AROC_HELPY
ID AROC_HELPY Reviewed; 365 AA.
AC P56122;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000303|PubMed:15095868};
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};
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH FMN, COFACTOR, AND
RP SUBUNIT.
RX PubMed=15095868; DOI=10.1016/j.jmb.2003.12.072;
RA Ahn H.J., Yoon H.J., Lee B., Suh S.W.;
RT "Crystal structure of chorismate synthase: a novel FMN-binding protein fold
RT and functional insights.";
RL J. Mol. Biol. 336:903-915(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 ECO:0000269|PubMed:15095868};
CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:15095868};
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:15095868}.
CC -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00300}.
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DR EMBL; AE000511; AAD07726.1; -; Genomic_DNA.
DR PIR; G64602; G64602.
DR RefSeq; NP_207457.1; NC_000915.1.
DR RefSeq; WP_001094036.1; NC_018939.1.
DR PDB; 1UM0; X-ray; 1.95 A; A/B/C/D=1-365.
DR PDB; 1UMF; X-ray; 2.25 A; A/B/C/D=1-365.
DR PDBsum; 1UM0; -.
DR PDBsum; 1UMF; -.
DR AlphaFoldDB; P56122; -.
DR SMR; P56122; -.
DR IntAct; P56122; 7.
DR MINT; P56122; -.
DR STRING; 85962.C694_03430; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR PaxDb; P56122; -.
DR EnsemblBacteria; AAD07726; AAD07726; HP_0663.
DR KEGG; hpy:HP_0663; -.
DR PATRIC; fig|85962.47.peg.713; -.
DR eggNOG; COG0082; Bacteria.
DR OMA; MLSINAV; -.
DR PhylomeDB; P56122; -.
DR BRENDA; 4.2.3.5; 2604.
DR UniPathway; UPA00053; UER00090.
DR EvolutionaryTrace; P56122; -.
DR Proteomes; UP000000429; 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; IDA:UniProtKB.
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 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; Reference proteome.
FT CHAIN 1..365
FT /note="Chorismate synthase"
FT /id="PRO_0000140596"
FT BINDING 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 123..125
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300,
FT ECO:0000269|PubMed:15095868"
FT BINDING 241..242
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 281
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 296..300
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300,
FT ECO:0000269|PubMed:15095868"
FT BINDING 322
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 126..145
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 180..195
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:1UM0"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1UM0"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1UM0"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 328..349
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1UM0"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:1UM0"
SQ SEQUENCE 365 AA; 40100 MW; 98ABC708E1909561 CRC64;
MNTLGRFLRL TTFGESHGDV IGGVLDGMPS GIKIDYALLE NEMKRRQGGR NVFITPRKED
DKVEITSGVF EDFSTGTPIG FLIHNQRARS KDYDNIKNLF RPSHADFTYF HKYGIRDFRG
GGRSSARESA IRVAAGAFAK MLLREIGIVC ESGIIEIGGI KAKNYDFNHA LKSEIFALDE
EQEEAQKTAI QNAIKNHDSI GGVALIRARS IKTNQKLPIG LGQGLYAKLD AKIAEAMMGL
NGVKAVEIGK GVESSLLKGS EYNDLMDQKG FLSNRSGGVL GGMSNGEEII VRVHFKPTPS
IFQPQRTIDI NGNECECLLK GRHDPCIAIR GSVVCESLLA LVLADMVLLN LTSKIEYLKT
IYNEN
