PKSG_BACSU
ID PKSG_BACSU Reviewed; 420 AA.
AC P40830;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Polyketide biosynthesis 3-hydroxy-3-methylglutaryl-ACP synthase PksG;
DE Short=HMG synthase;
DE EC=2.3.3.-;
GN Name=pksG; OrderedLocusNames=BSU17150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / PB1424;
RX PubMed=7704258; DOI=10.1099/13500872-141-2-299;
RA Albertini A.M., Caramori T., Scoffone F., Scotti C., Galizzi A.;
RT "Sequence around the 159 degree region of the Bacillus subtilis genome: the
RT pksX locus spans 33.6 kb.";
RL Microbiology 141:299-309(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16757561; DOI=10.1073/pnas.0603148103;
RA Calderone C.T., Kowtoniuk W.E., Kelleher N.L., Walsh C.T., Dorrestein P.C.;
RT "Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-
RT S-carrier proteins in the pksX pathway of Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8977-8982(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT "A singular enzymatic megacomplex from Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN [6]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA Walsh C.T., Clardy J.;
RT "The identification of bacillaene, the product of the PksX megacomplex in
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. It catalyzes the aldol condensation between the acetyl
CC group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta-
CC ketothioester polyketide intermediate linked to one of the consecutive
CC thiolation domains of PksL. {ECO:0000269|PubMed:16757561,
CC ECO:0000269|PubMed:17234808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxobutanoyl-[ACP] + acetyl-[ACP] + H2O = (3S)-hydroxy-3-
CC methylglutaryl-[ACP] + H(+) + holo-[ACP]; Xref=Rhea:RHEA:52936,
CC Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685,
CC Rhea:RHEA-COMP:13408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78446, ChEBI:CHEBI:78450,
CC ChEBI:CHEBI:136897; Evidence={ECO:0000269|PubMed:16757561};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85140.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U11039; AAA85140.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB13586.2; -; Genomic_DNA.
DR PIR; E69678; E69678.
DR RefSeq; NP_389595.2; NC_000964.3.
DR RefSeq; WP_003231805.1; NZ_JNCM01000035.1.
DR PDB; 4YXQ; X-ray; 2.47 A; A/B/C/D=1-420.
DR PDB; 4YXT; X-ray; 2.10 A; A/B=1-420.
DR PDB; 4YXV; X-ray; 2.75 A; A/B=1-420.
DR PDBsum; 4YXQ; -.
DR PDBsum; 4YXT; -.
DR PDBsum; 4YXV; -.
DR AlphaFoldDB; P40830; -.
DR SMR; P40830; -.
DR STRING; 224308.BSU17150; -.
DR SwissLipids; SLP:000001711; -.
DR PaxDb; P40830; -.
DR PRIDE; P40830; -.
DR DNASU; 940121; -.
DR EnsemblBacteria; CAB13586; CAB13586; BSU_17150.
DR GeneID; 940121; -.
DR KEGG; bsu:BSU17150; -.
DR PATRIC; fig|224308.179.peg.1860; -.
DR eggNOG; COG3425; Bacteria.
DR InParanoid; P40830; -.
DR OMA; DDAYNWI; -.
DR PhylomeDB; P40830; -.
DR BioCyc; BSUB:BSU17150-MON; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR InterPro; IPR013528; HMG_CoA_synth_N.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08540; HMG_CoA_synt_C; 1.
DR Pfam; PF01154; HMG_CoA_synt_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Cytoplasm; Reference proteome;
KW Transferase.
FT CHAIN 1..420
FT /note="Polyketide biosynthesis 3-hydroxy-3-methylglutaryl-
FT ACP synthase PksG"
FT /id="PRO_0000213759"
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 114
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 250
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 182..195
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 213..234
FT /evidence="ECO:0007829|PDB:4YXT"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:4YXT"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 331..339
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:4YXT"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:4YXQ"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:4YXT"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:4YXT"
SQ SEQUENCE 420 AA; 46780 MW; 8808BDDFEEAC8F70 CRC64;
MVSAGIEAMN VFGGTAYLDV MELAKYRHLD TARFENLLMK EKAVALPYED PVTFGVNAAK
PIIDALSEAE KDRIELLITC SESGIDFGKS LSTYIHEYLG LNRNCRLFEV KQACYSGTAG
FQMAVNFILS QTSPGAKALV IASDISRFLI AEGGDALSED WSYAEPSAGA GAVAVLVGEN
PEVFQIDPGA NGYYGYEVMD TCRPIPDSEA GDSDLSLMSY LDCCEQTFLE YQKRVPGANY
QDTFQYLAYH TPFGGMVKGA HRTMMRKVAK VKTSGIETDF LTRVKPGLNY CQRVGNIMGA
ALFLALASTI DQGRFDTPKR IGCFSYGSGC CSEFYSGITT PQGQERQRTF GIEKHLDRRY
QLSMEEYELL FKGSGMVRFG TRNVKLDFEM IPGIMQSTQE KPRLFLEEIS EFHRKYRWIS
