ID S0ARX0_FERAC Unreviewed; 219 AA.
AC S0ARX0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Probable octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013};
DE EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_00013};
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=FACI_IFERC00001G0870 {ECO:0000313|EMBL:AGO60850.1};
OS Ferroplasma acidarmanus Fer1.
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Ferroplasmaceae; Ferroplasma.
OX NCBI_TaxID=333146 {ECO:0000313|EMBL:AGO60850.1, ECO:0000313|Proteomes:UP000014660};
RN [1] {ECO:0000313|EMBL:AGO60850.1, ECO:0000313|Proteomes:UP000014660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=fer1 {ECO:0000313|Proteomes:UP000014660};
RX PubMed=17267615; DOI=10.1073/pnas.0604851104;
RA Allen E.E., Tyson G.W., Whitaker R.J., Detter J.C., Richardson P.M.,
RA Banfield J.F.;
RT "Genome dynamics in a natural archaeal population.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1883-1888(2007).
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|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:0000256|ARBA:ARBA00000953, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004821, ECO:0000256|HAMAP-
CC Rule:MF_00013}.
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}.
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DR EMBL; CP004145; AGO60850.1; -; Genomic_DNA.
DR RefSeq; WP_009886902.1; NC_021592.1.
DR AlphaFoldDB; S0ARX0; -.
DR GeneID; 16025035; -.
DR KEGG; fac:FACI_IFERC01G0870; -.
DR PATRIC; fig|333146.12.peg.884; -.
DR HOGENOM; CLU_035168_3_1_2; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000014660; Chromosome.
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 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:AGO60850.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014660};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00013}.
FT DOMAIN 35..207
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 174
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
FT BINDING 71..78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
FT BINDING 142..144
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
FT BINDING 155..157
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
FT SITE 139
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013"
SQ SEQUENCE 219 AA; 25047 MW; 0474BEAD033EAAF9 CRC64;
MQQKGVTNYW TDLEKVSYSD ALDIQYNLVA RRKENKIPDT ILFLDHYNVY TIGRKSDPEN
YRNVNVIKTD RGGDVTYHGE GQLITYFIFD VRINGKKEVR KLLENIEESY IAMLKTYGYN
AMLYGEPGIW IDKGGVKNKV ASLGMAVDDY VSYHGMALNI SASVLNGFRL INPCGMNSSV
ISYVDIPRED AIKGLLKEFS RHFGEFSYID KEKLIRTPV
//