ID PKSH_BACSU Reviewed; 259 AA.
AC P40805;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Probable polyketide biosynthesis enoyl-CoA hydratase PksH;
DE EC=4.2.1.-;
GN Name=pksH; OrderedLocusNames=BSU17160;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; 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 FUNCTION.
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 [4]
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 [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 3-259.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of a putative polyketide biosynthesis enoyl-COA
RT hydratase (pksH) from Bacillus subtilis.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. Probably catalyzes the dehydration of the (S)-3-hydroxy-3-
CC methylglutaryl group attached to PksL. {ECO:0000269|PubMed:16757561,
CC ECO:0000269|PubMed:17234808}.
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; U11039; AAA85141.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13587.1; -; Genomic_DNA.
DR PIR; F69678; F69678.
DR RefSeq; NP_389596.1; NC_000964.3.
DR RefSeq; WP_010886512.1; NZ_JNCM01000035.1.
DR PDB; 3HP0; X-ray; 2.32 A; A/B/C/D/E/F=3-259.
DR PDBsum; 3HP0; -.
DR AlphaFoldDB; P40805; -.
DR SMR; P40805; -.
DR STRING; 224308.BSU17160; -.
DR PaxDb; 224308-BSU17160; -.
DR EnsemblBacteria; CAB13587; CAB13587; BSU_17160.
DR GeneID; 940033; -.
DR KEGG; bsu:BSU17160; -.
DR PATRIC; fig|224308.43.peg.1812; -.
DR eggNOG; COG1024; Bacteria.
DR InParanoid; P40805; -.
DR OrthoDB; 9775794at2; -.
DR PhylomeDB; P40805; -.
DR BioCyc; BSUB:BSU17160-MONOMER; -.
DR UniPathway; UPA01003; -.
DR EvolutionaryTrace; P40805; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06558; crotonase-like; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR PANTHER; PTHR42964; ENOYL-COA HYDRATASE; 1.
DR PANTHER; PTHR42964:SF1; POLYKETIDE BIOSYNTHESIS ENOYL-COA HYDRATASE PKSH-RELATED; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..259
FT /note="Probable polyketide biosynthesis enoyl-CoA hydratase
FT PksH"
FT /id="PRO_0000109346"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:3HP0"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:3HP0"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:3HP0"
FT TURN 75..79
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:3HP0"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:3HP0"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:3HP0"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:3HP0"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3HP0"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:3HP0"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:3HP0"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:3HP0"
SQ SEQUENCE 259 AA; 29411 MW; 441F76B77234DA9D CRC64;
MDLVTYQTIK VRFQASVCYI TFHRPEANNT INDTLIEECL QVLNQCETST VTVVVLEGLP
EVFCFGADFQ EIYQEMKRGR KQASSQEPLY DLWMKLQTGP YVTISHVRGK VNAGGLGFVS
ATDIAIADQT ASFSLSELLF GLYPACVLPF LIRRIGRQKA HYMTLMTKPI SVQEASEWGL
IDAFDAESDV LLRKHLLRLR RLNKKGIAHY KQFMSSLDHQ VSRAKATALT ANQDMFSDPQ
NQMGIIRYVE TGQFPWEDQ
//
