ID   LIPB_PYRAE              Reviewed;         224 AA.
AC   Q8ZUR4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Probable 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=PAE2651;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64342.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZUR4; -.
DR   SMR; Q8ZUR4; -.
DR   STRING; 178306.PAE2651; -.
DR   EnsemblBacteria; AAL64342; AAL64342; PAE2651.
DR   KEGG; pai:PAE2651; -.
DR   PATRIC; fig|178306.9.peg.1974; -.
DR   eggNOG; arCOG01942; Archaea.
DR   HOGENOM; CLU_035168_3_1_2; -.
DR   InParanoid; Q8ZUR4; -.
DR   OMA; GEVTYHC; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000002439; 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   PIRSF; PIRSF016262; LPLase; 1.
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..224
FT                   /note="Probable octanoyltransferase"
FT                   /id="PRO_0000062905"
FT   DOMAIN          28..199
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        161
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         66..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         130..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         143..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   SITE            127
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ   SEQUENCE   224 AA;  24377 MW;  A0C009794227C311 CRC64;
     MKILWIGRTQ YAEAWRLMKS LHCAVAQGLT GDIALVTEHE PVVTVGKHGR LNNVIKWDVP
     VYLVERGGDA TYHGPGQAVV YPIVALRWPL KRYIDAIEDA VIKTLGTYGI LAGKKQGHRG
     VWVGDRKIAS IGIAVENNVA YHGVAINVTI DPREFARINP CGLPASTMIS MKELGVVAEV
     RDVGIETAKK LALELGLTPE LISKPPEVPQ VAEELKPVRV AINA