AROC_CLAM3
ID AROC_CLAM3 Reviewed; 412 AA.
AC A5CRZ1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=CMM_1798;
OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=443906;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 382;
RX PubMed=18192381; DOI=10.1128/jb.01595-07;
RA Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA Bartels D.;
RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT in pathogenicity.";
RL J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN01854.1; -; Genomic_DNA.
DR RefSeq; WP_012038486.1; NC_009480.1.
DR AlphaFoldDB; A5CRZ1; -.
DR SMR; A5CRZ1; -.
DR STRING; 443906.CMM_1798; -.
DR EnsemblBacteria; CAN01854; CAN01854; CMM_1798.
DR GeneID; 56886125; -.
DR KEGG; cmi:CMM_1798; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_2_0_11; -.
DR OMA; MLSINAV; -.
DR OrthoDB; 981870at2; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000001564; 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 InterPro; IPR020541; Chorismate_synthase_CS.
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.
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; Aromatic amino acid biosynthesis; FAD;
KW Flavoprotein; FMN; Lyase; NADP.
FT CHAIN 1..412
FT /note="Chorismate synthase"
FT /id="PRO_0000322397"
FT BINDING 40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 134..136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 255..256
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 299
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 314..318
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 340
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ SEQUENCE 412 AA; 42970 MW; 3EE358540D81B85A CRC64;
MLRWLTAGES HGPELIAVLE GLPAGVPVSL DGIRADLARR KLGYGRGARM AFEQDELSLS
TGVVHGRTLG SPIAVRIGNT EWPKWVDIMS PEPVDPEKLQ GARAAALTRP RPGHADLVGM
QKYDFDEARP VLERASARET AARVALGAVA RAFLAELGIT LVSHTLSIGP VRVPEGAPLP
TPADVDALDA DPLRCFHPET SARMVAEVDD TKSSGDTVGG VVEVLAYDLP PGLGSHVHWD
RRLDSKLAAA LMGIQAIKGV EVGDGFLTTT RRGSEAHDEL FSTDAGIGRS TDRAGGTEGG
MSTGTVLRVR AGMKPIATVP RALRTIDTAT GGAAPANHQR SDVCAVPAAG VVAEAMVALT
LADAVLEKFG GDSVGETLRN LRGYLDAIPE GRRTGADLVD EADAAPPAAP EA
