HYG5_STRHY
ID HYG5_STRHY Reviewed; 340 AA.
AC O30478;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=3-hydroxybenzoate synthase {ECO:0000303|PubMed:21383123};
DE EC=4.1.3.45 {ECO:0000269|PubMed:21383123, ECO:0000269|PubMed:26247872};
OS Streptomyces hygroscopicus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=1912;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29253;
RX PubMed=9426000; DOI=10.1016/s0378-1119(97)00450-2;
RA Ruan X., Stassi D., Lax S.A., Katz L.;
RT "A second type-I PKS gene cluster isolated from Streptomyces hygroscopicus
RT ATCC 29253, a rapamycin-producing strain.";
RL Gene 203:1-9(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-240; CYS-327 AND GLU-334,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=26247872; DOI=10.1021/jacs.5b05559;
RA Hubrich F., Juneja P., Muller M., Diederichs K., Welte W., Andexer J.N.;
RT "Chorismatase mechanisms reveal fundamentally different types of reaction
RT in a single conserved protein fold.";
RL J. Am. Chem. Soc. 137:11032-11037(2015).
CC -!- FUNCTION: Involved in the biosynthesis of BC325, a rapamycin analog
CC containing a 3-hydroxybenzoate starter unit. Catalyzes the hydrolysis
CC of chorismate via an intramolecular mechanism to yield 3-
CC hydroxybenzoate (3HBA). {ECO:0000269|PubMed:21383123,
CC ECO:0000269|PubMed:26247872}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = 3-hydroxybenzoate + pyruvate;
CC Xref=Rhea:RHEA:38315, ChEBI:CHEBI:15361, ChEBI:CHEBI:16193,
CC ChEBI:CHEBI:29748; EC=4.1.3.45;
CC Evidence={ECO:0000269|PubMed:21383123, ECO:0000269|PubMed:26247872};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.53 mM for chorismate {ECO:0000269|PubMed:21383123};
CC Note=kcat is 22.4 sec(-1) for 3-hydroxybenzoate synthase activity
CC with chorismate as substrate. {ECO:0000269|PubMed:21383123};
CC -!- SUBUNIT: Trimer. {ECO:0000305|PubMed:26247872}.
CC -!- SIMILARITY: Belongs to the FkbO/Hyg5 family. {ECO:0000305}.
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DR EMBL; AF007101; AAC38060.1; -; Genomic_DNA.
DR PIR; T03220; T03220.
DR PDB; 5A3K; X-ray; 2.75 A; A/B/C=1-340.
DR PDB; 5AG3; X-ray; 1.90 A; A/B/C=1-340.
DR PDBsum; 5A3K; -.
DR PDBsum; 5AG3; -.
DR AlphaFoldDB; O30478; -.
DR SMR; O30478; -.
DR BRENDA; 4.1.3.45; 6043.
DR GO; GO:0016833; F:oxo-acid-lyase 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 3D-structure; Lyase.
FT CHAIN 1..340
FT /note="3-hydroxybenzoate synthase"
FT /id="PRO_0000435464"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:26247872"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26247872"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26247872"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26247872"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26247872"
FT SITE 240
FT /note="Important for product selectivity"
FT /evidence="ECO:0000269|PubMed:26247872"
FT SITE 327
FT /note="Important for product selectivity"
FT /evidence="ECO:0000269|PubMed:26247872"
FT MUTAGEN 240
FT /note="G->A: Decrease of the 3-hydroxybenzoate synthase
FT activity compared to the wild-type and complete loss of
FT product selectivity."
FT /evidence="ECO:0000269|PubMed:26247872"
FT MUTAGEN 327
FT /note="C->A: Decrease of the 3-hydroxybenzoate synthase
FT activity compared to the wild-type and complete loss of
FT product selectivity."
FT /evidence="ECO:0000269|PubMed:26247872"
FT MUTAGEN 334
FT /note="E->Q: Loss of chorismatase activity."
FT /evidence="ECO:0000269|PubMed:26247872"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 26..38
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:5AG3"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 170..191
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5A3K"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 255..270
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 289..298
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5AG3"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5AG3"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:5AG3"
SQ SEQUENCE 340 AA; 37429 MW; 74B9440290366D8B CRC64;
MNPSSLVLNG LTSYFENGRA RVVPPVGRNI LGVVNYASVC EYPTLDHGYP ELEINMVAPT
AEPFAEVWVT DAESEHGERD GITYAHDGEY FFCAGRVPPT GRYTEATRAA YVTMFELLEE
FGYSSVFRMW NFIGDINRDN AEGMEVYRDF CRGRAEAFEQ CRLEFDQFPA ATGIGSRGGG
IAFYLLACRS GGHVHIENPR QVPAYHYPKR YGPRAPRFAR ATYLPSRAAD GVGGQVFVSG
TASVLGHETA HEGDLVKQCR LALENIELVI SGGNLAAHGI SAGHGLTALR NIKVYVRRSE
DVPAVREICR EAFSPDADIV YLTVDVCRSD LLVEIEGVVM
