ID A0A4Q2LZQ4_9BACL Unreviewed; 339 AA.
AC A0A4Q2LZQ4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=EBB07_10270 {ECO:0000313|EMBL:RXZ82450.1};
OS Paenibacillaceae bacterium.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae.
OX NCBI_TaxID=2003592 {ECO:0000313|EMBL:RXZ82450.1, ECO:0000313|Proteomes:UP000289243};
RN [1] {ECO:0000313|EMBL:RXZ82450.1, ECO:0000313|Proteomes:UP000289243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAVE-418 {ECO:0000313|EMBL:RXZ82450.1,
RC ECO:0000313|Proteomes:UP000289243};
RA Coelho C., Verissimo A., Tiago I.;
RT "Draft Genome Sequence of strain CAVE-418, a bacterium isolated from a
RT karstic cave dripping water in Portugal.";
RL Submitted (OCT-2018) 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:RXZ82450.1}.
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DR EMBL; REGQ01000008; RXZ82450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q2LZQ4; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000289243; 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:RXZ82450.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000289243}.
FT DOMAIN 27..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 339 AA; 38140 MW; 356A7F2DE79CC926 CRC64;
MQFIDNKGIT DPAINLALEE YALRNLPMDD SYLLFYINEP SIIIGKNQNT IEEINKGYVE
ENGIHVVRRL SGGGAVYHDL GNLNFSFLTK DDGQSFSNFA KFTQPVIDTL QKLSVNAALT
GRNDIQVGEQ KISGNAQFTT KGRLFTHGTL LFNSAMENVA SALQVKPMKI ESKSTKSVRS
RVANISEFLA TPLTIEQFRE TLLRELFQCD PTQIQVYPLT DEQWAAVHKL ADERYRTWDW
NYGHSPKFNL QHAVKFPSGI VDVRLLVEEG KIADCKIYGD FFGILDVAEL EKALCGTRYV
EADIRSVLEG IDLSRYFGQM SLEAFVALLL QQEQPPALS
//
