ID D4E713_SEROD Unreviewed; 337 AA.
AC D4E713;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 ECO:0000313|EMBL:EFE94389.1};
GN ORFNames=HMPREF0758_3963 {ECO:0000313|EMBL:EFE94389.1};
OS Serratia odorifera DSM 4582.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE94389.1, ECO:0000313|Proteomes:UP000005723};
RN [1] {ECO:0000313|EMBL:EFE94389.1, ECO:0000313|Proteomes:UP000005723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE94389.1,
RC ECO:0000313|Proteomes:UP000005723};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2010) 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:EFE94389.1}.
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DR EMBL; ADBY01000054; EFE94389.1; -; Genomic_DNA.
DR RefSeq; WP_004963623.1; NZ_GG753567.1.
DR AlphaFoldDB; D4E713; -.
DR STRING; 667129.HMPREF0758_3963; -.
DR HOGENOM; CLU_022986_0_1_6; -.
DR OrthoDB; 9787898at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000005723; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005723};
KW Transferase {ECO:0000313|EMBL:EFE94389.1}.
FT DOMAIN 28..215
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 75..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 133
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01602"
SQ SEQUENCE 337 AA; 37440 MW; 106591ADFE618F2F CRC64;
MTSLRLLISD SYDPWFNLAV EECIFREMNS QVILFLWRNA ETVVIGQSQN PWKECNTRRM
EQDGIRLARR SSGGGAVFHD LGNTCFTFMA GKPGYDKAVS TNIILQALSR LGINASASGR
NDLVIETADG IRKISGSAYR ETADRGFHHG TLLLNADLNR LADYLNPDPK KLQAKGITSV
RSRVANLAEF APDITHQQVC EAIIQTFFAY YGSSATAEVI SPDAFPDLPN FADQFAKQSS
WQWNFGKAPA FSHLLNERFS WGGVDIFFDV EQGAITRAQI FSDSLQPAPL QQLAGLLVGC
AYRSDAVAAC CQRLLADYPQ QATELQQLQR WLSEVIK
//
