ID J5WN68_9FIRM Unreviewed; 333 AA.
AC J5WN68;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=HMPREF1152_1849 {ECO:0000313|EMBL:EJU23172.1};
OS Mogibacterium sp. CM50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU23172.1, ECO:0000313|Proteomes:UP000003142};
RN [1] {ECO:0000313|EMBL:EJU23172.1, ECO:0000313|Proteomes:UP000003142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM50 {ECO:0000313|EMBL:EJU23172.1,
RC ECO:0000313|Proteomes:UP000003142};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU23172.1}.
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DR EMBL; ALNL01000012; EJU23172.1; -; Genomic_DNA.
DR RefSeq; WP_009643503.1; NZ_ALNL01000012.1.
DR AlphaFoldDB; J5WN68; -.
DR STRING; 936375.HMPREF1152_1849; -.
DR PATRIC; fig|936375.3.peg.424; -.
DR eggNOG; COG0095; Bacteria.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000003142; 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:EJU23172.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003142};
KW Transferase {ECO:0000313|EMBL:EJU23172.1}.
FT DOMAIN 28..211
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 333 AA; 37439 MW; A161A454C8250F0F CRC64;
MNLRYTETDC TNPFINLATE EYMTFRATEG EVTMYLWQNA NTVVIGKNQN PWRECRVESM
KAGGCKLARR ISGGGAVYHD LGNLNFTFIA REDEYNIPKQ TEVILEAVRI LGINAEKTGR
NDLTIDGMKF SGHAYYRSHG YCYHHGTIMF DVDPAPLGEY LNVSAAKLKS KGVKSVRSRV
TNLIDHKPDI TLKELKDALY EAFAKVYAGT PERFDTPSPD SNTELKALVD KYSSEDWRYG
RKIPFTTSIT ERLDWGGIDI ELQVEGGFIK DCGLYSDSLE TAVFDELRDK LLGCKYNKAA
MSTLVEGMLP YAPASKEYQI CSDITDLIAD GIM
//
