ID   W0E5Z5_9FIRM            Unreviewed;       334 AA.
AC   W0E5Z5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=DESME_03790 {ECO:0000313|EMBL:AHF06275.1};
OS   Desulfitobacterium metallireducens DSM 15288.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF06275.1, ECO:0000313|Proteomes:UP000010847};
RN   [1] {ECO:0000313|EMBL:AHF06275.1, ECO:0000313|Proteomes:UP000010847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG   DOE Joint Genome Institute;
RA   Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP007032; AHF06275.1; -; Genomic_DNA.
DR   RefSeq; WP_006715226.1; NZ_CP007032.1.
DR   AlphaFoldDB; W0E5Z5; -.
DR   STRING; 871968.DESME_03790; -.
DR   KEGG; dmt:DESME_03790; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_022986_0_1_9; -.
DR   OrthoDB; 9788148at2; -.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000010847; 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:AHF06275.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010847};
KW   Transferase {ECO:0000313|EMBL:AHF06275.1}.
FT   DOMAIN          32..215
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   334 AA;  38200 MW;  7DCEDEE13E1C2B0B CRC64;
     MTQPVQTKIV LSDSFDPWHN LALEEFLFRN VEKNQVILYL WQNQNTVVIG RNQNAWKECR
     CTKLEDDGGK LARRLSGGGA VFHDLGNLNF TFILDRALYD LKKQLQVILE AVKKLGIHAE
     FTGRNDLTVD GKKFSGNAFY FEGDKAYHHG TIMIDVDVQK VSAYLQVSKE KMASKGVDSV
     RSRVTNLHNY RPELTIDEMK ETLKQSFQEL YGESPEPVLI KENDHDLKEL YAKYSSWDWL
     YGKTPQFDVV FETRFPWGGI DLGLTLNKGI VTESKIYSDA MNANLIEQIA SSLIERPLKS
     ESIGKGLDVL EVNEEDKPII EDMKTWLQTK IAEI
//