RPPA_STRCO
ID RPPA_STRCO Reviewed; 374 AA.
AC Q9FCA7;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=1,3,6,8-tetrahydroxynaphthalene synthase {ECO:0000303|PubMed:12905073};
DE Short=THNS {ECO:0000303|PubMed:12905073};
DE EC=2.3.1.233 {ECO:0000269|PubMed:12905073, ECO:0000269|PubMed:15265863};
DE AltName: Full=1,3,6,8-tetrahydroxynaphthalene synthesis polyketide synthase type III {ECO:0000305};
GN OrderedLocusNames=SCO1206;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12905073; DOI=10.1007/s10295-003-0075-8;
RA Izumikawa M., Shipley P.R., Hopke J.N., O'Hare T., Xiang L., Noel J.P.,
RA Moore B.S.;
RT "Expression and characterization of the type III polyketide synthase
RT 1,3,6,8-tetrahydroxynaphthalene synthase from Streptomyces coelicolor
RT A3(2).";
RL J. Ind. Microbiol. Biotechnol. 30:510-515(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF CYS-106; CYS-168; CYS-171 AND CYS-184, AND SUBUNIT.
RX PubMed=15265863; DOI=10.1074/jbc.m406567200;
RA Austin M.B., Izumikawa M., Bowman M.E., Udwary D.W., Ferrer J.L.,
RA Moore B.S., Noel J.P.;
RT "Crystal structure of a bacterial type III polyketide synthase and
RT enzymatic control of reactive polyketide intermediates.";
RL J. Biol. Chem. 279:45162-45174(2004).
CC -!- FUNCTION: Involved in the biosynthesis of melanin but also various
CC secondary metabolites containing a naphthoquinone ring. Catalyzes the
CC iterative condensation of five CoA-linked malonyl units to form a
CC pentaketide intermediate. THNS subsequently catalyzes the dual
CC intramolecular Claisen and aldol condensations of this linear
CC intermediate to produce the fused ring of 1,3,6,8-
CC tetrahydroxynaphthalene (THN). {ECO:0000269|PubMed:12905073,
CC ECO:0000269|PubMed:15265863}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5 H(+) + 5 malonyl-CoA = 5 CO2 + 5 CoA + H2O + naphthalene-
CC 1,3,6,8-tetrol; Xref=Rhea:RHEA:41524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:18365,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384; EC=2.3.1.233;
CC Evidence={ECO:0000269|PubMed:12905073, ECO:0000269|PubMed:15265863};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.58 uM for 5 malonyl-CoA {ECO:0000269|PubMed:12905073};
CC Note=kcat is 0.48 min(-1) for THN synthase activity with THN as
CC substrate. {ECO:0000269|PubMed:12905073};
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000250|UniProtKB:Q54240}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15265863}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AL939108; CAC01488.1; -; Genomic_DNA.
DR RefSeq; NP_625495.1; NC_003888.3.
DR RefSeq; WP_011027653.1; NZ_VNID01000006.1.
DR PDB; 1U0M; X-ray; 2.22 A; A/B=1-374.
DR PDBsum; 1U0M; -.
DR AlphaFoldDB; Q9FCA7; -.
DR SMR; Q9FCA7; -.
DR STRING; 100226.SCO1206; -.
DR GeneID; 1096629; -.
DR KEGG; sco:SCO1206; -.
DR PATRIC; fig|100226.15.peg.1205; -.
DR eggNOG; COG3424; Bacteria.
DR HOGENOM; CLU_034992_0_0_11; -.
DR InParanoid; Q9FCA7; -.
DR OMA; TAWLINE; -.
DR PhylomeDB; Q9FCA7; -.
DR BioCyc; MetaCyc:MON-14457; -.
DR BRENDA; 2.3.1.233; 5998.
DR UniPathway; UPA00785; -.
DR EvolutionaryTrace; Q9FCA7; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0042438; P:melanin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030639; P:polyketide biosynthetic process; IBA:GO_Central.
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; Melanin biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..374
FT /note="1,3,6,8-tetrahydroxynaphthalene synthase"
FT /id="PRO_0000430880"
FT ACT_SITE 138
FT /evidence="ECO:0000250|UniProtKB:Q54240"
FT MUTAGEN 106
FT /note="C->S: Still able to produce THN."
FT /evidence="ECO:0000269|PubMed:15265863"
FT MUTAGEN 168
FT /note="C->S: Still able to produce THN."
FT /evidence="ECO:0000269|PubMed:15265863"
FT MUTAGEN 171
FT /note="C->S: Still able to produce THN."
FT /evidence="ECO:0000269|PubMed:15265863"
FT MUTAGEN 184
FT /note="C->S: Still able to produce THN."
FT /evidence="ECO:0000269|PubMed:15265863"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 65..91
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:1U0M"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 203..214
FT /evidence="ECO:0007829|PDB:1U0M"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:1U0M"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:1U0M"
FT HELIX 307..318
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:1U0M"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1U0M"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:1U0M"
SQ SEQUENCE 374 AA; 40934 MW; 8907CCDC30B1AFC9 CRC64;
MATLCRPSVS VPEHVITMEE TLELARRRHT DHPQLPLALR LIENTGVRTR HIVQPIEDTL
EHPGFEDRNK VYEREAKSRV PAVIQRALDD AELLATDIDV IIYVSCTGFM MPSLTAWLIN
EMGFDSTTRQ IPIAQLGCAA GGAAINRAHD FCTAYPEANA LIVACEFCSL CYQPTDLGVG
SLLCNGLFGD GIAAAVVRGR GGTGVRLERN GSYLIPKTED WIMYDVKATG FHFLLDKRVP
ATMEPLAPAL KELAGEHGWD ASDLDFYIVH AGGPRILDDL STFLEVDPHA FRFSRATLTE
YGNIASAVVL DALRRLFDEG GVEEGARGLL AGFGPGITAE MSLGCWQTAD VRRGIRQDVT
RTAARGVSRR VRQA
