ID   PPTA_PAXIN              Reviewed;         263 AA.
AC   A0A0S1RVB0;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=4'-phosphopantetheinyl transferase pptA;
DE            Short=PPTase;
DE            EC=2.7.8.7 {ECO:0000269|PubMed:26496685};
DE   AltName: Full=Phosphopantetheinyl transferase;
GN   Name=pptA;
OS   Paxillus involutus (Naked brimcap).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=71150;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC MYA-4647;
RX   PubMed=26496685; DOI=10.1016/j.chembiol.2015.08.016;
RA   Braesel J., Gotze S., Shah F., Heine D., Tauber J., Hertweck C., Tunlid A.,
RA   Stallforth P., Hoffmeister D.;
RT   "Three redundant synthetases secure redox-active pigment production in the
RT   basidiomycete Paxillus involutus.";
RL   Chem. Biol. 22:1325-1334(2015).
CC   -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC       a Ser of an acyl-carrier-protein. Activates the peptidyl carrier
CC       protein (PCP) domains of surfactin synthas.
CC       {ECO:0000269|PubMed:26496685}.
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:26496685};
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; KT935507; ALL98444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S1RVB0; -.
DR   SMR; A0A0S1RVB0; -.
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   Gene3D; 3.90.470.20; -; 2.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   Pfam; PF01648; ACPS; 1.
DR   SUPFAM; SSF56214; SSF56214; 2.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..263
FT                   /note="4'-phosphopantetheinyl transferase pptA"
FT                   /id="PRO_0000442636"
SQ   SEQUENCE   263 AA;  29595 MW;  AB77874C08F80EC5 CRC64;
     MQVWAIIYDK ADFPDTLYQN ALPFVDQAVQ SKIKRFHRRE DACRSLIGSL LPRVLLRKRG
     VSRDEMTFAT TENGKPYCTT PDIDPPLGFN VTHDESVIAM AFGSGDLGPP AYNLGVDVMQ
     LKVPPRITFS EFVDSVSSQE SDQLTARERN IVLADIPEGE ALRRFYWVWT LKEAYTKALG
     IGLGFDFRRI QYDVLEEKVT IDGELARGWQ FRKFEVAHSG NKYVGVAARF VGGRNPSITD
     LDEGSLVCYD AASFVNRAIE ELV