PPSA_ASPOR
ID PPSA_ASPOR Reviewed; 561 AA.
AC Q2UB01;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Acyl-CoA ligase ppsA {ECO:0000303|PubMed:32885554};
DE EC=6.2.1.13 {ECO:0000269|PubMed:32885554};
DE EC=6.2.1.17 {ECO:0000269|PubMed:32885554};
DE AltName: Full=2,4'-dihydroxy-3'-methoxypropiophenone biosynthesis cluster protein A {ECO:0000303|PubMed:32885554};
GN Name=ppsA {ECO:0000303|PubMed:32885554}; ORFNames=AO090102000165;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=32885554; DOI=10.1002/cbic.202000505;
RA Kan E., Tomita H., Katsuyama Y., Maruyama J.I., Koyama Y., Ohnishi Y.;
RT "Discovery of the 2,4'-dihydroxy-3'-methoxypropiophenone biosynthesis genes
RT in Aspergillus oryzae.";
RL ChemBioChem 22:203-211(2021).
CC -!- FUNCTION: Acyl-CoA ligase; part of the gene cluster that mediates the
CC biosynthesis of 2,4'-dihydroxy-3'-methoxypropiophenone
CC (PubMed:32885554). The first step of the pathway is the conversion of
CC acetate into acetyl-CoA by the acyl-CoA ligase ppsA (PubMed:32885554).
CC Acetyl-CoA is then used as a starter unit by the polyketide synthase
CC ppsB and condensed with 4 malonyl-CoA unit to produce the pentaketide
CC backbone (PubMed:32885554). During polyketide extension, the polykedite
CC chain is probably reduced and dehydrated by the KR and PT domains,
CC respectively (Probable). O-methylation seems to be catalyzed by an
CC unknown methyltransferase rather than by the CMeT domain of ppsB
CC (Probable). Two hydroxylations and one further decarboxylation step
CC catalyzed by yet unknown enzymes are then required to yield 4'-hydroxy-
CC 3'-methoxypropiophenone (Probable). PpsC functions as a carrier protein
CC to transport 4'-hydroxy-3'-methoxypropiophenone to a specific cell
CC compartment in which 4'-hydroxy-3'-methoxypropiophenone is hydroxylated
CC to 2,4'-dihydroxy-3'-methoxypropiophenone by a still to be identified
CC enzyme (PubMed:32885554). {ECO:0000269|PubMed:32885554,
CC ECO:0000305|PubMed:32885554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate;
CC Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456216; EC=6.2.1.13;
CC Evidence={ECO:0000269|PubMed:32885554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15082;
CC Evidence={ECO:0000269|PubMed:32885554};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456215; EC=6.2.1.17;
CC Evidence={ECO:0000269|PubMed:32885554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000269|PubMed:32885554};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:32885554}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of 2,4'-dihydroxy-3'-
CC methoxypropiophenone and 4'-hydroxy-3'-methoxypropiophenone.
CC {ECO:0000269|PubMed:32885554}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AP007162; BAE61264.1; -; Genomic_DNA.
DR RefSeq; XP_001822397.1; XM_001822345.2.
DR AlphaFoldDB; Q2UB01; -.
DR SMR; Q2UB01; -.
DR EnsemblFungi; BAE61264; BAE61264; AO090102000165.
DR GeneID; 5994442; -.
DR KEGG; aor:AO090102000165; -.
DR VEuPathDB; FungiDB:AO090102000165; -.
DR HOGENOM; CLU_000022_59_2_1; -.
DR OMA; ATNPFTH; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Ligase; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..561
FT /note="Acyl-CoA ligase ppsA"
FT /id="PRO_0000451833"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 462..540
FT /note="AMP-binding"
FT /evidence="ECO:0000255"
FT BINDING 203..214
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 561 AA; 61699 MW; A8EBDD59F7C15CE8 CRC64;
MNSNTPTDIV SFCFETQADH NATGPILIDG LTPTRSLTLH QFRQLVCQLI AGLHEQKIQQ
GQCILVHLEN SILYPALFLA IVGVGAVYMG AHPASSATEL EHLLSLANPS LIITGRDTLS
TVLQCTMSPS GGKKEKIPSD RVWVLNDIDQ VLCEAFSSTP DASMGDAAYH HRRDITKLLH
SGQRPWRTFD DDGQKSKITP AAMFATSGTS GLPKAAILSH HALIQQHISI HHPVPYPVTR
LLTLPLFHRY GALVALFFPT RYAQPLILLP GFQLRPFLSA IHVHGVTETY LSPAMVHILI
QSTPQSSSIR ESLRSLRYVC VGGAPIDSRP LQSLQDMLHP EACVAQAWGM TETATVFQDR
YCLPSRQFDK GSVGVVLPGY QVRLVDVSGS GRVLDNATEI PGELQVRGSG LFTSYKGHPD
HTDGDGWFST GDVMYQKNGH YFLVGRMKEM IKVRGYQVSP VELEAELAQH PLVKDAAVIG
VLATDGSSEL PRAYVVPLSW AERPSPEDIY DFMRQRLAGY KFLEGGVVFV DSIPRNSGGK
IRRTKLSELD DQRDKLIALL T
