ID A0A5P8E401_9BACT Unreviewed; 333 AA.
AC A0A5P8E401;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=C7Y71_001040 {ECO:0000313|EMBL:QFQ11723.1};
OS Pseudoprevotella muciniphila.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC Prevotellaceae; Pseudoprevotella.
OX NCBI_TaxID=2133944 {ECO:0000313|EMBL:QFQ11723.1, ECO:0000313|Proteomes:UP000249375};
RN [1] {ECO:0000313|EMBL:QFQ11723.1, ECO:0000313|Proteomes:UP000249375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E39 {ECO:0000313|EMBL:QFQ11723.1,
RC ECO:0000313|Proteomes:UP000249375};
RA Na S.W., Baik M.;
RL Submitted (NOV-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}.
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DR EMBL; CP033459; QFQ11723.1; -; Genomic_DNA.
DR RefSeq; WP_111897901.1; NZ_CP033459.1.
DR AlphaFoldDB; A0A5P8E401; -.
DR KEGG; alq:C7Y71_001040; -.
DR OrthoDB; 9787898at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000249375; 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 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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000249375};
KW Transferase {ECO:0000313|EMBL:QFQ11723.1}.
FT DOMAIN 36..221
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 333 AA; 37427 MW; D25635FB6E3FDA08 CRC64;
MTKFFFPAVE IVFPDDGIPR RAAFYLAAEE YVARTFPEGS YLFSWILNKT VVIGRNQVAH
KELDIDFCRG NGIDIIRRKS GGGAVFADRN NIMWSLVTYG GDVETVFGVY SKRMADALTE
VGVPVEVSGR NDILLENGRK ICGNAFYHLT NRNIVHGTML YDTTMELMQK SLLPAPEKLK
ARGVQSVRTR VGFIKDYYLG SIQELRSELT KVLCSRSLSF TSDDIREIEK IEATYYTDEY
LWGNVSGIVE TFSRHIDHCG EITISFSLLG SIIKDVTLSG DFFELEDAQS AFSTAFRGVP
FTHKDLTDAV LTHHPERSIR GLSTSVLIDM LHT
//
