AROA_COLP3
ID AROA_COLP3 Reviewed; 426 AA.
AC Q482G5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {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 {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210};
GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210}; OrderedLocusNames=CPS_2333;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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}.
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; CP000083; AAZ27668.1; -; Genomic_DNA.
DR RefSeq; WP_011043147.1; NC_003910.7.
DR PDB; 5XWB; X-ray; 2.20 A; A/B=1-426.
DR PDBsum; 5XWB; -.
DR AlphaFoldDB; Q482G5; -.
DR SMR; Q482G5; -.
DR STRING; 167879.CPS_2333; -.
DR EnsemblBacteria; AAZ27668; AAZ27668; CPS_2333.
DR KEGG; cps:CPS_2333; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_0_6; -.
DR OMA; YEDHRMA; -.
DR OrthoDB; 533829at2; -.
DR BRENDA; 2.5.1.19; 8143.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000000547; 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..426
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_1000012428"
FT REGION 94..97
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 342
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 22..23
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 124
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 170..172
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 198
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 337
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 341
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 345
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 387
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 412
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5XWB"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5XWB"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 336..340
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 386..392
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:5XWB"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:5XWB"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:5XWB"
FT HELIX 417..423
FT /evidence="ECO:0007829|PDB:5XWB"
SQ SEQUENCE 426 AA; 46234 MW; 69B32A4E8270AA9E CRC64;
MEQLTLNPIG KINGEIFLPG SKSLSNRALL IAALANGVTK ITNLLVSDDI NHMLNALKSL
GIEYTLSDCG TECTVIGNGG FFNAKKPLEL YLGNAGTAMR PLCAALAASE GEFILTGEPR
MKERPIGHLV DALAQLDADI EYLENKDYPP VKIKGKALTG NTVTIDGSIS SQFLTAILMI
APLLETNTTI EIDGELVSKP YIDITLDIMR RFNVSVQNND YKSFIVNGKQ SYQALDKYMV
EGDASSASYF LAAGAIKGGE VTVHGIGKLS VQGDKHFADV LEKMGAEIHW KDESITVIGK
PLTAVDMDMN HIPDAAMTIA TTALFATGTT TIRNIYNWRV KETDRLNAMA TELRKVGAEV
VEGKDYISIT PPKSLKHAEI DTYNDHRVAM CFSLVALSDT PVTINDPKCT AKTFPDYFDK
LAQVSC
