ID D7DC60_STAHD Unreviewed; 95 AA.
AC D7DC60;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN OrderedLocusNames=Shell_0633 {ECO:0000313|EMBL:ADI31757.1};
OS Staphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 /
OS P8).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=591019 {ECO:0000313|EMBL:ADI31757.1, ECO:0000313|Proteomes:UP000002573};
RN [1] {ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.;
RT "Complete sequence of Staphylothermus hellenicus DSM 12710.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI31757.1, ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RX PubMed=22180806; DOI=10.4056/sigs.2054696;
RA Anderson I., Wirth R., Lucas S., Copeland A., Lapidus A., Cheng J.F.,
RA Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Pati A., Mikhailova N., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Staphylothermus hellenicus P8.";
RL Stand. Genomic Sci. 5:12-20(2011).
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}.
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DR EMBL; CP002051; ADI31757.1; -; Genomic_DNA.
DR RefSeq; WP_013142955.1; NC_014205.1.
DR AlphaFoldDB; D7DC60; -.
DR STRING; 591019.Shell_0633; -.
DR GeneID; 9233922; -.
DR KEGG; shc:Shell_0633; -.
DR eggNOG; arCOG03837; Archaea.
DR HOGENOM; CLU_181210_1_0_2; -.
DR OMA; IRIWARF; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000002573; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR InterPro; IPR019491; Lipoate_protein_ligase_C.
DR Pfam; PF10437; Lip_prot_lig_C; 1.
DR SUPFAM; SSF82649; SufE/NifU; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 12..63
FT /note="Lipoate protein ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10437"
SQ SEQUENCE 95 AA; 10771 MW; 1882ADC3A560DBEA CRC64;
MNNPIKKSIT YRVPGGKTLK IDVEIKDNTI IDIIISGDFF AYPEEGIELL ENDLKGKTIN
EAIRIIDDYR DKIKLLGISL ENIKNILIKI FHGVS
//