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Database: UniProt
Entry: A0A3S0IBL4_9DEIO
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ID   A0A3S0IBL4_9DEIO        Unreviewed;       371 AA.
AC   A0A3S0IBL4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
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   Name=pheA {ECO:0000313|EMBL:RTR29875.1};
GN   ORFNames=EJ104_02720 {ECO:0000313|EMBL:RTR29875.1};
OS   Deinococcus radiophilus.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=32062 {ECO:0000313|EMBL:RTR29875.1, ECO:0000313|Proteomes:UP000277766};
RN   [1] {ECO:0000313|EMBL:RTR29875.1, ECO:0000313|Proteomes:UP000277766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27603 {ECO:0000313|EMBL:RTR29875.1,
RC   ECO:0000313|Proteomes:UP000277766};
RA   Maclea K.S., Maynard C.R.;
RT   "Deinococcus radiophilus ATCC 27603 genome sequencing and assembly.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:RTR29875.1}.
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DR   EMBL; RXPE01000003; RTR29875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0IBL4; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000277766; 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; 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; 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, ECO:0000313|EMBL:RTR29875.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
FT   DOMAIN          13..101
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          101..278
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          292..369
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            271
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   371 AA;  40321 MW;  D22EEE8E4F131739 CRC64;
     MSDQPDRPPL TPEALAQAIA PHRERIDQID AQLLELLNQR ANQARAIGTL KGEAAVYRPE
     REAQVLARIA ALNAGPLHGN AVQRIFREVM SECLALERPL TVTYLGPRGT FTEQAAARHF
     GSAALLQPCA TIDETLREVE ARQADYAVVP IENSSEGAVN RTLDLLTSTE LRACGEATLR
     IHHLLMSQAQ ELPEVIQVYA HPQALAQCRD FLSRCLPQAE QVAVSSNAEA ARLAAQPQQT
     HTAAIGPGQA AALYGLNVLD QNVEDDPNNT TRFLVLGHQA AGPSGADRTT LIVAAPQADH
     AGAMHRLLEP FSRLGISMTK LESRPVRGGL WQYVFFIDIE GHADDPSVAQ ALLEMRQRAN
     FLKVVGSYPR A
//
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