AROC_ACIBY
ID AROC_ACIBY Reviewed; 363 AA.
AC B0VDX7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, 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}; OrderedLocusNames=ABAYE1953;
OS Acinetobacter baumannii (strain AYE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509173;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYE;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(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; CU459141; CAM86832.1; -; Genomic_DNA.
DR RefSeq; WP_000918444.1; NC_010410.1.
DR PDB; 5WUY; X-ray; 2.50 A; A/B=1-363.
DR PDBsum; 5WUY; -.
DR AlphaFoldDB; B0VDX7; -.
DR SMR; B0VDX7; -.
DR PRIDE; B0VDX7; -.
DR EnsemblBacteria; CAM86832; CAM86832; ABAYE1953.
DR GeneID; 66397239; -.
DR KEGG; aby:ABAYE1953; -.
DR HOGENOM; CLU_034547_0_2_6; -.
DR OMA; MLSINAV; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000002446; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW FAD; Flavoprotein; FMN; Lyase; NADP.
FT CHAIN 1..363
FT /note="Chorismate synthase"
FT /id="PRO_1000115320"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 125..127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 238..239
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 278
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 293..297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 319
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:5WUY"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:5WUY"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:5WUY"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5WUY"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5WUY"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5WUY"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:5WUY"
FT HELIX 132..149
FT /evidence="ECO:0007829|PDB:5WUY"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:5WUY"
FT TURN 170..175
FT /evidence="ECO:0007829|PDB:5WUY"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5WUY"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:5WUY"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:5WUY"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:5WUY"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:5WUY"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:5WUY"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:5WUY"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:5WUY"
FT HELIX 329..350
FT /evidence="ECO:0007829|PDB:5WUY"
SQ SEQUENCE 363 AA; 39001 MW; 6EC0BA8A243EE418 CRC64;
MAGNSIGQLF RVTTCGESHG VGLMAIVDGV PPGLALTEED LQKDLDRRKP GTSKFATQRK
EPDQVEIISG VFEGKTTGTP IGLLIRNTDQ KSKDYGNIAQ TFRPGHADYT YTQKYGFRDY
RGGGRSSARE TAMRVAAGAI AKKYLAEKFG VLIRGHVTQI GNEVAEKLDW NEVPNNPFFC
GDVDAVPRFE ALVTSLREQG TSCGAKLEIL AEKVPVGWGE PVFDRLDADI AHAMMSINAV
KGVEIGDGFA VAGQFGHETR DELTSHGFLA NHAGGILGGI SSGQTIRVAI ALKPTASITT
PGKTINLNRE DTDVLTKGRH DPCVGVRATP IAEAMLAIVL MDHFLRHRAQ NADVVPPFAP
IEP
