ID A0A1W1ZMF4_9FIRM Unreviewed; 326 AA.
AC A0A1W1ZMF4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=SAMN02745168_1257 {ECO:0000313|EMBL:SMC49740.1};
OS Papillibacter cinnamivorans DSM 12816.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Papillibacter.
OX NCBI_TaxID=1122930 {ECO:0000313|EMBL:SMC49740.1, ECO:0000313|Proteomes:UP000192790};
RN [1] {ECO:0000313|EMBL:SMC49740.1, ECO:0000313|Proteomes:UP000192790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12816 {ECO:0000313|EMBL:SMC49740.1,
RC ECO:0000313|Proteomes:UP000192790};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWXW01000002; SMC49740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1ZMF4; -.
DR STRING; 1122930.SAMN02745168_1257; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000192790; 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:SMC49740.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000192790}.
FT DOMAIN 30..213
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 326 AA; 36604 MW; 7B65D49BE09976E6 CRC64;
MISQLFTFRS PGTHPFENQA LESFFLEAVP DDACVLYLWR NDRTVVIGKN QNAWKECRVS
RLEGEGGHLA RRISGGGAVY HDLHNLNFTF LLPTREYDED RQLEVILRAV RDLGIDASKS
GRNDLTAEGR KFSGSAYWHG RGRSLHHGTL LVGSDLDTLT RYLSVSPDKL KSKGVESVRS
RVVNLAQLCP GLTVESLVPR LTEAFGEVCG LRPRAWELTG KDRERVSELT GRFSSREWRF
GQNVPFTAEL SRRFPWGGVE LSLRVEGGIV RQAAVYTDAM ETELFDTLSR SLEGAPFSSR
DLVKHLSFSD SALLADLRAW LETEAM
//
