AROC_PSEA8
ID AROC_PSEA8 Reviewed; 363 AA.
AC B7UV40;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=PLES_36461;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(2009).
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 Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300};
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 -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00300}.
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DR EMBL; FM209186; CAW28373.1; -; Genomic_DNA.
DR RefSeq; WP_003087653.1; NC_011770.1.
DR PDB; 5Z9A; X-ray; 2.79 A; A/B=1-363.
DR PDBsum; 5Z9A; -.
DR AlphaFoldDB; B7UV40; -.
DR SMR; B7UV40; -.
DR KEGG; pag:PLES_36461; -.
DR HOGENOM; CLU_034547_0_2_6; -.
DR OMA; MLSINAV; -.
DR UniPathway; UPA00053; UER00090.
DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule.
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..363
FT /note="Chorismate synthase"
FT /id="PRO_1000119495"
FT REGION 42..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 125..127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 237..238
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 277
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 292..296
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 318
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:5Z9A"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:5Z9A"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:5Z9A"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:5Z9A"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5Z9A"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:5Z9A"
FT HELIX 132..147
FT /evidence="ECO:0007829|PDB:5Z9A"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:5Z9A"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:5Z9A"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5Z9A"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:5Z9A"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:5Z9A"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:5Z9A"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:5Z9A"
FT TURN 245..250
FT /evidence="ECO:0007829|PDB:5Z9A"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:5Z9A"
FT HELIX 328..348
FT /evidence="ECO:0007829|PDB:5Z9A"
SQ SEQUENCE 363 AA; 38987 MW; 1DAF720DEF754C01 CRC64;
MSGNTYGKLF TVTTAGESHG PALVAIVDGC PPGLELSARD LQRDLDRRKP GTSRHTTQRQ
EADEVEILSG VFEGKTTGTP IGLLIRNTDQ KSKDYSAIKD LFRPAHADYT YHHKYGVRDY
RGGGRSSARE TAMRVAAGAI AKKYLAGLGI QVRGYMSQLG PIEIPFRSWD SVEQNAFFSP
DPDKVPELEA YMDQLRRDQD SVGAKITVVA EGVPPGLGEP IFDRLDAELA HALMSINAVK
GVEIGAGFAS IAQRGTEHRD ELTPQGFLSN NAGGILGGIS SGQPIVAHLA LKPTSSITTP
GRSIDTAGEP VDMITKGRHD PCVGIRATPI AEAMMAIVLL DQLLRQRGQN ADVRVDTPVL
PQL
