ADPPT_XENLA
ID ADPPT_XENLA Reviewed; 302 AA.
AC Q6DJH2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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. {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; BC075207; AAH75207.1; -; mRNA.
DR RefSeq; NP_001086383.1; NM_001092914.1.
DR AlphaFoldDB; Q6DJH2; -.
DR SMR; Q6DJH2; -.
DR DNASU; 444812; -.
DR GeneID; 444812; -.
DR KEGG; xla:444812; -.
DR CTD; 444812; -.
DR Xenbase; XB-GENE-985888; aasdhppt.S.
DR OrthoDB; 960416at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 444812; Expressed in testis and 20 other tissues.
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; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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 InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 2.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /id="PRO_0000175739"
FT BINDING 44
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 83..88
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 105..108
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 178..182
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
SQ SEQUENCE 302 AA; 35035 MW; F4A3700369FA5BBC CRC64;
MKLSALKRCV MGSVRWAFQC GSWCPSQAEW LLCARCVQPE EKQRIGHFMF TRDAKAAMAG
RLLMRKVIAD KLQIPWDRIL LERTGKGKPF LTGGSSSEYP CFNFNVSHQG DYAVLAAEPD
RQVGVDIMKT DLPGSSSIEE FFRLMNRQFT EKEWNSIRSM NNDWARLDMF YRHWALKESF
IKAIGVGLGF NLQRIEFEVS PVTMEIGKIY KETKMFLDDE EETWTFEEIL LDNQHHVAIA
LGEVDHLQHQ SPKIGDVAES TFTLLNFEDL MVSAIPMSDE DPDYWINFQS KQELPFRQRR
SR
