ID A0A175VVF7_9PEZI Unreviewed; 425 AA.
AC A0A175VVF7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Putative lipoate-protein ligase A {ECO:0000256|ARBA:ARBA00015925};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=MMYC01_208337 {ECO:0000313|EMBL:KXX75149.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX75149.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX75149.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) 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|ARBA:ARBA00003253}.
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}.
CC -!- SIMILARITY: Belongs to the LplA family.
CC {ECO:0000256|ARBA:ARBA00008242}.
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:KXX75149.1}.
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DR EMBL; LCTW02000291; KXX75149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VVF7; -.
DR STRING; 100816.A0A175VVF7; -.
DR VEuPathDB; FungiDB:MMYC01_208337; -.
DR OrthoDB; 168805at2759; -.
DR UniPathway; UPA00537; UER00595.
DR Proteomes; UP000078237; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16443; LplA; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR PANTHER; PTHR12561; LIPOATE-PROTEIN LIGASE; 1.
DR PANTHER; PTHR12561:SF3; LIPOYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KXX75149.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237}.
FT DOMAIN 45..259
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 425 AA; 47163 MW; EBE3659FF81E9E52 CRC64;
MSWRNQMWAT SFTQSLLNSP VQIYRSTATD PYLNLSIEHH LLQRSHPDST ILFLYANRPC
VVIGRNQNPW LEVNLHLLQQ GLAQETPSSD ILSPEPSNVP ISLVRRRSGG GTVFHDAGNI
NWSVICPPPA FNRDKHAEMV VRALREQLGV RGVRVNGRHD IVMDVPASDP HSDGAVQTFK
VSGSAYKLTR TRSLHHGTCL LSSPNLGKVS GLLRSPAEGF IKARGVESVK SRIRNVGVGM
EDFMDVVVRE FVKMYGEGAG RGLVVGEEEA LGMEEVVHGV KELRSATWIF GQTPHFTFST
HPTKDDPRER PELPGSLPYG FQAQFTVRHG EIQSAAFSGL EYHDFVDEAS QDEALSQALV
KKRLYDITDW RRTLKSASPI QADTDEVGEW LNHMFGIQPQ KEKGGLVGPA TTNLITDALT
IPLFE
//
