ID   G3J853_CORMM            Unreviewed;       367 AA.
AC   G3J853;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Putative lipoate-protein ligase A {ECO:0000256|ARBA:ARBA00015925};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=CCM_02165 {ECO:0000313|EMBL:EGX93895.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX93895.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX93895.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX93895.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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}.
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DR   EMBL; JH126400; EGX93895.1; -; Genomic_DNA.
DR   RefSeq; XP_006667381.1; XM_006667318.1.
DR   AlphaFoldDB; G3J853; -.
DR   STRING; 983644.G3J853; -.
DR   GeneID; 18164193; -.
DR   KEGG; cmt:CCM_02165; -.
DR   VEuPathDB; FungiDB:CCM_02165; -.
DR   eggNOG; KOG3159; Eukaryota.
DR   HOGENOM; CLU_022986_3_0_1; -.
DR   InParanoid; G3J853; -.
DR   OMA; TTFTRNK; -.
DR   OrthoDB; 168805at2759; -.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000001610; 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   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:EGX93895.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT   DOMAIN          53..238
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   367 AA;  40442 MW;  515798941454CE89 CRC64;
     MACRPRLLCQ LSRRLFSTAA AADPSHKTQI YLSRSADPLL NLSVEHHLLR TVPADATVLM
     LYANAPCVVV GRNQNPWIET DLARLAGGGV QLVRRRSGGG TVFHDPGNVN FSVIGPSAAF
     DRDRHADMVV RALRRLGRPT ARVNARHDIV VDEPGATFKV SGSAYKLTRL RSLHHGTCLL
     RSPHLDAISG LLRAPAAPFV RARGVESVRS PVRNLDLDAD AFRDAVVREF EAMYGPPDVR
     AVVEDGPARA VDPVRRGYAE MASREWLYGQ TPRFTLSTHP TEQDPRPRPK LPFEERVYIE
     AKQGVIERFQ VENGNGARRD LSSLVGVTMY NINDWSAQLA DAGIASHQAQ PIGNWLNSIL
     GTAFTRQ
//