PCS_ALOAR
ID PCS_ALOAR Reviewed; 403 AA.
AC Q58VP7;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=5,7-dihydroxy-2-methylchromone synthase;
DE EC=2.3.1.216;
DE AltName: Full=Pentaketide chromone synthase;
DE Short=PCS;
OS Aloe arborescens (Kidachi aloe).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asphodelaceae;
OC Asphodeloideae; Aloe.
OX NCBI_TaxID=45385;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF MET-207.
RX PubMed=15686354; DOI=10.1021/ja0431206;
RA Abe I., Utsumi Y., Oguro S., Morita H., Sano Y., Noguchi H.;
RT "A plant type III polyketide synthase that produces pentaketide chromone.";
RL J. Am. Chem. Soc. 127:1362-1363(2005).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=16946474; DOI=10.1107/s174430910602968x;
RA Morita H., Kondo S., Abe T., Noguchi H., Sugio S., Abe I., Kohno T.;
RT "Crystallization and preliminary crystallographic analysis of a novel plant
RT type III polyketide synthase that produces pentaketide chromone.";
RL Acta Crystallogr. F 62:899-901(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH COENZYME A, SUBUNIT,
RP AND OXIDATION AT CYS-174.
RX PubMed=17462571; DOI=10.1016/j.chembiol.2007.02.003;
RA Morita H., Kondo S., Oguro S., Noguchi H., Sugio S., Abe I., Kohno T.;
RT "Structural insight into chain-length control and product specificity of
RT pentaketide chromone synthase from Aloe arborescens.";
RL Chem. Biol. 14:359-369(2007).
CC -!- FUNCTION: Catalyzes the iterative condensations of 5 molecules of
CC malonyl-CoA to produce a pentaketide 5,7-dihydroxy-2-methylchromone.
CC {ECO:0000269|PubMed:15686354}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H(+) + 5 malonyl-CoA = 5,7-dihydroxy-2-methyl-4H-chromen-4-
CC one + 5 CO2 + 5 CoA + H2O; Xref=Rhea:RHEA:34839, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:77977; EC=2.3.1.216;
CC Evidence={ECO:0000269|PubMed:15686354};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=71 uM for malonyl-CoA {ECO:0000269|PubMed:15686354};
CC Note=kcat is 0.445 min(-1).;
CC pH dependence:
CC Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:15686354};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15686354,
CC ECO:0000269|PubMed:17462571}.
CC -!- MISCELLANEOUS: A.arborescens is a medicinal plant rich in aromatic
CC polyketides, such as pharmaceutically important aloenin (hexaketide),
CC aloesin (heptaketide) and barbaloin (octaketide).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AY823626; AAX35541.1; -; mRNA.
DR PDB; 2D3M; X-ray; 1.60 A; A/B=1-403.
DR PDB; 2D51; X-ray; 1.60 A; A/B=1-403.
DR PDB; 2D52; X-ray; 1.60 A; A/B=1-403.
DR PDBsum; 2D3M; -.
DR PDBsum; 2D51; -.
DR PDBsum; 2D52; -.
DR AlphaFoldDB; Q58VP7; -.
DR SMR; Q58VP7; -.
DR KEGG; ag:AAX35541; -.
DR UniPathway; UPA00154; -.
DR EvolutionaryTrace; Q58VP7; -.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR InterPro; IPR011141; Polyketide_synthase_type-III.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11877; PTHR11877; 1.
DR Pfam; PF02797; Chal_sti_synt_C; 1.
DR Pfam; PF00195; Chal_sti_synt_N; 1.
DR PIRSF; PIRSF000451; PKS_III; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Flavonoid biosynthesis; Oxidation;
KW Transferase.
FT CHAIN 1..403
FT /note="5,7-dihydroxy-2-methylchromone synthase"
FT /id="PRO_0000422574"
FT ACT_SITE 174
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17462571"
FT BINDING 277
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17462571"
FT BINDING 281
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17462571"
FT BINDING 318..321
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT SITE 207
FT /note="Determines the polyketide chain length and product
FT specificity"
FT MOD_RES 174
FT /note="Cysteine sulfinic acid (-SO2H)"
FT /evidence="ECO:0000269|PubMed:17462571"
FT MUTAGEN 207
FT /note="M->G: Turns into a an octaketide synthase that
FT efficiently produces aromatic octaketides, SEK4 and SEK4b,
FT the products of the minimal polyketide synthase for the
FT benzoisochromanequinone actinorhodin."
FT /evidence="ECO:0000269|PubMed:15686354"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:2D3M"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 101..127
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:2D3M"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 281..298
FT /evidence="ECO:0007829|PDB:2D3M"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:2D3M"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2D3M"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:2D3M"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:2D3M"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:2D3M"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:2D3M"
SQ SEQUENCE 403 AA; 44571 MW; 6BA8ADBDE5BE09B1 CRC64;
MSSLSNSLPL MEDVQGIRKA QKADGTATVM AIGTAHPPHI FPQDTYADVY FRATNSEHKV
ELKKKFDHIC KKTMIGKRYF NYDEEFLKKY PNITSYDEPS LNDRQDICVP GVPALGTEAA
VKAIEEWGRP KSEITHLVFC TSCGVDMPSA DFQCAKLLGL HANVNKYCIY MQGCYAGGTV
MRYAKDLAEN NRGARVLVVC AELTIMMLRA PNETHLDNAI GISLFGDGAA ALIIGSDPII
GVEKPMFEIV CTKQTVIPNT EDVIHLHLRE TGMMFYLSKG SPMTISNNVE ACLIDVFKSV
GITPPEDWNS LFWIPHPGGR AILDQVEAKL KLRPEKFRAA RTVLWDYGNM VSASVGYILD
EMRRKSAAKG LETYGEGLEW GVLLGFGPGI TVETILLHSL PLM
