AROC_BIFLS
ID AROC_BIFLS Reviewed; 395 AA.
AC B7GS97; E8ML08;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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};
GN OrderedLocusNames=Blon_1598, BLIJ_1653;
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
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; CP001095; ACJ52677.1; -; Genomic_DNA.
DR EMBL; AP010889; BAJ69235.1; -; Genomic_DNA.
DR RefSeq; WP_012577913.1; NZ_JDTT01000018.1.
DR PDB; 4ECD; X-ray; 2.50 A; A/B=1-395.
DR PDBsum; 4ECD; -.
DR AlphaFoldDB; B7GS97; -.
DR SMR; B7GS97; -.
DR PRIDE; B7GS97; -.
DR EnsemblBacteria; ACJ52677; ACJ52677; Blon_1598.
DR KEGG; bln:Blon_1598; -.
DR KEGG; blon:BLIJ_1653; -.
DR PATRIC; fig|391904.8.peg.1667; -.
DR HOGENOM; CLU_034547_2_0_11; -.
DR OMA; MLSINAV; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000001360; 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; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW FAD; Flavoprotein; FMN; Lyase; NADP.
FT CHAIN 1..395
FT /note="Chorismate synthase"
FT /id="PRO_1000132755"
FT REGION 98..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 256..257
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 301
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 316..320
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"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:4ECD"
FT TURN 264..268
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4ECD"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 348..371
FT /evidence="ECO:0007829|PDB:4ECD"
FT HELIX 376..386
FT /evidence="ECO:0007829|PDB:4ECD"
SQ SEQUENCE 395 AA; 42317 MW; E4A8201B5BF239FB CRC64;
MLRWQTAGES HGEALVAMIE GLPAGVRIST DDIVSALARR RLGYGRGARM KFEQDKVRLL
TGVRHGLTLG SPVAIEIANT EWPKWTEVMS ADALDHDLPR EGRNAPLSRP RPGHADLTGM
RKYGFDDARP VLERSSARET ASRVALGEVA KQFLDQAFGI RTVAHVVALG GVQTNPDLPL
PTPDDLEALD ASPVRTLDKE AEVRIIERIN EAKKAADTLG GVIEVLAYGV PAGIGTYVES
DRRLDAALAS AIMGIQAFKG VEIGDGFLAA SRPGSQAHDE IVVNADGRID RLSNRAGGIE
GGMSNGQVIR VRGAMKPIPS IPKALRTVDV LTGESAQAIN QRSDSTAVPA ASVVAEAMVR
LTLAKYALDK FGGDSVAETR RNLESYLASW PEHMR
