ID A0A1Y5JXS4_9BACL Unreviewed; 331 AA.
AC A0A1Y5JXS4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=B1748_33455 {ECO:0000313|EMBL:OUS68647.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS68647.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS68647.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS68647.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-2017) 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}.
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:OUS68647.1}.
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DR EMBL; MXQD01000069; OUS68647.1; -; Genomic_DNA.
DR RefSeq; WP_087572312.1; NZ_MXQD01000069.1.
DR AlphaFoldDB; A0A1Y5JXS4; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000195591; Unassembled WGS sequence.
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:OUS68647.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000195591}.
FT DOMAIN 27..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 331 AA; 37452 MW; 67A6C3EE3A15282F CRC64;
MRFVSNKGIT DPAINLALEE YILRSLPSEH DYLLFYINEP SIIIGKNQNT VEEINAEYVE
ASKLHVVRRL SGGGAVYHDL GNLNFSFIMQ DDGGSFHNFR KFTEPVVKAL RKLGVEAELT
GRNDLQVGER KISGNAQFHT RGKMFSHGTL LFDSEIENVV SALKVNAEKY VSKATKSIRS
RVANISEFLP EPMTVEQFRE TLLQSIFEDR GGEPAAYELT EADWEKVHKL ADERYRSWEW
NYGRSPAFNV QQRKRIEGVG TFDVRLQVED GSISEAAIYG DYFGRGDSAE VAAKLAGTKY
DAAALRQLTE TLDLPYYFGP ITEEQWLSLL M
//
