ID   LIPL_ANOFW              Reviewed;         275 AA.
AC   B7GML0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_02119};
DE            EC=2.3.1.204 {ECO:0000255|HAMAP-Rule:MF_02119};
DE   AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase {ECO:0000255|HAMAP-Rule:MF_02119};
GN   Name=lipL {ECO:0000255|HAMAP-Rule:MF_02119}; OrderedLocusNames=Aflv_2759;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
CC   -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the octanoyl
CC       moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of
CC       lipoate-dependent enzymes. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-
CC         [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage
CC         complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein];
CC         Xref=Rhea:RHEA:20213, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501,
CC         Rhea:RHEA-COMP:10503, Rhea:RHEA-COMP:10504, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:78809; EC=2.3.1.204; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02119};
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC       intermediate. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC       {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACJ35112.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000922; ACJ35112.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041639174.1; NC_011567.1.
DR   AlphaFoldDB; B7GML0; -.
DR   SMR; B7GML0; -.
DR   STRING; 491915.Aflv_2759; -.
DR   EnsemblBacteria; ACJ35112; ACJ35112; Aflv_2759.
DR   KEGG; afl:Aflv_2759; -.
DR   PATRIC; fig|491915.6.peg.2842; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_067270_0_0_9; -.
DR   Proteomes; UP000000742; Chromosome.
DR   GO; GO:0016415; F:octanoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_02119; LipL; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR024897; LipL.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..275
FT                   /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT                   /id="PRO_0000410832"
FT   DOMAIN          42..246
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        145
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
FT   SITE            157
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
SQ   SEQUENCE   275 AA;  30728 MW;  D2F5F453930DE9C5 CRC64;
     MMSELLQQQT WRVIDHTSLG PSFDAKQSFA FDDALCESVG SGQSQPVVRL WVHHQTVVLG
     IQDTKLPYIE KGLAYLHEQG WRTIVRNSGG LAVVLDEGVL NVSLIFPDTK KGIDIDRGYE
     AMATLIAHML PEAHVQTGEV VGSYCPGSFD LSINGKKFAG ISQRRIRGGV AVQVYICVNG
     SGAERAGWIR EFYERSLAGE QTKFTYPTIV PHTMASLSEL LSKEMTVSAL VIRLYEALQA
     FGSRLEPSSL TPAEWERYYM YFQRMIDRNE TMLPT