ID   PPTAS_NOCIO             Reviewed;         222 AA.
AC   A1YCA5;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=4'-phosphopantetheinyl transferase Npt;
DE            Short=PPTase;
DE            EC=2.7.8.7;
GN   Name=npt;
OS   Nocardia iowensis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=204891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RC   STRAIN=DSM 45197 / JCM 18299 / NRRL 5646 / BM123;
RX   PubMed=17102130; DOI=10.1074/jbc.m607980200;
RA   Venkitasubramanian P., Daniels L., Rosazza J.P.;
RT   "Reduction of carboxylic acids by Nocardia aldehyde oxidoreductase requires
RT   a phosphopantetheinylated enzyme.";
RL   J. Biol. Chem. 282:478-485(2007).
CC   -!- FUNCTION: Catalyzes the transfer of the 4'-phosphopantetheine moiety
CC       from coenzyme A to a serine residue in the acyl-carrier domain of
CC       carboxylic acid reductase Car, thus converting apo-Car to fully active
CC       holo-Car. Is probably also responsible for the activation of other
CC       proteins with phosphopantetheine attachment sites.
CC       {ECO:0000269|PubMed:17102130}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC         [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC         Evidence={ECO:0000269|PubMed:17102130};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17102130}.
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; DQ904035; ABI83656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1YCA5; -.
DR   SMR; A1YCA5; -.
DR   GO; GO:0009366; C:enterobactin synthetase complex; IEA:InterPro.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.90.470.20; -; 1.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR041354; 4PPT_N.
DR   InterPro; IPR003542; Enbac_synth_compD-like.
DR   PANTHER; PTHR38096; PTHR38096; 1.
DR   Pfam; PF17837; 4PPT_N; 1.
DR   Pfam; PF01648; ACPS; 1.
DR   PRINTS; PR01399; ENTSNTHTASED.
DR   SUPFAM; SSF56214; SSF56214; 1.
PE   1: Evidence at protein level;
KW   Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..222
FT                   /note="4'-phosphopantetheinyl transferase Npt"
FT                   /id="PRO_0000425450"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  24287 MW;  38F90D197CAC340F CRC64;
     MIETILPAGV ESAELLEYPE DLKAHPAEEH LIAKSVEKRR RDFIGARHCA RLALAELGEP
     PVAIGKGERG APIWPRGVVG SLTHCDGYRA AAVAHKMRFR SIGIDAEPHA TLPEGVLDSV
     SLPPEREWLK TTDSALHLDR LLFCAKEATY KAWWPLTARW LGFEEAHITF EIEDGSADSG
     NGTFHSELLV PGQTNDGGTP LLSFDGRWLI ADGFILTAIA YA