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Alpha-pyrone synthesis polyketide synthase-like Pks18 (EC 2.3.1.-) (Alpha-pyrone synthesis polyketide synthase type III Pks18) (Chalcone synthase-like protein) (CHS-like)

 PKS18_MYCTU             Reviewed;         393 AA.
P9WPF1; L0T6G2; Q79FQ0; Q7D8I1;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
22-NOV-2017, entry version 21.
RecName: Full=Alpha-pyrone synthesis polyketide synthase-like Pks18;
EC=2.3.1.-;
AltName: Full=Alpha-pyrone synthesis polyketide synthase type III Pks18;
AltName: Full=Chalcone synthase-like protein;
Short=CHS-like;
Name=pks18; OrderedLocusNames=Rv1372;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION AS A POLYKETIDE SYNTHASE, STARTER UNIT SPECIFICITY,
MUTAGENESIS OF ALA-148; LYS-318 AND LEU-348, AND BIOPHYSICOCHEMICAL
PROPERTIES.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12941968; DOI=10.1074/jbc.M306714200;
Saxena P., Yadav G., Mohanty D., Gokhale R.S.;
"A new family of type III polyketide synthases in Mycobacterium
tuberculosis.";
J. Biol. Chem. 278:44780-44790(2003).
[3]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT PHE-205 IN COMPLEX
WITH SUBSTRATE, MUTAGENESIS OF THR-144; CYS-175; CYS-205 AND CYS-275,
STARTER UNIT SPECIFICITY, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15286723; DOI=10.1038/nsmb809;
Sankaranarayanan R., Saxena P., Marathe U.B., Gokhale R.S.,
Shanmugam V.M., Rukmini R.;
"A novel tunnel in mycobacterial type III polyketide synthase reveals
the structural basis for generating diverse metabolites.";
Nat. Struct. Mol. Biol. 11:894-900(2004).
-!- FUNCTION: Involved in the biosynthesis of tri- and tetraketide
alpha-pyrones. Pks18 catalyzes the extension of medium- and long-
chain aliphatic acyl-CoA substrates by using malonyl-CoA as an
extender molecule to synthesize polyketide products.
{ECO:0000269|PubMed:12941968}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4.2 uM for lauroyl-CoA (at 30 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:12941968};
KM=5.4 uM for palmitoyl-CoA (at 30 degrees Celsius and at pH
7.5) {ECO:0000269|PubMed:12941968};
KM=6.1 uM for arachidoyl-CoA (at 30 degrees Celsius and at pH
7.5) {ECO:0000269|PubMed:12941968};
KM=19.2 uM for hexanoyl-CoA (at 30 degrees Celsius and at pH
7.5) {ECO:0000269|PubMed:12941968};
KM=49.2 uM for acetyl-CoA (at 30 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:12941968};
KM=58.4 uM for malonyl-CoA (at 30 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:12941968};
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15286723}.
-!- SIMILARITY: Belongs to the chalcone/stilbene synthases family.
{ECO:0000305}.
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EMBL; AL123456; CCP44131.1; -; Genomic_DNA.
PIR; A70958; A70958.
RefSeq; WP_003407185.1; NZ_KK339370.1.
RefSeq; YP_177803.1; NC_000962.3.
PDB; 1TED; X-ray; 2.25 A; A/B/C/D=1-393.
PDB; 1TEE; X-ray; 2.90 A; A/B/C/D=1-393.
PDBsum; 1TED; -.
PDBsum; 1TEE; -.
ProteinModelPortal; P9WPF1; -.
SMR; P9WPF1; -.
STRING; 83332.Rv1372; -.
SwissLipids; SLP:000001035; -.
PaxDb; P9WPF1; -.
EnsemblBacteria; CCP44131; CCP44131; Rv1372.
GeneID; 886797; -.
KEGG; mtu:Rv1372; -.
TubercuList; Rv1372; -.
eggNOG; ENOG41065KQ; Bacteria.
eggNOG; COG3424; LUCA.
KO; K16233; -.
OMA; PIWGLGC; -.
PhylomeDB; P9WPF1; -.
UniPathway; UPA00094; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro.
GO; GO:0009715; P:chalcone biosynthetic process; IDA:MTBBASE.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR012328; Chalcone/stilbene_synth_C.
InterPro; IPR001099; Chalcone/stilbene_synthase_N.
InterPro; IPR011141; Polyketide_synthase_type-III.
InterPro; IPR016039; Thiolase-like.
PANTHER; PTHR11877; PTHR11877; 1.
Pfam; PF02797; Chal_sti_synt_C; 1.
Pfam; PF00195; Chal_sti_synt_N; 1.
PIRSF; PIRSF000451; PKS_III; 1.
SUPFAM; SSF53901; SSF53901; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Complete proteome;
Fatty acid metabolism; Lipid metabolism; Reference proteome;
Transferase.
CHAIN 1 393 Alpha-pyrone synthesis polyketide
synthase-like Pks18.
/FTId=PRO_0000407320.
ACT_SITE 175 175 Nucleophile.
BINDING 221 221 Substrate; via carbonyl oxygen.
{ECO:0000269|PubMed:15286723}.
SITE 205 205 Important for broad specificity for
aliphatic long-chain acyl-CoA starter
units.
SITE 209 209 Important for broad specificity for
aliphatic long-chain acyl-CoA starter
units.
MUTAGEN 144 144 T->F: Completely abolishes the polyketide
synthase activity with lauroyl-CoA and
palmitoyl-CoA.
{ECO:0000269|PubMed:15286723}.
MUTAGEN 148 148 A->F: Cannot be recovered in the soluble
form. {ECO:0000269|PubMed:12941968}.
MUTAGEN 148 148 A->M: Cannot be recovered in the soluble
form. {ECO:0000269|PubMed:12941968}.
MUTAGEN 148 148 A->T: Cannot be recovered in the soluble
form. {ECO:0000269|PubMed:12941968}.
MUTAGEN 175 175 C->A: Loss of polyketide synthase
activity. {ECO:0000269|PubMed:15286723}.
MUTAGEN 205 205 C->A: No significant change in polyketide
synthase activity.
{ECO:0000269|PubMed:15286723}.
MUTAGEN 205 205 C->F: Efficiently catalyzed the synthesis
of the triketide pyrone of the C6 starter
unit and shows weak polyketide synthase
activity with the C12 starter molecule.
{ECO:0000269|PubMed:15286723}.
MUTAGEN 209 209 A->F: Retained reasonable polyketide
synthase activity with lauroyl-CoA.
MUTAGEN 275 275 C->A: No significant change in polyketide
synthase activity.
{ECO:0000269|PubMed:15286723}.
MUTAGEN 318 318 K->A: Unable to synthesize any polyketide
products. {ECO:0000269|PubMed:12941968}.
MUTAGEN 348 348 L->S: Increase in the synthesis of the
tetraketide products.
{ECO:0000269|PubMed:12941968}.
STRAND 32 41 {ECO:0000244|PDB:1TED}.
STRAND 46 48 {ECO:0000244|PDB:1TED}.
HELIX 49 57 {ECO:0000244|PDB:1TED}.
HELIX 68 74 {ECO:0000244|PDB:1TED}.
STRAND 79 82 {ECO:0000244|PDB:1TED}.
HELIX 92 95 {ECO:0000244|PDB:1TED}.
STRAND 98 100 {ECO:0000244|PDB:1TEE}.
HELIX 102 125 {ECO:0000244|PDB:1TED}.
HELIX 132 134 {ECO:0000244|PDB:1TED}.
STRAND 135 144 {ECO:0000244|PDB:1TED}.
HELIX 151 159 {ECO:0000244|PDB:1TED}.
STRAND 166 172 {ECO:0000244|PDB:1TED}.
HELIX 174 176 {ECO:0000244|PDB:1TED}.
HELIX 177 191 {ECO:0000244|PDB:1TED}.
STRAND 196 204 {ECO:0000244|PDB:1TED}.
HELIX 206 208 {ECO:0000244|PDB:1TED}.
HELIX 215 223 {ECO:0000244|PDB:1TED}.
STRAND 226 236 {ECO:0000244|PDB:1TED}.
STRAND 247 256 {ECO:0000244|PDB:1TED}.
STRAND 263 269 {ECO:0000244|PDB:1TED}.
STRAND 272 277 {ECO:0000244|PDB:1TED}.
HELIX 281 299 {ECO:0000244|PDB:1TED}.
HELIX 304 306 {ECO:0000244|PDB:1TED}.
STRAND 310 312 {ECO:0000244|PDB:1TED}.
HELIX 317 327 {ECO:0000244|PDB:1TED}.
HELIX 331 334 {ECO:0000244|PDB:1TED}.
HELIX 335 344 {ECO:0000244|PDB:1TED}.
HELIX 350 361 {ECO:0000244|PDB:1TED}.
STRAND 364 378 {ECO:0000244|PDB:1TED}.
TURN 379 381 {ECO:0000244|PDB:1TED}.
STRAND 382 390 {ECO:0000244|PDB:1TED}.
SEQUENCE 393 AA; 42032 MW; 317D24C33B9CFD42 CRC64;
MNVSAESGAP RRAGQRHEVG LAQLPPAPPT TVAVIEGLAT GTPRRVVNQS DAADRVAELF
LDPGQRERIP RVYQKSRITT RRMAVDPLDA KFDVFRREPA TIRDRMHLFY EHAVPLAVDV
SKRALAGLPY RAAEIGLLVL ATSTGFIAPG VDVAIVKELG LSPSISRVVV NFMGCAAAMN
ALGTATNYVR AHPAMKALVV CIELCSVNAV FADDINDVVI HSLFGDGCAA LVIGASQVQE
KLEPGKVVVR SSFSQLLDNT EDGIVLGVNH NGITCELSEN LPGYIFSGVA PVVTEMLWDN
GLQISDIDLW AIHPGGPKII EQSVRSLGIS AELAAQSWDV LARFGNMLSV SLIFVLETMV
QQAESAKAIS TGVAFAFGPG VTVEGMLFDI IRR


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