AROC_LANP1
ID AROC_LANP1 Reviewed; 380 AA.
AC C8WAF3;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=Apar_0662;
OS Lancefieldella parvula (strain ATCC 33793 / DSM 20469 / CCUG 32760 / JCM
OS 10300 / KCTC 3663 / VPI 0546 / 1246) (Atopobium parvulum).
OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Lancefieldella.
OX NCBI_TaxID=521095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33793 / DSM 20469 / CCUG 32760 / JCM 10300 / KCTC 3663 / VPI
RC 0546 / 1246;
RX PubMed=21304653; DOI=10.4056/sigs.29547;
RA Copeland A., Sikorski J., Lapidus A., Nolan M., Del Rio T.G., Lucas S.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Pukall R., Chertkov O.,
RA Brettin T., Han C., Detter J.C., Kuske C., Bruce D., Goodwin L.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Atopobium parvulum type strain (IPP 1246).";
RL Stand. Genomic Sci. 1:166-173(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; CP001721; ACV51091.1; -; Genomic_DNA.
DR AlphaFoldDB; C8WAF3; -.
DR SMR; C8WAF3; -.
DR STRING; 521095.Apar_0662; -.
DR EnsemblBacteria; ACV51091; ACV51091; Apar_0662.
DR KEGG; apv:Apar_0662; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_0_0_11; -.
DR OMA; PCIVQRA; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000000960; 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 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD;
KW Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT CHAIN 1..380
FT /note="Chorismate synthase"
FT /id="PRO_0000405964"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 126..128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 300
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 315..319
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 342
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ SEQUENCE 380 AA; 40578 MW; 365B1E25CC817C4F CRC64;
MMTSTFGTTV KVSIFGESHA PKIGCTIEGL PAGFTVDLHE LKTFLQRRSP SHPWDTPRKE
IDNPKFVSGI SAKGILDGFP LTAELPNNNV RQKDYTATKL VPRPGHADFS AWAKWGNSYK
QTGGGHFSAR LTAPLCIAGG IALQILHAQG ITIAAHVLKI KNINDTPFKL IDNSVEANKL
LALQMNQLLQ AAPQELPFLD AQTGEKTRAL LTQLRSEKNT VGGIIECVAT GVPAGIGCPH
FQGLENTISA AVFGVPAVKA IEFGSGMNVA NLLGSENNDA YEVRDGSVVP TTNHAGGILG
GISTGAPIWF RCALKPISSI GLSQHSVNLQ TMESEQLVVQ GRHDVTAVLR AVPCVESAFA
LALLDTLYSW PSEQNGYHND
