ID A0A1G8C8Y1_9BACI Unreviewed; 331 AA.
AC A0A1G8C8Y1;
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 {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=SAMN05192534_10599 {ECO:0000313|EMBL:SDH41832.1};
OS Alteribacillus persepolensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=568899 {ECO:0000313|EMBL:SDH41832.1, ECO:0000313|Proteomes:UP000199163};
RN [1] {ECO:0000313|EMBL:SDH41832.1, ECO:0000313|Proteomes:UP000199163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21632 {ECO:0000313|EMBL:SDH41832.1,
RC ECO:0000313|Proteomes:UP000199163};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNDK01000005; SDH41832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8C8Y1; -.
DR STRING; 568899.SAMN05192534_10599; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000199163; Unassembled WGS sequence.
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:SDH41832.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199163}.
FT DOMAIN 29..216
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 331 AA; 38130 MW; A9A48B2B823532C7 CRC64;
MRFIDNKGVT DPQINLAIEE FALEHMDLDK EDTYLLFYVN RPSIIIGKNQ NTIEEINVDY
VEENDIRVVR RLSGGGAVYH DLGNLNFSFL TKDDGNSFHN FKKFTEPVIE ALNNMGVPAE
LSGRNDIQAN GKKISGNAQF TTKGRMYSHG TLMLDSQIEH VVSALNVKDE KIKSKGIKSI
KSRVGNINDF LDTPLSINEF KQTLLRHIFH SEDHIPVYHL TKDDWDKVHV IAEKRYKNWN
WNYGKSPAFD VERSKKFDAG LIDIRFNVKK GYIETCKIYG DYFGVKDTKE IEHALEGQKY
EVRALKEALE PFDLHEYFGP VNEEDILSLL Y
//
