ID A0A0M8MML1_9BASI Unreviewed; 382 AA.
AC A0A0M8MML1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=Malapachy_2606 {ECO:0000313|EMBL:KOS15536.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15536.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS15536.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15536.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) 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:KOS15536.1}.
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DR EMBL; LGAV01000002; KOS15536.1; -; Genomic_DNA.
DR RefSeq; XP_017993168.1; XM_018137094.1.
DR AlphaFoldDB; A0A0M8MML1; -.
DR STRING; 77020.A0A0M8MML1; -.
DR GeneID; 28728969; -.
DR VEuPathDB; FungiDB:Malapachy_2606; -.
DR OrthoDB; 168805at2759; -.
DR UniPathway; UPA00537; UER00595.
DR Proteomes; UP000037751; 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 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; 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 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:KOS15536.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT DOMAIN 52..258
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 382 AA; 42895 MW; AF6E7011F88F6995 CRC64;
MALALRRRGR SVRYLLARGY ASASTNPVVY ISRTRNPYFN LAWEDFLFRT LPENEPACFL
YVNDPCVVVG RNQNLWSEVD PQAMREENVS VIRRQSGGGT VYHDPGNLNF SFHTSKASFA
RRIHTELIAE AFKSKPVSLP SKHGIDPVFL TDRNDLAVLD VQATEAEEKW FRKVSGSAYK
LANHRAYHHG TLLLDANLRR MSMLKQRRSH MTTNAVSSVP SPVTNLTMAF PDQAARLACE
CVMEAIYAAF CRKYGPSNKV WVDERMLDHT AQIKSRTYHV RENYESLQSW DWLYGSNPAF
SVTASTEHVP FDQASLTVTL HCTHGRVDRV DVETPSPTLA QAVQQLKGAP YDALAWAPPS
SVPPSTAPAV EARLAAWLKK AL
//
