AROC_STRPN
ID AROC_STRPN Reviewed; 388 AA.
AC P0A2Y6; Q97Q57;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300};
DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300};
DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300};
GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300}; OrderedLocusNames=SP_1374;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN, COFACTOR, AND
RP SUBUNIT.
RX PubMed=14656434; DOI=10.1016/j.str.2003.11.005;
RA Maclean J., Ali S.;
RT "The structure of chorismate synthase reveals a novel flavin binding site
RT fundamental to a unique chemical reaction.";
RL Structure 11:1499-1511(2003).
CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and
CC the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to
CC yield chorismate, which is the branch point compound that serves as the
CC starting substrate for the three terminal pathways of aromatic amino
CC acid biosynthesis. This reaction introduces a second double bond into
CC the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300};
CC -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:14656434};
CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:14656434};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:14656434}.
CC -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00300}.
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DR EMBL; AE005672; AAK75472.1; -; Genomic_DNA.
DR PIR; G95159; G95159.
DR RefSeq; WP_001269860.1; NZ_AKVY01000001.1.
DR PDB; 1QXO; X-ray; 2.00 A; A/B/C/D=1-388.
DR PDBsum; 1QXO; -.
DR AlphaFoldDB; P0A2Y6; -.
DR SMR; P0A2Y6; -.
DR STRING; 170187.SP_1374; -.
DR BindingDB; P0A2Y6; -.
DR ChEMBL; CHEMBL4788; -.
DR EnsemblBacteria; AAK75472; AAK75472; SP_1374.
DR GeneID; 60233178; -.
DR KEGG; spn:SP_1374; -.
DR eggNOG; COG0082; Bacteria.
DR OMA; MLSINAV; -.
DR PhylomeDB; P0A2Y6; -.
DR BioCyc; SPNE170187:G1FZB-1383-MON; -.
DR BRENDA; 4.2.3.5; 1960.
DR UniPathway; UPA00053; UER00090.
DR EvolutionaryTrace; P0A2Y6; -.
DR PRO; PR:P0A2Y6; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; -; 1.
DR HAMAP; MF_00300; Chorismate_synth; 1.
DR InterPro; IPR000453; Chorismate_synth.
DR InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR InterPro; IPR020541; Chorismate_synthase_CS.
DR PANTHER; PTHR21085; PTHR21085; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; SSF103263; 1.
DR TIGRFAMs; TIGR00033; aroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW FAD; Flavoprotein; FMN; Lyase; NADP.
FT CHAIN 1..388
FT /note="Chorismate synthase"
FT /id="PRO_0000140655"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 130..132
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 251..252
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300,
FT ECO:0000269|PubMed:14656434"
FT BINDING 296
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300,
FT ECO:0000269|PubMed:14656434"
FT BINDING 311..315
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300,
FT ECO:0000269|PubMed:14656434"
FT BINDING 337
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:1QXO"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1QXO"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1QXO"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:1QXO"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1QXO"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:1QXO"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 343..365
FT /evidence="ECO:0007829|PDB:1QXO"
FT HELIX 371..386
FT /evidence="ECO:0007829|PDB:1QXO"
SQ SEQUENCE 388 AA; 42872 MW; 766565BDD9267D83 CRC64;
MRYLTAGESH GPRLTAIIEG IPAGLPLTAE DINEDLRRRQ GGYGRGGRMK IENDQVVFTS
GVRHGKTTGA PITMDVINKD HQKWLDIMSA EDIEDRLKSK RKITHPRPGH ADLVGGIKYR
FDDLRNSLER SSARETTMRV AVGAVAKRLL AELDMEIANH VVVFGGKEID VPENLTVAEI
KQRAAQSEVS IVNQEREQEI KDYIDQIKRD GDTIGGVVET VVGGVPVGLG SYVQWDRKLD
ARLAQAVVSI NAFKGVEFGL GFEAGYRKGS QVMDEILWSK EDGYTRRTNN LGGFEGGMTN
GQPIVVRGVM KPIPTLYKPL MSVDIETHEP YKATVERSDP TALPAAGMVM EAVVATVLAQ
EILEKFSSDN LEELKEAVAK HRDYTKNY
