GenomeNet

Database: UniProt
Entry: N9T6M9_9GAMM
LinkDB: N9T6M9_9GAMM
Original site: N9T6M9_9GAMM 
ID   N9T6M9_9GAMM            Unreviewed;       754 AA.
AC   N9T6M9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_00210};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_00210};
GN   Name=aroA {ECO:0000256|HAMAP-Rule:MF_00210};
GN   ORFNames=F884_02237 {ECO:0000313|EMBL:ENX62771.1};
OS   Acinetobacter sp. CIP 102143.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144666 {ECO:0000313|EMBL:ENX62771.1};
RN   [1] {ECO:0000313|EMBL:ENX62771.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102143 {ECO:0000313|EMBL:ENX62771.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 102143.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001901, ECO:0000256|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:0000256|ARBA:ARBA00004811, ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|ARBA:ARBA00009948, ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENX62771.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; APSE01000080; ENX62771.1; -; Genomic_DNA.
DR   RefSeq; WP_004682340.1; NZ_KB850238.1.
DR   AlphaFoldDB; N9T6M9; -.
DR   PATRIC; fig|1144666.3.peg.2196; -.
DR   HOGENOM; CLU_018912_1_0_6; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000018424; Unassembled WGS sequence.
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:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR003099; Prephen_DH.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   NCBIfam; TIGR01356; aroA; 1.
DR   PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00210};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00210};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00210}.
FT   DOMAIN          12..301
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   REGION          402..405
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        627
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        655
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         331..332
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         336
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         432
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         654
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         658
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         707
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   754 AA;  80340 MW;  67147AC3144E05EA CRC64;
     MSQASVSKVL FKKVAFIGLG LIGSSLARVI VAEQLASEIV ASTRSKKTLE DAKALGLIQH
     GYTNPEEAVQ GADLIVLALP VRATQKVLEQ IKPYLAENVI ITDVGSTKGN VVDAAKAVFG
     EHLPVGFVPG HPIAGAEHTG VHAGKVDLFA NHKVILTPLP SSADWAVQKL IQLWSVAKAE
     VICMDVSKHD EVLAHTSHLP HLMAFNLVEQ LANREDNLDI FRYAAGGFRD FSRIAASDPQ
     MWHDIFFANK NAILNAVAGF EQQLSVLKQL IENEDSQALM GLLGHAQAAR QHFNHMLAKK
     PLMEKNKVTQ QFTILPGKKT FTGKFTVPGD KSVSHRSIMF GAIAEGTTHV TGFLEGEDAL
     ATLQAFRDMG VSIEGPKNGE VTIHGVGMQG LKAPASALYM GNSGTSMRLL SGMLSAQKFD
     SVMTGDASLS KRPMERIAKP LRLMGAQIQT TGEKGTPPVS ITGSQALKGI QYDLPMASAQ
     VKSGILLAGL WAEGETSVTE PEPTRDHTER MLRAFGYEVK TEGNKISLVG GGKLVGTDIQ
     VPSDISSAAF FMVGAAITEG ADVILEAVGI NPTRTGVIEI LKQMGSDISV ENERIAGGEP
     IADIHIKGSR TLKGIHMPED QVPLAIDEFP ALFIAAACAE GQTVLTGAAE LRVKESDRIQ
     VMADGLKVMG IDCTPTEDGI IIEGKGKSGD WSAIFTGGEI ESHHDHRIAM SFSIAGLRTS
     GEIIIHGTET VATSFPTFTE LANAAGLDLQ VVDQ
//
DBGET integrated database retrieval system