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Database: UniProt
Entry: S0ARX0_FERAC
LinkDB: S0ARX0_FERAC
Original site: S0ARX0_FERAC 
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
//
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