ID G9YZ72_9ENTR Unreviewed; 338 AA.
AC G9YZ72;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Lipoate-protein ligase A {ECO:0000256|HAMAP-Rule:MF_01602};
DE EC=6.3.1.20 {ECO:0000256|HAMAP-Rule:MF_01602};
DE AltName: Full=Lipoate--protein ligase {ECO:0000256|HAMAP-Rule:MF_01602};
GN Name=lplA {ECO:0000256|HAMAP-Rule:MF_01602};
GN ORFNames=HMPREF0880_00517 {ECO:0000313|EMBL:EHM51138.1};
OS Yokenella regensburgei ATCC 43003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Yokenella.
OX NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM51138.1, ECO:0000313|Proteomes:UP000003044};
RN [1] {ECO:0000313|EMBL:EHM51138.1, ECO:0000313|Proteomes:UP000003044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM51138.1,
RC ECO:0000313|Proteomes:UP000003044};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC onto the lipoyl domains of lipoate-dependent enzymes.
CC {ECO:0000256|HAMAP-Rule:MF_01602}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01602};
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, ECO:0000256|HAMAP-Rule:MF_01602}.
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, ECO:0000256|HAMAP-Rule:MF_01602}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01602}.
CC -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group of
CC lipoic acid is attached via an amide linkage to the epsilon-amino group
CC of a specific lysine residue of lipoyl domains of lipoate-dependent
CC enzymes. {ECO:0000256|HAMAP-Rule:MF_01602}.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000256|HAMAP-
CC Rule:MF_01602}.
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:EHM51138.1}.
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DR EMBL; AGCL01000008; EHM51138.1; -; Genomic_DNA.
DR RefSeq; WP_006817042.1; NZ_JH417862.1.
DR AlphaFoldDB; G9YZ72; -.
DR STRING; 1002368.HMPREF0880_00517; -.
DR GeneID; 66905437; -.
DR PATRIC; fig|1002368.3.peg.467; -.
DR HOGENOM; CLU_022986_0_1_6; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000003044; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01602; LplA; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR023741; Lipoate_ligase_A.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01602};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01602};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01602};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01602}.
FT DOMAIN 29..216
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 76..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 134
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
SQ SEQUENCE 338 AA; 37937 MW; 271A90046B2B301B CRC64;
MSTLRLLISD SHDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
MEDDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STAIVLNALQ ALGVTAEASG
RNDLIVKTAE GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLQAKGITS
VRGRVANLTE LLPGITHEQI CDAIREAFFT HYGERVEAEV ISPDKAPDLP NFAETFARQS
SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGHITRIQ VFTDSLNPAP LEALADRLQG
SLYRADMLQQ ACEALLVDFP DQENELREVS AWMASAVR
//
