AROC_GLAP5
ID AROC_GLAP5 Reviewed; 360 AA.
AC B8F415;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=HAPS_0387;
OS Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Glaesserella.
OX NCBI_TaxID=557723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH0165;
RX PubMed=19074396; DOI=10.1128/jb.01682-08;
RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA Jin M., Jin Q., Chen H.;
RT "Complete genome sequence of Haemophilus parasuis SH0165.";
RL J. Bacteriol. 191:1359-1360(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; CP001321; ACL32067.1; -; Genomic_DNA.
DR RefSeq; WP_005712594.1; NC_011852.1.
DR AlphaFoldDB; B8F415; -.
DR SMR; B8F415; -.
DR STRING; 557723.HAPS_0387; -.
DR EnsemblBacteria; ACL32067; ACL32067; HAPS_0387.
DR GeneID; 66618821; -.
DR KEGG; hap:HAPS_0387; -.
DR HOGENOM; CLU_034547_0_2_6; -.
DR OMA; MLSINAV; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000006743; Chromosome.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD;
KW Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT CHAIN 1..360
FT /note="Chorismate synthase"
FT /id="PRO_1000132774"
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 246..247
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 286
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 301..305
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 327
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ SEQUENCE 360 AA; 38983 MW; D5FF83A64FD0065C CRC64;
MAGNSIGQLF KVTTFGESHG IALGCIVDGV PPNMELSEAD LQPDLDRRKP GTSRYTTPRR
EDDEVQILSG VFEGKTTGTS IGLIIKNGDQ RSKDYGDIMD KFRPGHADYT YQQKYGIRDY
RGGGRSSARE TAMRVAAGAI AKKYLKEQFG VEIRGYLSQI GSVKIDPQTV ANIEQIDWQQ
VNSNPFFCPD PVAVEQFDEL IRELKKEGNS IGAKLTVIAE NVPVGLGEPV FDRLDADLAH
ALMSINAVKG VEIGDGFAAV EQKGSEHRDE MTPEGFCSNH SGGILGGISS GQPIIAHIAL
KPTSSITVPG KSVNVHNEPV EVVTKGRHDP CVGIRAVPIA EAMMAIVVLD HLLRFKAQCR
