ID A0A221W2D0_9PSEU Unreviewed; 395 AA.
AC A0A221W2D0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chorismate synthase {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|HAMAP-Rule:MF_00300};
DE Short=CS {ECO:0000256|HAMAP-Rule:MF_00300};
DE EC=4.2.3.5 {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|HAMAP-Rule:MF_00300};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000256|HAMAP-Rule:MF_00300};
GN Name=aroC {ECO:0000256|HAMAP-Rule:MF_00300,
GN ECO:0000313|EMBL:ASO19928.1};
GN ORFNames=AHOG_11425 {ECO:0000313|EMBL:ASO19928.1}, FHR81_000391
GN {ECO:0000313|EMBL:MBB5919362.1};
OS Actinoalloteichus hoggarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO19928.1, ECO:0000313|Proteomes:UP000204221};
RN [1] {ECO:0000313|EMBL:ASO19928.1, ECO:0000313|Proteomes:UP000204221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO19928.1,
RC ECO:0000313|Proteomes:UP000204221};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT strain of Actinoalloteichus hoggarensis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5919362.1, ECO:0000313|Proteomes:UP000541573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8639 {ECO:0000313|EMBL:MBB5919362.1,
RC ECO:0000313|Proteomes:UP000541573};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605};
CC -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605};
CC Note=Reduced FMN (FMNH(2)). {ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7. {ECO:0000256|ARBA:ARBA00005044, ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00300}.
CC -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000256|ARBA:ARBA00008014, ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605}.
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DR EMBL; CP022521; ASO19928.1; -; Genomic_DNA.
DR EMBL; JACHJM010000001; MBB5919362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221W2D0; -.
DR KEGG; ahg:AHOG_11425; -.
DR OrthoDB; 9771806at2; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000204221; Chromosome.
DR Proteomes; UP000541573; Unassembled WGS sequence.
DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; Chorismate synthase AroC; 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 NCBIfam; TIGR00033; aroC; 1.
DR PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1.
DR PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; Chorismate synthase, AroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00300};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00300}; FAD {ECO:0000256|HAMAP-Rule:MF_00300};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00300};
KW FMN {ECO:0000256|HAMAP-Rule:MF_00300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00300};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00300};
KW Reference proteome {ECO:0000313|Proteomes:UP000204221}.
FT BINDING 40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 135..137
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 256..257
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 302
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 317..321
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 343
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
SQ SEQUENCE 395 AA; 42105 MW; 8492963ABF06B057 CRC64;
MLRWMTAGES HGPALVAVME GMVAGVEVTT ADMTTQLERR RLGFGRSPRM AFEVDELEVI
GGVRHGITQG GPVAVRIGNT EWPKWRQVMA ADPVDEAELA GMARNAPLTR PRPGHADLAG
MQKYGFDEAR PVLERASARE TAARTVLGTV AARFLDQVLG VRVISHVVSI GAAASEGHPV
PLPDDLPAID EHPVRSFDQA AGEAMMAEVE SAKQDGDTLG GVIEVLAYGL PPGLGSHVHW
DRRLDARLAG ALMGVQAMKG VEIGDGFTTA RRRGSAAHDE IDPADGPTWV RRRSNRAGGL
EGGMTNGEPL RVRVAMKPIS TVPRALATMD VSTGEPAVAI HQRSDICAVP RAGVVVESVV
ALVLADAVLE KFGGDSVAET RRNAEGYLRE LEERR
//
