ADPPT_RAT
ID ADPPT_RAT Reviewed; 309 AA.
AC B2RYJ4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; CH474089; EDL85225.1; -; Genomic_DNA.
DR EMBL; BC166800; AAI66800.1; -; mRNA.
DR RefSeq; NP_001100268.2; NM_001106798.2.
DR AlphaFoldDB; B2RYJ4; -.
DR SMR; B2RYJ4; -.
DR STRING; 10116.ENSRNOP00000008062; -.
DR iPTMnet; B2RYJ4; -.
DR PhosphoSitePlus; B2RYJ4; -.
DR jPOST; B2RYJ4; -.
DR PaxDb; B2RYJ4; -.
DR PeptideAtlas; B2RYJ4; -.
DR PRIDE; B2RYJ4; -.
DR GeneID; 300328; -.
DR KEGG; rno:300328; -.
DR UCSC; RGD:1311360; rat.
DR CTD; 60496; -.
DR RGD; 1311360; Aasdhppt.
DR VEuPathDB; HostDB:ENSRNOG00000005795; -.
DR eggNOG; KOG0945; Eukaryota.
DR HOGENOM; CLU_057011_3_0_1; -.
DR InParanoid; B2RYJ4; -.
DR OMA; IPWSEIR; -.
DR OrthoDB; 960416at2759; -.
DR PhylomeDB; B2RYJ4; -.
DR TreeFam; TF313753; -.
DR Reactome; R-RNO-199220; Vitamin B5 (pantothenate) metabolism.
DR PRO; PR:B2RYJ4; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000005795; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; B2RYJ4; RN.
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:0009258; P:10-formyltetrahydrofolate catabolic process; ISO:RGD.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /id="PRO_0000379130"
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"
SQ SEQUENCE 309 AA; 35816 MW; 8E35E6BA4BB13620 CRC64;
MVFPAKRLCV VPYMEGVRWA FSCGTWLPSP AEWLLAVRSI QPEEKERIGQ FVFARDAKAA
LAGRLMIRKL VAEKLNIPWD HIRLQRTSKG KPILAKDTLN PYPNFNFNIS HQGDYTVLAA
EPELQVGIDI MKTSFPGRGS IPEFFHIMKR KFTNKEWETI RSFNDEWSQL DMFYRHWALK
ESFIKAIGVG LGFEMQRLEF DVSPLSMDIG QVYKETRLIL DGEEEKEWAF EESKIDQHHF
VAVALRKPDG SRHQNVSYQD DSKPSQRQFT ILNFNDLIAS AIPMTPEDPS FWDCFCFTEE
ILIRNGSKS
