ID A0A1M7MK62_9SPHI Unreviewed; 369 AA.
AC A0A1M7MK62;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05216524_10484 {ECO:0000313|EMBL:SHM91361.1};
OS Mucilaginibacter sp. OK098.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHM91361.1, ECO:0000313|Proteomes:UP000184158};
RN [1] {ECO:0000313|EMBL:SHM91361.1, ECO:0000313|Proteomes:UP000184158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK098 {ECO:0000313|EMBL:SHM91361.1,
RC ECO:0000313|Proteomes:UP000184158};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRCM01000004; SHM91361.1; -; Genomic_DNA.
DR RefSeq; WP_073404411.1; NZ_FRCM01000004.1.
DR AlphaFoldDB; A0A1M7MK62; -.
DR STRING; 1855297.SAMN05216524_10484; -.
DR OrthoDB; 9771806at2; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000184158; 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.
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|HAMAP-Rule:MF_00300}.
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 125..127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 244..245
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 289
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 304..308
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 330
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
SQ SEQUENCE 369 AA; 39805 MW; FFC4C7FD1C662AE3 CRC64;
MAGNSFGQLF RITTFGESHG EAIGVIIDGC PAQLDVDLDY IQGELDKRKP GQSKITTQRK
ESDTVKILSG VFEGKTTGTP IAMLIPNEDQ RSKDYTHNVD VFRPSHADYT YQAKYGIRDH
RGGGRSSARE TAARVAAGAL AKLLLKTQGI EIVAHVSSVG KIDAPNVEIK SAQEFIDERE
KNIVRCADPA TAEEMIEYID SIRKQGDTVG GKVSCHILNC PVGLGEPVFD KLHADLGKAM
LSINAVHGFE YGSGFSGSEM RGSEHNDIFI KNHLGDIGTL TNYSGGIQGG LSNGMPIDFK
VAFKPVATIM HNQATIDSEG NAAEISGKGR HDPCVVPRAV PIVEAMAALV LADHWLRNRN
SIMPSAFPY
//
