ID A0A0B7NP22_9FUNG Unreviewed; 574 AA.
AC A0A0B7NP22;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Putative lipoate-protein ligase A {ECO:0000256|ARBA:ARBA00015925};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN Name=PARPA_13459.1 scaffold 46870 {ECO:0000313|EMBL:CEP19147.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP19147.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP19147.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP19147.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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}.
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DR EMBL; LN734014; CEP19147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NP22; -.
DR STRING; 35722.A0A0B7NP22; -.
DR OrthoDB; 168805at2759; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000054107; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 254..440
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 574 AA; 65970 MW; 15C51123B1FDD777 CRC64;
MRVICLSPEK NTLLHLFMMD KSANKTKQVK KEQEALIPRN KWPFEEVLAD EYERQLETVD
VYTAHVEPKQ TNSILKLAQN KLPPLEGLEH CKKIRRISKP DTELGFELEV IMCLKEKIPQ
ETLEQRLKEH QFENCKISIV SVSRHAPLNR QQFEAWNHLW PLSYREDTRL DPKFTQQDID
IVHSHMQAIL ANERSTVICR IVDPSTNTIM AEKGDTRTEH PLHHAVMNID CYISTINDAY
TNLAIEEYLL RETKPDRYVL YLWRNKPCVV VGRNQNPFQE CNLRFMRENN IPLVRRRSGG
GAVYHDMGNS IYTIFMPREA FSRKTNAQLV ARSLNQLDIP ANVNERHDIV VDNHKVSGSA
YKITSSRAYH HGTMLIDAEI EMLKGCLSKK RMDNNGIVSK GVESVPSPVT NLRDYSFTVD
HQQFCESVLA EFVDAYNDGI PVKGPTQPII LNKQTDLPNK VKETRQELKT WDWIYGQTPE
FTNTFETDFD WGHVKSHIIS RHGKIIKADI STNNNLLHEP TIAAAISVAL EGLPYSDSSA
EEAIEKINTE VPGLINSEND HISKDISNWL QARL
//
