ID A0A1J4UYW0_9BACT Unreviewed; 371 AA.
AC A0A1J4UYW0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000256|ARBA:ARBA00014401};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
DE AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000256|ARBA:ARBA00031520};
DE AltName: Full=p-protein {ECO:0000256|ARBA:ARBA00031175};
GN ORFNames=AUJ18_07630 {ECO:0000313|EMBL:OIO30098.1};
OS Candidatus Hydrogenedentes bacterium CG1_02_42_14.
OC Bacteria; Candidatus Hydrogenedentes.
OX NCBI_TaxID=1805216 {ECO:0000313|EMBL:OIO30098.1, ECO:0000313|Proteomes:UP000182230};
RN [1] {ECO:0000313|EMBL:OIO30098.1, ECO:0000313|Proteomes:UP000182230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_42_14 {ECO:0000313|EMBL:OIO30098.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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 -!- 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:OIO30098.1}.
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DR EMBL; MNVL01000171; OIO30098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4UYW0; -.
DR STRING; 1805216.AUJ18_07630; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000182230; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
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; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
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; PS00858; PREPHENATE_DEHYDR_2; 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};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
FT DOMAIN 6..95
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 95..272
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 289..366
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 265
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 371 AA; 41402 MW; 8F3AFA4BEFFD213F CRC64;
MAKEAKRANR GLKRLRVAID SLDSKLVALL DERVKFAAET LHHKRKLGLE LYQPSREAEV
IKKAISRRKL FPEASLKSIY REIIGATLQL ENPFTAAILG PEATYTHLAT VKHFGHTVNI
SFESSIPDVF LKVEKKEADL GVVPIENSSE GSIVHTLDNL VTSTLSIAAE ILMPVRHNLM
ALQENSKKFL PNLIVSHAQG LAQCRNFIES HYPGVPLKQV PSTAIAALEA SKKKGVAAIA
SELAAEKYGL KIIHSNIEDI ADNTTRFLVL RNSDETIPAK RKGCEYKTSI AFSMKDKPGA
LFSMLEPFKR SGINLTKIES RPSRIKTWIY TFFLDMEGHA DDLKVKRALT ELQEECHFYR
LLGSYPKGIT L
//
