HPAAS_RHORB
ID HPAAS_RHORB Reviewed; 490 AA.
AC A0A2I6B3P0;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=4-hydroxyphenylacetaldehyde synthase {ECO:0000303|PubMed:29277428};
DE Short=HPAA synthase {ECO:0000303|PubMed:29277428};
DE Short=RrHPAAS {ECO:0000303|PubMed:29277428};
DE EC=4.1.1.108 {ECO:0000269|PubMed:29277428};
OS Rhodiola rosea (Roseroot) (Sedum rhodiola).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Saxifragales; Crassulaceae; Rhodiola.
OX NCBI_TaxID=203015;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29277428; DOI=10.1016/j.molp.2017.12.007;
RA Torrens-Spence M.P., Pluskal T., Li F.S., Carballo V., Weng J.K.;
RT "Complete pathway elucidation and heterologous reconstitution of Rhodiola
RT salidroside biosynthesis.";
RL Mol. Plant 11:205-217(2018).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH 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: Catalyzes the production of 4-hydroxyphenylacetaldehyde
CC (HPAA) directly from L-tyrosine, tyramine not being formed as an
CC intermediate. {ECO:0000269|PubMed:29277428}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + L-tyrosine + O2 = (4-hydroxyphenyl)acetaldehyde +
CC CO2 + H2O2 + NH4(+); Xref=Rhea:RHEA:55528, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15621,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58315; EC=4.1.1.108;
CC Evidence={ECO:0000269|PubMed:29277428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55529;
CC Evidence={ECO:0000269|PubMed:29277428};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.42 mM for L-tyrosine {ECO:0000269|PubMed:29277428};
CC Note=kcat is 4.91 sec(-1) with L-tyrosine as substrate.
CC {ECO:0000269|PubMed:29277428};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; MF674522; AUI41111.1; -; mRNA.
DR PDB; 6EEQ; X-ray; 2.60 A; A=1-490.
DR PDBsum; 6EEQ; -.
DR AlphaFoldDB; A0A2I6B3P0; -.
DR SMR; A0A2I6B3P0; -.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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 Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..490
FT /note="4-hydroxyphenylacetaldehyde synthase"
FT /id="PRO_0000450478"
FT BINDING 97
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT BINDING 198
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT BINDING 313
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT BINDING 343
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT MOD_RES 314
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.2"
FT HELIX 19..39
FT /evidence="ECO:0007829|PDB:6EEQ"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:6EEQ"
FT TURN 51..57
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 125..141
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 365..400
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 430..444
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:6EEQ"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:6EEQ"
FT HELIX 471..486
FT /evidence="ECO:0007829|PDB:6EEQ"
SQ SEQUENCE 490 AA; 54374 MW; DAE950FEA59578D4 CRC64;
MGSLPSPNDP SNTFNPMDLT ELSTESKLVV DFITQYYQTL ETRPVQPRVK PGFLTGQLPD
KAPFHGESME VILSDVNEKI VPGLTHWQSP NFHAYFPASS SNAGLLGELL CSGLSVIGFT
WSSSPAATEL ENVVVDWMAK MLNLPSSFCF SGGGGGVLQA NTCEAVLCTL AAARDKALNR
VGDDQINKLV LYCSDQTHFT IHKGAKLIGI RSKNIKSITT KKENEFKLCP NDLRDAIRSD
LEAGLVPFYV CGTIGTTALG VVDPIKELGK VAREFDLWLH VDGAYGGSAC ICPEFQHYLD
GVDLVDSISM NAHKWLLSNL DCCFLWLQSP NALIESLAAE ANFLKGGSEM VDYKDWQISL
SRRFRAIKMW MVIRRYGVSN LIEHIRSDVS MAVRFEEMVA ADDRFEIVFP RKFALVCFKL
SSEKTPPGRD SELTRELMER VNSSGKAYLS GVQMGRIFFI RCVIGSSLTE ERHVDNLWRL
IQETAQSIVS
