ID D3DI54_HYDTT Unreviewed; 344 AA.
AC D3DI54;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN OrderedLocusNames=HTH_1048 {ECO:0000313|EMBL:BAI69506.1};
OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobacter.
OX NCBI_TaxID=608538 {ECO:0000313|EMBL:BAI69506.1, ECO:0000313|Proteomes:UP000002574};
RN [1] {ECO:0000313|EMBL:BAI69506.1, ECO:0000313|Proteomes:UP000002574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo]
RC {ECO:0000313|Proteomes:UP000002574};
RX PubMed=20348262; DOI=10.1128/JB.00158-10;
RA Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT "Complete genome sequence of the thermophilic, obligately
RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT thermophilus TK-6.";
RL J. Bacteriol. 192:2651-2652(2010).
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; AP011112; BAI69506.1; -; Genomic_DNA.
DR RefSeq; WP_012963686.1; NC_017161.1.
DR AlphaFoldDB; D3DI54; -.
DR STRING; 608538.HTH_1048; -.
DR KEGG; hth:HTH_1048; -.
DR eggNOG; COG0095; Bacteria.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000002574; 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 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:BAI69506.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002574}.
FT DOMAIN 24..215
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 344 AA; 39292 MW; 376FCD975DFAAEDE CRC64;
MKIYRLGRVK NLRSITTFHA MARLGYTGLV ITEPEDTYIS IGYFDRLEDI IDYEKCRKLN
IPVIRREVGG GAVLLSEGQV FYQLILPKRL VPFKVEDAYK KFSKAVIETY KKLGIEVFYR
PINDLVLKSG KKISGQGAAD IGNFFVFVGN VLLRFDTKLM AELFKVQEEK FRDKIYKSLE
ENISWVERET GRSFSYKEVE SILVEEFSKV VDFEGEGEIG EDVFELADKL MKDMTSPEVL
FEDTGRKHAF IKLREGVYIR NAVRKAKGGL LKCEVYLVDG KIDRVKIYGD FTLVPKDALG
DFESSLKGLG LEEVDKKVRE FLEKVDMPGV EAKDLIYLLT GGES
//
