ID A0A1R4B2N4_9VIBR Unreviewed; 338 AA.
AC A0A1R4B2N4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN Name=lplA {ECO:0000313|EMBL:SJL83177.1};
GN ORFNames=VPAL9027_01126 {ECO:0000313|EMBL:SJL83177.1};
OS Vibrio palustris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1918946 {ECO:0000313|EMBL:SJL83177.1, ECO:0000313|Proteomes:UP000189475};
RN [1] {ECO:0000313|EMBL:SJL83177.1, ECO:0000313|Proteomes:UP000189475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 9027 {ECO:0000313|EMBL:SJL83177.1,
RC ECO:0000313|Proteomes:UP000189475};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUFT01000002; SJL83177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4B2N4; -.
DR STRING; 1918946.VPAL9027_01126; -.
DR OrthoDB; 9787898at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000189475; 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:SJL83177.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189475}.
FT DOMAIN 29..216
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 338 AA; 38251 MW; 9DF38CEFF791B397 CRC64;
MNKTRVLISN SHNPWFNLAV EDIIFRSMSA DQRVLFLWQN DDTVVIGRAQ NPWKECRTEQ
MERDNVTLAR RQTGGGAVFH DLGNTCFTFM AGKPEYDKTV STQIVLDALA SLGIDAQANG
RNDLVVSDEN GIRKFSGSAY RETINRGFHH GTILMSTDMT RLGDYLNPDE KKLKAKGITS
VKSRVINLNT LIENIDHPMI CEAMINAYCH YFDTEVEIEH ISPDNAEYLP DFKEKFAKQS
SWEWNFGSTP AFEHALSERF SWGGVDIHLD VEKGQISRAQ LFTDMLDPTP IEALQSALVG
YNYEPQALSQ CIATVQAELP EHTDLLNDVK IWLNQQVS
//
