV-2023, entry version 35.
DE   RecName: Full=Octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262};
DE            EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262};
DE   AltName: Full=Lipoate-protein ligase B {ECO:0000256|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoyl/octanoyl transferase {ECO:0000256|HAMAP-Rule:MF_00013};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013};
GN   Name=lipB {ECO:0000256|HAMAP-Rule:MF_00013};
GN   ORFNames=VZ95_04200 {ECO:0000313|EMBL:KJV10541.1};
OS   Elstera litoralis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Elstera.
OX   NCBI_TaxID=552518 {ECO:0000313|EMBL:KJV10541.1, ECO:0000313|Proteomes:UP000033774};
RN   [1] {ECO:0000313|EMBL:KJV10541.1, ECO:0000313|Proteomes:UP000033774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dia-1 {ECO:0000313|EMBL:KJV10541.1,
RC   ECO:0000313|Proteomes:UP000033774};
RA   Rahalkar M.C., Dhakephalkar P.K., Pore S.D., Arora P., Kapse N.G.,
RA   Pandit P.S.;
RT   "Draft genome sequence of Elstera litoralis.";
RL   Submitted (MAR-2015) 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, ECO:0000256|HAMAP-Rule:MF_00013,
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|ARBA:ARBA00000953, ECO:0000256|HAMAP-
CC         Rule:MF_00013, 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, ECO:0000256|HAMAP-
CC       Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00013}.
CC   -!- SIMILARITY: Belongs to the LipB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}.
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:KJV10541.1}.
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DR   EMBL; LAJY01000080; KJV10541.1; -; Genomic_DNA.
DR   RefSeq; WP_045774765.1; NZ_LAJY01000080.1.
DR   AlphaFoldDB; A0A0F3IV03; -.
DR   PATRIC; fig|552518.3.peg.4408; -.
DR   OrthoDB; 9787061at2; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000033774; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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, ECO:0000256|HAMAP-
KW   Rule:MF_00013}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013};
KW   Ligase {ECO:0000313|EMBL:KJV10541.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033774};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00013}.
FT   DOMAIN          29..207
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   ACT_SITE        170
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-1"
FT   BINDING         67..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   BINDING         152..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-2"
FT   SITE            136
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT                   ECO:0000256|PIRSR:PIRSR016262-3"
SQ   SEQUENCE   207 AA;  22567 MW;  1422FE15F5A4A768 CRC64;
     MEWRVTPGLT PYPEALAAMD ARADAIHAGT ADELIWLLEH PPLYTAGTSA QAEDLLDPRF
     PVYDAGRGGQ YTYHGPGQRV VYLMLDLKAR GRDVRAYVTS LEEWIIQSLA RLGVIGERRQ
     GRVGIWVQRG PLKEDKIAAI GVRIRRWVTL HGIAINVSPD LGHFTGIVPC GIQEHGVTSL
     ADLGLTASLA DLDAALAATR PTLFPNL
//
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