AROC_AQUAE
ID AROC_AQUAE Reviewed; 398 AA.
AC O66493;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=aq_081;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND SUBUNIT.
RX PubMed=14705034; DOI=10.1002/prot.10592;
RA Viola C.M., Saridakis V., Christendat D.;
RT "Crystal structure of chorismate synthase from Aquifex aeolicus reveals a
RT novel beta alpha beta sandwich topology.";
RL Proteins 54:166-169(2004).
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 ECO:0000269|PubMed:14705034}.
CC -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00300}.
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DR EMBL; AE000657; AAC06434.1; -; Genomic_DNA.
DR PIR; B70308; B70308.
DR RefSeq; NP_213053.1; NC_000918.1.
DR RefSeq; WP_010879991.1; NC_000918.1.
DR PDB; 1Q1L; X-ray; 2.05 A; A/B/C/D=1-398.
DR PDBsum; 1Q1L; -.
DR AlphaFoldDB; O66493; -.
DR SMR; O66493; -.
DR STRING; 224324.aq_081; -.
DR EnsemblBacteria; AAC06434; AAC06434; aq_081.
DR KEGG; aae:aq_081; -.
DR PATRIC; fig|224324.8.peg.71; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_2_0_0; -.
DR InParanoid; O66493; -.
DR OMA; MLSINAV; -.
DR OrthoDB; 981870at2; -.
DR BRENDA; 4.2.3.5; 396.
DR UniPathway; UPA00053; UER00090.
DR EvolutionaryTrace; O66493; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004107; F:chorismate synthase activity; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR CDD; cd07304; Chorismate_synthase; 1.
DR DisProt; DP00559; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW FAD; Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT CHAIN 1..398
FT /note="Chorismate synthase"
FT /id="PRO_0000140537"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 133..135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 261..262
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 306
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 321..325
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 347
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1Q1L"
FT TURN 119..123
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:1Q1L"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:1Q1L"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1Q1L"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:1Q1L"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:1Q1L"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 353..376
FT /evidence="ECO:0007829|PDB:1Q1L"
FT HELIX 381..396
FT /evidence="ECO:0007829|PDB:1Q1L"
SQ SEQUENCE 398 AA; 44254 MW; A0C59327BFA3B39A CRC64;
MSLRYLRFLT AGESHGKGLT AILEGIPANL PLSEEEINHE LRRRQRGYGR GGRMKIEKDT
AEILSGVRFG KTLGSPIALF IRNRDWENWK EKMAIEGEPS PSVVPFTRPR PGHADLSGGI
KYNQRDLRNI LERASARETA ARVAVGAVCK KFLSEFGIKI GSFVVSIGQK EVEELKDKSY
FANPEKLLSY HEKAEDSELR IPFPEKDEEF KTYIDEVKEK GESLGGVFEV FALNVPPGLG
SHIQWDRRID GRIAQAMMSI QAIKGVEIGL GFEAARRFGS QVHDEIGWSE GKGYFRHSNN
LGGTEGGITN GMPIVVRVAM KPIPTLKNPL RSVDIETKEE MKAGKERTDI VAVPAASVVG
EAMLAIVLAD ALLEKLGGDF MEEVKKRFED YVNHVKSF
