OKS_ALOAR
ID OKS_ALOAR Reviewed; 403 AA.
AC Q3L7F5;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Octaketide synthase 1;
DE Short=OKS;
DE EC=2.3.1.-;
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 GLY-207.
RX PubMed=16144421; DOI=10.1021/ja053945v;
RA Abe I., Oguro S., Utsumi Y., Sano Y., Noguchi H.;
RT "Engineered biosynthesis of plant polyketides: chain length control in an
RT octaketide-producing plant type III polyketide synthase.";
RL J. Am. Chem. Soc. 127:12709-12716(2005).
CC -!- FUNCTION: Catalyzes the iterative condensations of 8 molecules of
CC malonyl-CoA to produce aromatic octaketides, SEK4 and SEK4b, the
CC products of the minimal polyketide synthase for the
CC benzoisochromanequinone actinorhodin. May be involved in the
CC biosynthesis of the octaketide barbaloin.
CC {ECO:0000269|PubMed:16144421}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=95.0 uM for malonyl-CoA {ECO:0000269|PubMed:16144421};
CC Note=kcat is 0.094 min(-1).;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:16144421};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:16144421}.
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; AY567707; AAT48709.1; -; mRNA.
DR PDB; 7DTQ; X-ray; 1.75 A; A/B/C/D=1-403.
DR PDBsum; 7DTQ; -.
DR AlphaFoldDB; Q3L7F5; -.
DR SMR; Q3L7F5; -.
DR BioCyc; MetaCyc:MON-15013; -.
DR BRENDA; 2.3.1.B25; 263.
DR UniPathway; UPA00154; -.
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; Transferase.
FT CHAIN 1..403
FT /note="Octaketide synthase 1"
FT /id="PRO_0000422575"
FT ACT_SITE 174
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 318..321
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT SITE 207
FT /note="Determines the polyketide chain length and product
FT specificity"
FT MUTAGEN 207
FT /note="G->A: Turns into a heptaketide synthase."
FT /evidence="ECO:0000269|PubMed:16144421"
FT MUTAGEN 207
FT /note="G->L,F: Turns into a pentaketide synthase that
FT mediates production of the pentaketide 2,7-dihydroxy-5-
FT methylchromone."
FT /evidence="ECO:0000269|PubMed:16144421"
FT MUTAGEN 207
FT /note="G->M: Turns into an unnatural pentaketide synthase."
FT /evidence="ECO:0000269|PubMed:16144421"
FT MUTAGEN 207
FT /note="G->T: Turns into a hexaketide synthase."
FT /evidence="ECO:0000269|PubMed:16144421"
FT MUTAGEN 207
FT /note="G->W: Turns into an tetraketide synthase."
FT /evidence="ECO:0000269|PubMed:16144421"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 101..127
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:7DTQ"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 281..298
FT /evidence="ECO:0007829|PDB:7DTQ"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:7DTQ"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:7DTQ"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:7DTQ"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:7DTQ"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:7DTQ"
SQ SEQUENCE 403 AA; 44570 MW; 3F6A40BA792FDA0B CRC64;
MSSLSNASHL MEDVQGIRKA QRADGTATVM AIGTAHPPHI FPQDTYADFY FRATNSEHKV
ELKKKFDRIC KKTMIGKRYF NYDEEFLKKY PNITSFDEPS LNDRQDICVP GVPALGAEAA
VKAIAEWGRP KSEITHLVFC TSCGVDMPSA DFQCAKLLGL RTNVNKYCVY MQGCYAGGTV
MRYAKDLAEN NRGARVLVVC AELTIIGLRG PNESHLDNAI GNSLFGDGAA ALIVGSDPII
GVEKPMFEIV CAKQTVIPNS EDVIHLHMRE AGLMFYMSKD SPETISNNVE ACLVDVFKSV
GMTPPEDWNS LFWIPHPGGR AILDQVEAKL KLRPEKFRAT RTVLWDCGNM VSACVLYILD
EMRRKSADEG LETYGEGLEW GVLLGFGPGM TVETILLHSL PLM
