AROA1_ALKHC
ID AROA1_ALKHC Reviewed; 431 AA.
AC Q9KCA6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00210};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase 1 {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSP synthase 1 {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSPS 1 {ECO:0000255|HAMAP-Rule:MF_00210};
GN Name=aroA1 {ECO:0000255|HAMAP-Rule:MF_00210}; Synonyms=aroE;
GN OrderedLocusNames=BH1667;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND SUBUNIT.
RA Malashkevich V.N., Toro R., Seidel R., Ramagopal U., Zencheck W.,
RA Almo S.C.;
RT "Crystal structure of putative 5-enolpyruvoylshikimate-3-phosphate synthase
RT from Bacillus halodurans C-125.";
RL Submitted (APR-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of
CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate
CC (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic
CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00210};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00210}.
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DR EMBL; BA000004; BAB05386.1; -; Genomic_DNA.
DR PIR; C83858; C83858.
DR RefSeq; WP_010897829.1; NC_002570.2.
DR PDB; 3RMT; X-ray; 2.80 A; A/B/C/D=1-431.
DR PDBsum; 3RMT; -.
DR AlphaFoldDB; Q9KCA6; -.
DR SMR; Q9KCA6; -.
DR STRING; 272558.10174284; -.
DR EnsemblBacteria; BAB05386; BAB05386; BAB05386.
DR KEGG; bha:BH1667; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_1_9; -.
DR OMA; YEDHRMA; -.
DR OrthoDB; 533829at2; -.
DR UniPathway; UPA00053; UER00089.
DR EvolutionaryTrace; Q9KCA6; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase 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; cd01556; EPSP_synthase; 1.
DR Gene3D; 3.65.10.10; -; 2.
DR HAMAP; MF_00210; EPSP_synth; 1.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR006264; EPSP_synthase.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR Pfam; PF00275; EPSP_synthase; 1.
DR PIRSF; PIRSF000505; EPSPS; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR01356; aroA; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..431
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase 1"
FT /id="PRO_0000088222"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 344
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 23..24
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 28
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 93..96
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 123
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 343
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 347
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 390
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:3RMT"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:3RMT"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:3RMT"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 412..417
FT /evidence="ECO:0007829|PDB:3RMT"
FT HELIX 421..431
FT /evidence="ECO:0007829|PDB:3RMT"
SQ SEQUENCE 431 AA; 45485 MW; 12F4FFBE7BA0743D CRC64;
MENKTVIPHA KGLKGTIKVP GDKSISHRAV MFGALAKGTT TVEGFLPGAD CLSTISCFQK
LGVSIEQAEE RVTVKGKGWD GLREPSDILD VGNSGTTTRL ILGILSTLPF HSVIIGDESI
GKRPMKRVTE PLKSMGAQID GRDHGNLTPL SIRGGQLKGI DFHSPVASAQ MKSAILLAGL
RAEGKTSVTE PAKTRDHTER MLEAFGVNIE KDGLTVSIEG GQMLTGQHVV VPGDISSAAF
FLVAGAMVPH SRITLTNVGI NPTRAGILEV LKQMGATLAM ENERVQGGEP VADLTIETSV
LQGVEIGGDI IPRLIDEIPI IAVLATQASG RTVIKDAEEL KVKETNRIDT VVSELTKLGA
SIHATDDGMI IEGPTPLKGG VTVSSHGDHR IGMAMAIAAL LAEKPVTVEG TEAIAVSYPS
FFDHLDRLKS E
