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PKSI_BACSU
ID   PKSI_BACSU              Reviewed;         249 AA.
AC   P40802;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Putative polyketide biosynthesis enoyl-CoA isomerase PksI;
DE            EC=4.-.-.-;
GN   Name=pksI; OrderedLocusNames=BSU17170;
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 189.
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.
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. May have a role in the decarboxylation of the (S)-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; AAA85142.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13588.2; -; Genomic_DNA.
DR   PIR; G69678; G69678.
DR   RefSeq; NP_389597.2; NC_000964.3.
DR   RefSeq; WP_003231800.1; NZ_JNCM01000035.1.
DR   PDB; 4Q1G; X-ray; 2.10 A; A/B/C=1-249.
DR   PDB; 4Q1H; X-ray; 1.93 A; A/B/C=1-249.
DR   PDB; 4Q1I; X-ray; 2.10 A; A/B/C=1-249.
DR   PDB; 4Q1J; X-ray; 2.17 A; A/B/C=1-249.
DR   PDB; 4Q1K; X-ray; 1.75 A; A/B/C=1-249.
DR   PDBsum; 4Q1G; -.
DR   PDBsum; 4Q1H; -.
DR   PDBsum; 4Q1I; -.
DR   PDBsum; 4Q1J; -.
DR   PDBsum; 4Q1K; -.
DR   AlphaFoldDB; P40802; -.
DR   SMR; P40802; -.
DR   STRING; 224308.BSU17170; -.
DR   PaxDb; P40802; -.
DR   PRIDE; P40802; -.
DR   EnsemblBacteria; CAB13588; CAB13588; BSU_17170.
DR   GeneID; 940096; -.
DR   KEGG; bsu:BSU17170; -.
DR   PATRIC; fig|224308.179.peg.1862; -.
DR   eggNOG; COG1024; Bacteria.
DR   InParanoid; P40802; -.
DR   OMA; MHEKTFH; -.
DR   PhylomeDB; P40802; -.
DR   BioCyc; BSUB:BSU17170-MON; -.
DR   UniPathway; UPA01003; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 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..249
FT                   /note="Putative polyketide biosynthesis enoyl-CoA isomerase
FT                   PksI"
FT                   /id="PRO_0000109347"
FT   CONFLICT        189
FT                   /note="A -> E (in Ref. 1; AAA85142)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..12
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          15..20
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           23..25
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           31..46
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           68..75
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:4Q1H"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           108..114
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          116..122
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           131..134
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           142..150
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           152..161
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           167..173
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          176..180
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           182..196
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   HELIX           201..232
FT                   /evidence="ECO:0007829|PDB:4Q1K"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:4Q1G"
FT   HELIX           237..246
FT                   /evidence="ECO:0007829|PDB:4Q1K"
SQ   SEQUENCE   249 AA;  27896 MW;  FBBCDA0DCBD9C911 CRC64;
     MTHSVVELIE IESAIIQVKM QDRTHKNAFS QELTDDLIQA FEYIRQNPKY KAVILTGYDN
     YFASGGTQEG LLRIQQGLTK FTDDNLYSLA LDCEIPVIAA MQGHGIGGGF VMGLFADIVI
     LSRESVYTAN FMKYGFTPGM GATFIVPKKL GFSLAQEILL NAGSYRGADL EKRGVPFKVL
     PRAEVLDYAV ELAQELAEKP RNSLVTLKDH LVAPLRDQLP RVIEQELMMH EKTFHHEEVK
     SRIKGLYGN
 
 
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