AROC_HAEIN
ID AROC_HAEIN Reviewed; 357 AA.
AC P43875;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=HI_0196;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC21865.1; -; Genomic_DNA.
DR PIR; G64053; G64053.
DR RefSeq; NP_438365.1; NC_000907.1.
DR RefSeq; WP_005694095.1; NC_000907.1.
DR AlphaFoldDB; P43875; -.
DR SMR; P43875; -.
DR STRING; 71421.HI_0196; -.
DR EnsemblBacteria; AAC21865; AAC21865; HI_0196.
DR KEGG; hin:HI_0196; -.
DR PATRIC; fig|71421.8.peg.201; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_0_2_6; -.
DR OMA; MLSINAV; -.
DR PhylomeDB; P43875; -.
DR BioCyc; HINF71421:G1GJ1-207-MON; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000000579; 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 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD;
KW Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT CHAIN 1..357
FT /note="Chorismate synthase"
FT /id="PRO_0000140594"
FT REGION 37..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Basic and acidic residues"
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 243..244
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 283
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 298..302
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 324
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ SEQUENCE 357 AA; 38691 MW; 4504562BADF68164 CRC64;
MAGNTIGQLF RVTTFGESHG IALGCIVDGV PPNLELSEKD IQPDLDRRKP GTSRYTTPRR
EDDEVQILSG VFEGKTTGTS IGMIIKNGDQ RSQDYGDIKD RFRPGHADFT YQQKYGIRDY
RGGGRSSARE TAMRVAAGAI AKKYLREHFG IEVRGFLSQI GNIKIAPQKV GQIDWEKVNS
NPFFCPDESA VEKFDELIRE LKKEGDSIGA KLTVIAENVP VGLGEPVFDR LDADLAHALM
GINAVKGVEI GDGFAVVEQR GSEHRDEMTP NGFESNHAGG ILGGISSGQP IIATIALKPT
SSITIPGRSI NLNGEAVEVV TKGRHDPCVG IRAVPIAEAM VAIVLLDHLL RFKAQCK
