ID A0A1H7Z038_9FIRM Unreviewed; 334 AA.
AC A0A1H7Z038;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=SAMN05216180_0321 {ECO:0000313|EMBL:SEM50958.1};
OS Hydrogenoanaerobacterium saccharovorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Hydrogenoanaerobacterium.
OX NCBI_TaxID=474960 {ECO:0000313|EMBL:SEM50958.1, ECO:0000313|Proteomes:UP000199158};
RN [1] {ECO:0000313|EMBL:SEM50958.1, ECO:0000313|Proteomes:UP000199158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5070 {ECO:0000313|EMBL:SEM50958.1,
RC ECO:0000313|Proteomes:UP000199158};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOCG01000001; SEM50958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7Z038; -.
DR STRING; 474960.SAMN05216180_0321; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000199158; 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:SEM50958.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199158}.
FT DOMAIN 30..213
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 334 AA; 38104 MW; 59CB2B1B92C99772 CRC64;
MITKTQYYIT QNTLPYRNLA LEEYLLETVP VGTCVLYLWQ NRFTVVAGRN QNAWQECRIA
ELEADRGYFA RRLSGGGAVF HDLGNLNFTF LVREEDYNVS RQIDVILSAV KAFGIQAEKS
GRNDITVQGR KFSGNAFYRS GGSCYHHGTL LVNVNMQDLS RYLNVSAAKL SSKGVSSVKS
RVANLIDFCP ELTIKQLQHS LINSFAKTYG CTPSCIADDK IDWQRVEQLT EKFSSWEWKF
GHRLEFQYQL THRFVWGDIQ IQLSLDRGRV LQAAVYSDAM DAWLIAQIPQ QVRGCVFSSK
ALAASLNPLL QDTKGEQEKK IIYDLQDLIH KQEF
//
