ID   RAPK_STRRN              Reviewed;         334 AA.
AC   Q54305; A0A0A0NW69;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Chorismatase {ECO:0000303|PubMed:21383123};
DE            EC=3.3.2.13 {ECO:0000250|UniProtKB:Q9KID9};
GN   Name=rapK; ORFNames=M271_40655 {ECO:0000312|EMBL:AGP59510.1};
OS   Streptomyces rapamycinicus (strain ATCC 29253 / DSM 41530 / NRRL 5491 /
OS   AYB-994) (Streptomyces hygroscopicus (strain ATCC 29253)).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1343740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29253 / DSM 41530 / NRRL 5491 / AYB-994;
RX   PubMed=7644502; DOI=10.1073/pnas.92.17.7839;
RA   Schwecke T., Aparicio J.F., Molnar I., Koenig A., Khaw L.E., Haydock S.F.,
RA   Oliynyk M., Caffrey P., Cortes J., Lester J.B., Boehm G.A., Staunton J.,
RA   Leadlay P.F.;
RT   "The biosynthetic gene cluster for the polyketide immunosuppressant
RT   rapamycin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7839-7843(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29253 / DSM 41530 / NRRL 5491 / AYB-994;
RX   PubMed=23929477; DOI=10.1128/genomea.00581-13;
RA   Baranasic D., Gacesa R., Starcevic A., Zucko J., Blazic M., Horvat M.,
RA   Gjuracic K., Fujs S., Hranueli D., Kosec G., Cullum J., Petkovic H.;
RT   "Draft genome sequence of Streptomyces rapamycinicus strain NRRL 5491, the
RT   producer of the immunosuppressant rapamycin.";
RL   Genome Announc. 1:E00581-E00581(2013).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=21383123; DOI=10.1073/pnas.1015773108;
RA   Andexer J.N., Kendrew S.G., Nur-e-Alam M., Lazos O., Foster T.A.,
RA   Zimmermann A.S., Warneck T.D., Suthar D., Coates N.J., Koehn F.E.,
RA   Skotnicki J.S., Carter G.T., Gregory M.A., Martin C.J., Moss S.J.,
RA   Leadlay P.F., Wilkinson B.;
RT   "Biosynthesis of the immunosuppressants FK506, FK520, and rapamycin
RT   involves a previously undescribed family of enzymes acting on chorismate.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4776-4781(2011).
CC   -!- FUNCTION: Involved in the biosynthesis of the macrocyclic amino acid-
CC       linked polyketides rapamycin which is a potent immunosuppressant that
CC       prevents T-cell proliferation through initial binding to the
CC       immunophilin FKBP12. Catalyzes the hydrolysis of chorismate via a 1,4-
CC       conjugate elimination of water to yield (4R,5R)-4,5-dihydroxycyclohexa-
CC       1,5-dienecarboxylic acid (DCDC). {ECO:0000269|PubMed:21383123}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + H2O = (3R,4R)-3,4-dihydroxy-3,4-dihydrobenzoate +
CC         pyruvate; Xref=Rhea:RHEA:38319, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29748, ChEBI:CHEBI:75717; EC=3.3.2.13;
CC         Evidence={ECO:0000250|UniProtKB:Q9KID9};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9KID9}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC       rapamycin. {ECO:0000269|PubMed:21383123}.
CC   -!- SIMILARITY: Belongs to the FkbO/Hyg5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA60468.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA60468.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X86780; CAA60468.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP006567; AGP59510.1; -; Genomic_DNA.
DR   PIR; T30234; T30234.
DR   AlphaFoldDB; Q54305; -.
DR   SMR; Q54305; -.
DR   STRING; 1343740.M271_40655; -.
DR   KEGG; src:M271_40655; -.
DR   PATRIC; fig|1343740.8.peg.6274; -.
DR   eggNOG; COG0251; Bacteria.
DR   HOGENOM; CLU_060951_0_0_11; -.
DR   GO; GO:0016803; F:ether hydrolase activity; IDA:UniProtKB.
DR   Gene3D; 3.30.1330.40; -; 1.
DR   InterPro; IPR031038; Chori_FkbO_Hyg5.
DR   InterPro; IPR035959; RutC-like_sf.
DR   SUPFAM; SSF55298; SSF55298; 1.
DR   TIGRFAMs; TIGR04444; chori_FkbO_Hyg5; 1.
PE   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..334
FT                   /note="Chorismatase"
FT                   /id="PRO_0000435463"
FT   ACT_SITE        328
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KID9"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KID9"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KID9"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KID9"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KID9"
FT   CONFLICT        73..74
FT                   /note="GS -> SR (in Ref. 1; CAA60468)"
FT   CONFLICT        175..176
FT                   /note="GG -> AR (in Ref. 1; CAA60468)"
FT   CONFLICT        216..227
FT                   /note="RATWLSPPGADD -> GHLALAAGG (in Ref. 1; CAA60468)"
FT   CONFLICT        241
FT                   /note="H -> Q (in Ref. 1; CAA60468)"
SQ   SEQUENCE   334 AA;  35793 MW;  ACDA374FD96306D6 CRC64;
     MTPPVTAPYC RFEKLGASDL DGDETLLGVI EHRTGHTGVS LAEGCPRTAV HTTTREDESF
     AEAWHAEGPK ESGSHDGVAW ARTPDYLFGV ARVPEGGRYA AGTAAVYTGI FDLIGTLGYP
     SLARTWNYVS GINTPNADGL EVYRDFCVGR AEALDARGID PATMPAATGI GAHGGGITCY
     FIAARAGDRV NMENPAVLTA HRYPQRYGPR PPVFSRATWL SPPGADDGRL FVSATAGIVG
     HETVHHGDVA AQCEVSLENI ARVIGAENLG RHGLRRGYAL ADVDHLKVYV RHREDISTVR
     RICAERLSRE ATVAVLHTDI ARTDLLVEIE GVVA