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Entry: A0A0Q8V414_9ACTN
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ID   A0A0Q8V414_9ACTN        Unreviewed;       392 AA.
AC   A0A0Q8V414;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ORFNames=ASE19_19220 {ECO:0000313|EMBL:KRC49021.1};
OS   Nocardioides sp. Root79.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC49021.1, ECO:0000313|Proteomes:UP000051414};
RN   [1] {ECO:0000313|EMBL:KRC49021.1, ECO:0000313|Proteomes:UP000051414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root79 {ECO:0000313|EMBL:KRC49021.1,
RC   ECO:0000313|Proteomes:UP000051414};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC49021.1, ECO:0000313|Proteomes:UP000051414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root79 {ECO:0000313|EMBL:KRC49021.1,
RC   ECO:0000313|Proteomes:UP000051414};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRC49021.1}.
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DR   EMBL; LMIP01000014; KRC49021.1; -; Genomic_DNA.
DR   RefSeq; WP_056893423.1; NZ_LMIP01000014.1.
DR   AlphaFoldDB; A0A0Q8V414; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000051414; 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; PS00789; CHORISMATE_SYNTHASE_3; 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|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00300};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051414}.
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         300
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT   BINDING         315..319
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT   BINDING         341
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
SQ   SEQUENCE   392 AA;  41952 MW;  75BDD4A439BCBEBD CRC64;
     MLRWLTAGES HGPSLVAILE GLPAHVEVTT DDISDSLARR RLGYGRGARM KFEADEVTVT
     GGVRHGRTQG GPVAIQVGNT EWPKWETVMA ADPVEPELLE KQARNAPLTR PRPGHADLAG
     MQKYDFEDAR PILERASARE TAARVALGRV ASNFLEQATG ARIVSHVLEI GGVRTPSRDV
     PLPDDVTRLD EDPVRCLDPD GSKQMIERID QAHKDGDTLG GVVEVVVHGL PPGLGSHVHW
     DRRLDARLAG ALMGIQAIKG VEVGDGFELA ATPGSLAHDE IVPTDEGLRR VSGRSGGTEG
     GMTTGEVLRV RAAMKPIATV PRALRTVDLA TGEEAVAHHQ RSDVCAVPAA GIVAEAMVAL
     VLADAVLEKF GGDSVGETRR NVQTYLDNLR YR
//
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