ID A0A074JTD0_9RHOB Unreviewed; 366 AA.
AC A0A074JTD0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=DT23_11240 {ECO:0000313|EMBL:KEO60956.1};
OS Thioclava indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO60956.1, ECO:0000313|Proteomes:UP000027471};
RN [1] {ECO:0000313|EMBL:KEO60956.1, ECO:0000313|Proteomes:UP000027471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DT23-4 {ECO:0000313|EMBL:KEO60956.1,
RC ECO:0000313|Proteomes:UP000027471};
RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT Ocean.";
RL Antonie Van Leeuwenhoek 107:297-304(2015).
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:KEO60956.1}.
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DR EMBL; AUNB01000012; KEO60956.1; -; Genomic_DNA.
DR RefSeq; WP_038128582.1; NZ_AUNB01000012.1.
DR AlphaFoldDB; A0A074JTD0; -.
DR STRING; 1353528.DT23_11240; -.
DR eggNOG; COG0082; Bacteria.
DR OrthoDB; 9771806at2; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000027471; 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};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00300};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00300};
KW FMN {ECO:0000256|ARBA:ARBA00022643, 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:UP000027471}.
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 241..242
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 285
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 300..304
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 326
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
SQ SEQUENCE 366 AA; 38972 MW; DF3D69E3C764B984 CRC64;
MSFNSFGHLF RVTTWGESHG PALGATVDGC PPGIAIDEAF IQQFLDRRRP GQSKETTQRK
EPDAVRILSG TFEGRTTGTP IQVVIENTNQ RSKDYGEIAQ QFRPGHADIT YHQKYGVRDY
RGGGRSSARE TAARVAAGGV AQAALAQLVP DLKIYGYMVQ MGAKQINRAR FDREQILQNP
FFLPDALAVD EWADYLAAIR KGQNSVGAAI EVVAEGCPAG LGAPVYAKMD TELAAAMMSI
NAVKGVEIGE GMAAAALTGV DNADEMVMGP DGVEYLSNHA GGILGGITTG QPITVRFAVK
PTSSILTPRR SVNTRGEEVE VITKGRHDPC VGIRAVPVAE AMMACVILDQ LLMDRGQTGG
ARGVIG
//
