ID A0A2Z4JRC3_9BURK Unreviewed; 360 AA.
AC A0A2Z4JRC3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000256|ARBA:ARBA00014401};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
DE EC=5.4.99.5 {ECO:0000256|ARBA:ARBA00012404};
DE AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000256|ARBA:ARBA00031520};
DE AltName: Full=p-protein {ECO:0000256|ARBA:ARBA00031175};
GN Name=pheA {ECO:0000313|EMBL:MBT8618989.1};
GN ORFNames=DP176_03485 {ECO:0000313|EMBL:RAZ42899.1}, G6650_07665
GN {ECO:0000313|EMBL:MBT8618989.1}, Pas1_02320
GN {ECO:0000313|EMBL:AWW49310.1};
OS Polynucleobacter paneuropaeus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=2527775 {ECO:0000313|EMBL:AWW49310.1, ECO:0000313|Proteomes:UP000248592};
RN [1] {ECO:0000313|Proteomes:UP000248592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG-25-Pas1-D2 {ECO:0000313|Proteomes:UP000248592};
RA Hahn M.W.;
RT "Description of a new Polynucleobacter species.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAZ42899.1, ECO:0000313|Proteomes:UP000251072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FUKU-NW-11 {ECO:0000313|EMBL:RAZ42899.1,
RC ECO:0000313|Proteomes:UP000251072};
RA Hahn M.W.;
RT "Genome of strain Polynucleobacter sp. FUKU-NW-11.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AWW49310.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MG-25-Pas1-D2 {ECO:0000313|EMBL:AWW49310.1};
RX PubMed=30465643; DOI=10.1099/ijsem.0.003130;
RA Hoetzinger M., Schmidt J., Pitt A., Koll U., Lang E., Hahn M.W.;
RT "Polynucleobacter paneuropaeus sp. nov., characterized by six strains
RT isolated from freshwater lakes located along a 3000 km north-south cross-
RT section across Europe.";
RL Int. J. Syst. Evol. Microbiol. 69:203-213(2019).
RN [4] {ECO:0000313|EMBL:MBT8618989.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AP-ClouGG-20-C5 {ECO:0000313|EMBL:MBT8618989.1};
RX PubMed=33674852; DOI=10.1093/gbe/evab019;
RA Hoetzinger M., Pitt A., Huemer A., Hahn M.W.;
RT "Continental-Scale Gene Flow Prevents Allopatric Divergence of Pelagic
RT Freshwater Bacteria. .";
RL Genome Biol. Evol. 13:evab019-evab019(2021).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate and the decarboxylation/dehydration of prephenate to
CC phenylpyruvate. {ECO:0000256|ARBA:ARBA00002364}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00000913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000824};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000256|ARBA:ARBA00004817}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; CP030085; AWW49310.1; -; Genomic_DNA.
DR EMBL; JAANGZ010000004; MBT8618989.1; -; Genomic_DNA.
DR EMBL; QMCH01000002; RAZ42899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4JRC3; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000248592; Chromosome.
DR Proteomes; UP000251072; Unassembled WGS sequence.
DR Proteomes; UP000744877; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13630; PBP2_PDT_1; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR010957; G/b/e-P-prot_chorismate_mutase.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR NCBIfam; TIGR01807; CM_P2; 1.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF00800; PDT; 1.
DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:MBT8618989.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW Reference proteome {ECO:0000313|Proteomes:UP000248592}.
FT DOMAIN 2..92
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 92..267
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 279..356
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 260
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 360 AA; 38834 MW; F3EB7A039D557EF4 CRC64;
MSTEEQRLAP LRDKIDALDA KILDLLSQRA QAAQEVGHVK GGFASPIFRP ERERQVVAKL
QEINQGPLLP DGIAAIWREV MSACRALEAR QTIAYLGPVG TFSEQAAQTY FGQSIAGLPC
VSIDEVFKAV EKGAAQFGVV PVENSSEGAI SRTLDLLLDA PVQISGEVVL PIRHHLLTKS
GSLDGVTTVC AHAQALAQCQ QWLSEHAPQL KRQAVSSNAE AARMAAADPT LAAIAGEPAQ
IAYSLQAVAS QIQDDPHNRT RFVVIGNYVC QATGNDQTSL VLSVDNQPGA VHRLLAPLAK
HGVSMNRFES RPARKGTWEY HFFIDVAGHA DEEKVAKALT ELQDTAAFYK KLGSYPRSSI
//