PAAS_ARATH
ID PAAS_ARATH Reviewed; 490 AA.
AC Q8RY79; F6L7A0; Q9SK68; Q9SMY2; Q9SMY3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phenylacetaldehyde synthase {ECO:0000305};
DE Short=AtPAAS {ECO:0000303|PubMed:23204519};
DE EC=4.1.1.109 {ECO:0000269|PubMed:21284755, ECO:0000269|PubMed:23204519};
DE AltName: Full=3,4-dihydroxyphenylacetaldehyde synthase {ECO:0000305};
DE Short=DHPAA synthase {ECO:0000305};
DE EC=4.1.1.107 {ECO:0000269|PubMed:21284755};
DE AltName: Full=Aromatic L-amino acid decarboxylase {ECO:0000303|PubMed:21284755};
DE AltName: Full=Aromatic aldehyde synthase {ECO:0000303|PubMed:21284755};
DE Short=AtAAS {ECO:0000303|PubMed:21284755};
GN Name=ELI5 {ECO:0000312|EMBL:CAB56038.1};
GN Synonyms=AADC {ECO:0000303|PubMed:21284755},
GN AAS {ECO:0000303|PubMed:21284755};
GN OrderedLocusNames=At2g20340 {ECO:0000312|Araport:AT2G20340};
GN ORFNames=F11A3.11 {ECO:0000312|EMBL:AAD21754.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
RC STRAIN=cv. Columbia;
RA Nass N., Koehler C., Scheel D.;
RT "Tyrosine decarboxylase (eli5) from Arabidopsis thaliana, cloning and
RT expression analysis.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21284755; DOI=10.1111/j.1365-313x.2011.04515.x;
RA Gutensohn M., Klempien A., Kaminaga Y., Nagegowda D.A., Negre-Zakharov F.,
RA Huh J.H., Luo H., Weizbauer R., Mengiste T., Tholl D., Dudareva N.;
RT "Role of aromatic aldehyde synthase in wounding/herbivory response and
RT flower scent production in different Arabidopsis ecotypes.";
RL Plant J. 66:591-602(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF PHE-338.
RX PubMed=23204519; DOI=10.1074/jbc.m112.401752;
RA Torrens-Spence M.P., Liu P., Ding H., Harich K., Gillaspy G., Li J.;
RT "Biochemical evaluation of the decarboxylation and decarboxylation-
RT deamination activities of plant aromatic amino acid decarboxylases.";
RL J. Biol. Chem. 288:2376-2387(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH L-PHENYLALANINE AND
RP PYRIDOXAL PHOSPHATE.
RA Torrens-Spence M.P., Chiang Y.-C., Smith T., Vicent M.A., Wang Y.,
RA Weng J.K.;
RT "Structural basis for independent origins of new catalytic machineries in
RT plant AAAD proteins.";
RL Submitted (AUG-2018) to the PDB data bank.
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the decarboxylation of L-
CC phenylalanine to 2-phenylethylamine, which is then oxidized to form 2-
CC phenylacetaldehyde, a constituent of floral scent (PubMed:21284755,
CC PubMed:23204519). 2-phenylacetaldehyde is a precursor of 2-
CC phenylethanol, another constituent of floral scent (PubMed:21284755).
CC Catalyzes both the decarboxylation and deamination of L-dopa to 3,4-
CC dihydroxylphenylacetaldehyde (DHPAA) (PubMed:21284755).
CC {ECO:0000269|PubMed:21284755, ECO:0000269|PubMed:23204519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + L-phenylalanine + O2 = 2-phenylacetaldehyde + CO2
CC + H2O2 + NH4(+); Xref=Rhea:RHEA:55532, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16424, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58095; EC=4.1.1.109;
CC Evidence={ECO:0000269|PubMed:21284755, ECO:0000269|PubMed:23204519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55533;
CC Evidence={ECO:0000269|PubMed:21284755};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + L-dopa + O2 = 3,4-dihydroxyphenylacetaldehyde +
CC CO2 + H2O2 + NH4(+); Xref=Rhea:RHEA:55524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57504; EC=4.1.1.107;
CC Evidence={ECO:0000269|PubMed:21284755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55525;
CC Evidence={ECO:0000269|PubMed:21284755};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:21284755};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 mM for L-phenylalanine {ECO:0000269|PubMed:21284755};
CC KM=5.1 mM for L-phenylalanine {ECO:0000269|PubMed:23204519};
CC KM=0.55 mM for L-dopa {ECO:0000269|PubMed:21284755};
CC Vmax=449.6 pmol/sec/mg enzyme with L-phenylalanine as substrate
CC {ECO:0000269|PubMed:21284755};
CC Vmax=112 nmol/min/mg enzyme with L-phenylalanine as substrate
CC {ECO:0000269|PubMed:23204519};
CC Vmax=956.3 pmol/sec/mg enzyme with L-dopa as substrate
CC {ECO:0000269|PubMed:21284755};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21284755}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, stems, cauline
CC leaves and flowers. {ECO:0000269|PubMed:21284755}.
CC -!- INDUCTION: Induced by wounding and methyl jasmonate in leaves.
CC {ECO:0000269|PubMed:21284755}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21754.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ011048; CAB56119.1; -; Genomic_DNA.
DR EMBL; AJ011049; CAB56038.1; -; mRNA.
DR EMBL; HQ843094; ADV41492.1; -; mRNA.
DR EMBL; AC006569; AAD21754.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06995.1; -; Genomic_DNA.
DR EMBL; AY074539; AAL69507.1; -; mRNA.
DR EMBL; AY096475; AAM20115.1; -; mRNA.
DR PIR; A84588; A84588.
DR RefSeq; NP_849999.1; NM_179668.2.
DR PDB; 6EEI; X-ray; 1.99 A; A/B=1-490.
DR PDBsum; 6EEI; -.
DR AlphaFoldDB; Q8RY79; -.
DR SMR; Q8RY79; -.
DR MINT; Q8RY79; -.
DR STRING; 3702.AT2G20340.1; -.
DR iPTMnet; Q8RY79; -.
DR PaxDb; Q8RY79; -.
DR PRIDE; Q8RY79; -.
DR ProteomicsDB; 228613; -.
DR EnsemblPlants; AT2G20340.1; AT2G20340.1; AT2G20340.
DR GeneID; 816553; -.
DR Gramene; AT2G20340.1; AT2G20340.1; AT2G20340.
DR KEGG; ath:AT2G20340; -.
DR Araport; AT2G20340; -.
DR TAIR; locus:2038937; AT2G20340.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_3_1_1; -.
DR InParanoid; Q8RY79; -.
DR OMA; NPGFNWS; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; Q8RY79; -.
DR BioCyc; ARA:AT2G20340-MON; -.
DR BRENDA; 4.1.1.25; 399.
DR SABIO-RK; Q8RY79; -.
DR PRO; PR:Q8RY79; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RY79; baseline and differential.
DR Genevisible; Q8RY79; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:1990055; F:phenylacetaldehyde synthase activity; IDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IDA:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Phenylacetaldehyde synthase"
FT /id="PRO_0000146993"
FT BINDING 92
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:6EEI"
FT BINDING 193
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:6EEI"
FT BINDING 308
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:6EEI"
FT BINDING 338
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:6EEI"
FT MOD_RES 309
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 338
FT /note="F->Y: Abolishes phenylacetaldehyde synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:23204519"
FT CONFLICT 273..274
FT /note="WF -> V (in Ref. 1; CAB56119/CAB56038)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="F -> G (in Ref. 1; CAB56119)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="E -> Q (in Ref. 1; CAB56119)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="A -> D (in Ref. 1; CAB56038)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="I -> V (in Ref. 1; CAB56038)"
FT /evidence="ECO:0000305"
FT HELIX 14..33
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:6EEI"
FT TURN 46..52
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 157..176
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:6EEI"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 365..400
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 412..419
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 432..443
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:6EEI"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:6EEI"
FT HELIX 470..488
FT /evidence="ECO:0007829|PDB:6EEI"
SQ SEQUENCE 490 AA; 54423 MW; 25F76B6AD037691E CRC64;
MENGSGKVLK PMDSEQLREY GHLMVDFIAD YYKTIEDFPV LSQVQPGYLH KLLPDSAPDH
PETLDQVLDD VRAKILPGVT HWQSPSFFAY YPSNSSVAGF LGEMLSAGLG IVGFSWVTSP
AATELEMIVL DWVAKLLNLP EQFMSKGNGG GVIQGSASEA VLVVLIAARD KVLRSVGKNA
LEKLVVYSSD QTHSALQKAC QIAGIHPENC RVLTTDSSTN YALRPESLQE AVSRDLEAGL
IPFFLCANVG TTSSTAVDPL AALGKIANSN GIWFHVDAAY AGSACICPEY RQYIDGVETA
DSFNMNAHKW FLTNFDCSLL WVKDQDSLTL ALSTNPEFLK NKASQANLVV DYKDWQIPLG
RRFRSLKLWM VLRLYGSETL KSYIRNHIKL AKEFEQLVSQ DPNFEIVTPR IFALVCFRLV
PVKDEEKKCN NRNRELLDAV NSSGKLFMSH TALSGKIVLR CAIGAPLTEE KHVKEAWKII
QEEASYLLHK
