ID A0A1B1MWK0_9BACL Unreviewed; 334 AA.
AC A0A1B1MWK0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=AWM70_02360 {ECO:0000313|EMBL:ANS73562.1};
OS Paenibacillus yonginensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=1462996 {ECO:0000313|EMBL:ANS73562.1, ECO:0000313|Proteomes:UP000092573};
RN [1] {ECO:0000313|EMBL:ANS73562.1, ECO:0000313|Proteomes:UP000092573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY84 {ECO:0000313|EMBL:ANS73562.1,
RC ECO:0000313|Proteomes:UP000092573};
RA Kim Y.J., Yang D.C., Sukweenadhi J.;
RT "Complete Genome Sequence of Paenibacillus yonginensis DCY84, a novel Plant
RT Growth-Promoting Bacteria with Elicitation of Induced Systemic
RT Resistance.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[lipoyl-carrier protein] + (R)-lipoate + ATP = N(6)-
CC [(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate +
CC H(+); 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:ARBA00048037};
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}.
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DR EMBL; CP014167; ANS73562.1; -; Genomic_DNA.
DR RefSeq; WP_068694025.1; NZ_CP014167.1.
DR AlphaFoldDB; A0A1B1MWK0; -.
DR STRING; 1462996.AWM70_02360; -.
DR KEGG; pyg:AWM70_02360; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000092573; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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:0017118; F:lipoyltransferase activity; IEA:TreeGrafter.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16443; LplA; 1.
DR FunFam; 3.30.930.10:FF:000072; Lipoate--protein ligase; 1.
DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
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 NCBIfam; TIGR00545; lipoyltrans; 1.
DR PANTHER; PTHR12561; LIPOATE-PROTEIN LIGASE; 1.
DR PANTHER; PTHR12561:SF3; LIPOYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF10437; Lip_prot_lig_C; 1.
DR Pfam; PF21948; LplA-B_cat; 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:ANS73562.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000092573}.
FT DOMAIN 27..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 334 AA; 38090 MW; 1D8CCB574C7A6D41 CRC64;
MLFIDNEGIT DASVNLAIEE YALRHLPADE TYLLFYINAP SIIIGKHQNT IEEINAEYVK
ENGIQVVRRL SGGGAVYHDL GNLNFSFITK DDGESFHNFR KFTQPVVEAL RNFGVNAELT
GRNDLQVGDQ KISGNAQFST RGRMFSHGTL MFNLNLDHVA ASLHANPEKF KSKSTKSVRS
RVANIIDFMD NKITIEEFRS ELLRYIFGMD PDAVPKYVLK EEDWAKIHKI SEERYKNWDW
NYGLSPESNV KHSRKFPVGI IDLRMNIKEG HIEEIKIYGD FFGVGDVADI ENLLRGVKYE
ESAVRAALEG TDLKHYFGNL EPDDFVGLVF LEEE
//
