ID   ADPPT_PONAB             Reviewed;         309 AA.
AC   Q5NVE1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE            EC=2.7.8.7 {ECO:0000250|UniProtKB:Q9NRN7};
DE   AltName: Full=4'-phosphopantetheinyl transferase;
DE   AltName: Full=Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE            Short=AASD-PPT;
GN   Name=AASDHPPT;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the post-translational modification of target
CC       proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine
CC       moiety from coenzyme A, regardless of whether the CoA is presented in
CC       the free thiol form or as an acetyl thioester, to a serine residue of a
CC       broad range of acceptors including the acyl carrier domain of FASN.
CC       {ECO:0000250|UniProtKB:Q9NRN7}.
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:0000250|UniProtKB:Q9NRN7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12069;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + apo-[ACP] = acetyl-[ACP] + adenosine 3',5'-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:46564, Rhea:RHEA-COMP:9621,
CC         Rhea:RHEA-COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:58343, ChEBI:CHEBI:78446;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46565;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC       Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:Q9NRN7};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NRN7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9NRN7}.
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC       {ECO:0000305}.
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DR   EMBL; CR926096; CAI29722.1; -; mRNA.
DR   RefSeq; NP_001127117.1; NM_001133645.1.
DR   AlphaFoldDB; Q5NVE1; -.
DR   SMR; Q5NVE1; -.
DR   STRING; 9601.ENSPPYP00000004386; -.
DR   GeneID; 100174162; -.
DR   KEGG; pon:100174162; -.
DR   CTD; 60496; -.
DR   eggNOG; KOG0945; Eukaryota.
DR   InParanoid; Q5NVE1; -.
DR   OrthoDB; 960416at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0051604; P:protein maturation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..309
FT                   /note="L-aminoadipate-semialdehyde dehydrogenase-
FT                   phosphopantetheinyl transferase"
FT                   /id="PRO_0000175738"
FT   BINDING         47
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT   BINDING         86..91
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT   BINDING         108..111
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT   BINDING         181..185
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRN7"
SQ   SEQUENCE   309 AA;  35728 MW;  0E1C6259FB810729 CRC64;
     MVFPAKRFCL VPSMEGVRWA FSCGTWLPSR AEWLLAVRSI QPEEKERIGQ FVFARDAKAA
     MAGRLMIRKL VAEKLNIPWN HIRLQRTAKG KPVLAKDSSN PYPNFNFNIS HQGDYAVLAA
     EPELQVGIDI MKTSFPGRGS IPEFFHIMKR KFTNKEWETI RGFKDEWTQL DMFYRNWALK
     ESFIKAIGVG LGFELQRLEF DLSPLNLDIG QVYKETRLFL DGEEEKEWAF EESKIDEHHF
     VAVALRKPDG SRHQDVPSQD DSKPTQRQFT ILNFNDLISS AVPMTPEDPS FWDCFCFTEE
     IPIRNGTKS