ID A0A285K866_9ENTR Unreviewed; 338 AA.
AC A0A285K866;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lipoate-protein ligase A {ECO:0000256|HAMAP-Rule:MF_01602};
DE EC=6.3.1.20 {ECO:0000256|HAMAP-Rule:MF_01602};
DE AltName: Full=Lipoate--protein ligase {ECO:0000256|HAMAP-Rule:MF_01602};
GN Name=lplA {ECO:0000256|HAMAP-Rule:MF_01602};
GN ORFNames=SAMN02744775_01987 {ECO:0000313|EMBL:SNY68782.1};
OS Enterobacter sp. CC120223-11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=1378073 {ECO:0000313|EMBL:SNY68782.1, ECO:0000313|Proteomes:UP000219512};
RN [1] {ECO:0000313|EMBL:SNY68782.1, ECO:0000313|Proteomes:UP000219512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC120223-11 {ECO:0000313|EMBL:SNY68782.1,
RC ECO:0000313|Proteomes:UP000219512};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC onto the lipoyl domains of lipoate-dependent enzymes.
CC {ECO:0000256|HAMAP-Rule:MF_01602}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01602};
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, ECO:0000256|HAMAP-Rule:MF_01602}.
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, ECO:0000256|HAMAP-Rule:MF_01602}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01602}.
CC -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group of
CC lipoic acid is attached via an amide linkage to the epsilon-amino group
CC of a specific lysine residue of lipoyl domains of lipoate-dependent
CC enzymes. {ECO:0000256|HAMAP-Rule:MF_01602}.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000256|HAMAP-
CC Rule:MF_01602}.
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DR EMBL; OBEF01000007; SNY68782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285K866; -.
DR OrthoDB; 9787898at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000219512; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16443; LplA; 1.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR HAMAP; MF_01602; LplA; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR023741; Lipoate_ligase_A.
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; PF03099; BPL_LplA_LipB; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01602};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01602};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01602};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01602}.
FT DOMAIN 29..216
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 76..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 134
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
SQ SEQUENCE 338 AA; 37661 MW; 8F6844E428964EFA CRC64;
MSTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STSIVLNALN ALGVTAEASG
RNDLVVKTAE GDRKVSGSAY RETMDRGFHH GTLLLNADLS RLANYLNPDK KKLQAKGITS
VRGRVANLVE LLPGVTHEQI SKAVTEAFFT HYGERVEAEV ISPDKTPDLP NFAETFARQS
SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGHITRAQ VFTDSLNPAP LEALAAGLQG
CLYRADVLQQ ECEALIGAFP EQEKELRELS AWVAGAVR
//
