GenomeNet

Database: UniProt
Entry: A0A4Z0D2L5_9FIRM
LinkDB: A0A4Z0D2L5_9FIRM
Original site: A0A4Z0D2L5_9FIRM 
ID   A0A4Z0D2L5_9FIRM        Unreviewed;       333 AA.
AC   A0A4Z0D2L5;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   18-JUN-2025, entry version 24.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=E4100_05705 {ECO:0000313|EMBL:TFZ40000.1};
OS   Soehngenia longivitae.
OC   Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
OC   Tissierellaceae; Soehngenia.
OX   NCBI_TaxID=2562294 {ECO:0000313|EMBL:TFZ40000.1, ECO:0000313|Proteomes:UP000298381};
RN   [1] {ECO:0000313|EMBL:TFZ40000.1, ECO:0000313|Proteomes:UP000298381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1933P {ECO:0000313|EMBL:TFZ40000.1,
RC   ECO:0000313|Proteomes:UP000298381};
RA   Grouzdev D.S., Bidzhieva S.K., Sokolova D.S., Tourova T.P., Poltaraus A.B.,
RA   Nazina T.N.;
RT   "Draft genome sequence data and analysis of a Fermenting Bacterium,
RT   Soehngenia longevitae strain 1933PT, isolated from petroleum reservoir in
RT   Azerbaijan.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[lipoyl-carrier protein] + (R)-lipoate + ATP = N(6)-
CC         [(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate +
CC         H(+); 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:ARBA00048037};
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}.
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:TFZ40000.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; SRIB01000007; TFZ40000.1; -; Genomic_DNA.
DR   RefSeq; WP_135271072.1; NZ_SRIB01000007.1.
DR   AlphaFoldDB; A0A4Z0D2L5; -.
DR   OrthoDB; 9788148at2; -.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000298381; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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:0017118; F:lipoyltransferase activity; IEA:TreeGrafter.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd16443; LplA; 1.
DR   FunFam; 3.30.930.10:FF:000072; Lipoate--protein ligase; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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; PF10437; Lip_prot_lig_C; 1.
DR   Pfam; PF21948; LplA-B_cat; 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:TFZ40000.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000298381}.
FT   DOMAIN          26..213
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   333 AA;  38734 MW;  6EA7E0AC164827AA CRC64;
     MKFVTNLSNN PYYNLAFEEY LFKNLPDDEE YVFLWINSPA IIVGKNQNTI EEINQQFVND
     KDIKVVRRVT GGGAVYHDFG NLNFSIIKNI EGKEKIDFSV INIPILKALE KFGINAELSG
     RNDLTVDGKK ISGIAQSLHK RKVLNHGTIL YDTDLSVLSQ ALNVKQDKIE SKGVKSVKSR
     VTNIRPYMKE DIDIIEFKEI LLKYIFEYLD QPLEEYKLSD EHLENIDKLC KTKYNTWEWN
     YGQSPDFNWK NYKRFPSGSI DVRLEIKSGI IDNIKIYGDF FGTKDVSELE ELLKNTKYEK
     NEILNKISKI DIVNYLGNIT QDDFLELLFS YEE
//
DBGET integrated database retrieval system