ID   J9GM58_9ZZZZ            Unreviewed;       217 AA.
AC   J9GM58;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=EVA_03324 {ECO:0000313|EMBL:EJX08569.1};
OS   gut metagenome.
OC   unclassified sequences; metagenomes; organismal metagenomes.
OX   NCBI_TaxID=749906 {ECO:0000313|EMBL:EJX08569.1};
RN   [1] {ECO:0000313|EMBL:EJX08569.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23251564; DOI=10.1371/journal.pone.0051521;
RA   Alcaide M., Messina E., Richter M., Bargiela R., Peplies J., Huws S.A.,
RA   Newbold C.J., Golyshin P.N., Simon M.A., Lopez G., Yakimov M.M., Ferrer M.;
RT   "Gene sets for utilization of primary and secondary nutrition supplies in
RT   the distal gut of endangered iberian lynx.";
RL   PLoS ONE 7:E51521-E51521(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = AMP +
CC         diphosphate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier
CC         protein]; Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC         COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:456215; EC=6.3.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00043803};
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005124}.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00005085}.
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:EJX08569.1}.
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DR   EMBL; AMCI01000591; EJX08569.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9GM58; -.
DR   UniPathway; UPA00537; UER00594.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR019491; Lipoate_protein_ligase_C.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   PANTHER; PTHR12561; LIPOATE-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12561:SF3; LIPOYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF82649; SufE/NifU; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EJX08569.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          1..93
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   217 AA;  24055 MW;  15DFBF9F4FF38410 CRC64;
     MGAPATVSGR NDILLEGGGK ICGNAFYHLN DRNIVHGTML YGTNFEAMSQ ALTPDKAKLQ
     SKGVTSVKSR VSVLKDVLPL SLPTLRQCLR QQLTDRCIRL TEDDVQTIKA IEADYYDPIY
     LFGKSQHTDT TLQGHIDGCG MITFQFSLKG TLIDNVRLKG DFFTLEDASL AFRSAWSGVE
     FTPTHLIAAL HERHPERSIR GLTVEQLSAL ITQEFPK
//