ID C8S5G4_9RHOB Unreviewed; 358 AA.
AC C8S5G4;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=Rsw2DRAFT_3293 {ECO:0000313|EMBL:EEW23777.1};
OS Rhodobacter sp. SW2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW23777.1, ECO:0000313|Proteomes:UP000010121};
RN [1] {ECO:0000313|EMBL:EEW23777.1, ECO:0000313|Proteomes:UP000010121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW2 {ECO:0000313|EMBL:EEW23777.1,
RC ECO:0000313|Proteomes:UP000010121};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Emerson D.;
RT "The draft genome of Rhodobacter sp. SW2.";
RL Submitted (AUG-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEW23777.1}.
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DR EMBL; ACYY01000034; EEW23777.1; -; Genomic_DNA.
DR RefSeq; WP_008033019.1; NZ_ACYY01000034.1.
DR AlphaFoldDB; C8S5G4; -.
DR STRING; 371731.Rsw2DRAFT_3293; -.
DR eggNOG; COG0095; Bacteria.
DR OrthoDB; 9787898at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000010121; 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 PANTHER; PTHR43679:SF4; LIPOATE--PROTEIN LIGASE; 1.
DR PANTHER; PTHR43679; OCTANOYLTRANSFERASE LIPM-RELATED; 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:EEW23777.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010121}.
FT DOMAIN 29..220
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 358 AA; 38452 MW; 69BAEF011DA4B6BE CRC64;
MRLRVIDFGL VPGLRSQAVY HGLAETLGPD SDPILSLASP ATPYVCVGMH QDIEKEVDTA
FCAAHGLPVW RRQVGGGAVY LDHNQLFTHF IYPEAKAPSR ADQLYPMFIE PVVRTYREMG
INAVWRPVND IQVDGRKIGG TGAASIGQAT VMVGSFLLDF DTATMAKCLK VPSEKFRDKL
RQTLDDYMTT MVKELGHLPD RADLKARFLR HCADALGVQP VADQPTRAEW VAIEQAEAML
SDPEWTDVQH RKTVALGVKI AADTHLTEAA RKAPGGLVRV NLLAREGRVA DLLISGDFTC
LPPDGVDRLC DSLKGVALDE AALTAAATAA IARLGLDLPG VAAADLAATI LAAAEGAP
//
