ID A0A0M4U733_9GAMM Unreviewed; 339 AA.
AC A0A0M4U733;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN Name=lplA {ECO:0000313|EMBL:ALF59889.1};
GN ORFNames=AOC03_07415 {ECO:0000313|EMBL:ALF59889.1};
OS Psychrobacter urativorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=45610 {ECO:0000313|EMBL:ALF59889.1, ECO:0000313|Proteomes:UP000059847};
RN [1] {ECO:0000313|EMBL:ALF59889.1, ECO:0000313|Proteomes:UP000059847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R10.10B {ECO:0000313|EMBL:ALF59889.1,
RC ECO:0000313|Proteomes:UP000059847};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Psychrobacter urativorans R10.10B.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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};
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; CP012678; ALF59889.1; -; Genomic_DNA.
DR RefSeq; WP_062534695.1; NZ_CP012678.1.
DR AlphaFoldDB; A0A0M4U733; -.
DR STRING; 45610.AOC03_07415; -.
DR KEGG; pur:AOC03_07415; -.
DR OrthoDB; 9787898at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000059847; Chromosome.
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: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 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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ALF59889.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 33..216
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 339 AA; 38730 MW; 1ABC5D753525645B CRC64;
MKLRILKSAV TNPWFNLATE DWIFNTLGND KKAPDSHTLF LWRNRETVVI GRSQNPWVEC
KTDKMEEDNV FLARRQSGGG AVFHDLGNTN FTFLSPKSDY DQNANFTIII NALKKLGIDA
TLSGRNDMQV GDKKISGSAF KHAADRSFHH GTLLVNADMQ KLGDYLNPHP LKLQAKGIKS
VRSRVANLVE FNDSINHEIL SNAIIEAFCD YYGQTVAVED LDENTLAKEP SLNKYYQQMA
DWEWRFGKTP EFSHRLETRF DWGMIDLHLD VKQAVISEVV IFSDALNVEL IELLKETLTG
IKYDKHEIQA KLDKLQTAHS DLAAHINDFE QWLIKEMES
//
