ID A0A117M2V2_9BACT Unreviewed; 334 AA.
AC A0A117M2V2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=XD94_0522 {ECO:0000313|EMBL:KUK81311.1};
OS Mesotoga prima.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=1184387 {ECO:0000313|EMBL:KUK81311.1, ECO:0000313|Proteomes:UP000054092};
RN [1] {ECO:0000313|Proteomes:UP000054092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:ARBA00001121};
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:KUK81311.1}.
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DR EMBL; LGGP01000066; KUK81311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117M2V2; -.
DR PATRIC; fig|1184387.3.peg.867; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000054092; 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:KUK81311.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000313|EMBL:KUK81311.1}.
FT DOMAIN 35..218
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 334 AA; 38397 MW; 6F561CFD05D3AF45 CRC64;
MSEVGKIPST IFVESDSFDP WLNLAVEEYL LNSFAKENIV LYLWQNENTV VIGRNQNAWQ
ECRLDNLHRD GGKLARRLSG GGAVFHDLGN LNFTFLLPKR EYDLHRQLSV IVDGVKSVGI
DAHFSGRNDI LAEGRKFSGN AFYHGQYASY HHGTILVDVD TRRLSEYLNV SRAKIESKGV
KSVVSRVVNL RELKPDLTIE RMKEAMYRGF AEEYGRIYEV LDFDELRKSL DVKSLYEKYS
SKEWLLGKSP EFNFKIGNRF SWGGIELLFT SKKGIISDVI IYSDSMDVDF IEQLKRELIR
VEFSRVAIVK AIEMLPDCSE RNDIIAWLQT TDLN
//