ID A0A1H9YDT6_9GAMM Unreviewed; 381 AA.
AC A0A1H9YDT6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ORFNames=SAMN02583745_00181 {ECO:0000313|EMBL:SES66618.1};
OS Thorsellia anophelis DSM 18579.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Thorselliaceae; Thorsellia.
OX NCBI_TaxID=1123402 {ECO:0000313|EMBL:SES66618.1, ECO:0000313|Proteomes:UP000242642};
RN [1] {ECO:0000313|Proteomes:UP000242642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18579 {ECO:0000313|Proteomes:UP000242642};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOHV01000001; SES66618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9YDT6; -.
DR STRING; 1123402.SAMN02583745_00181; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000242642; 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; cd13631; PBP2_Ct-PDT_like; 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; IPR010952; CM_P_1.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR NCBIfam; TIGR01797; CM_P_1; 1.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000242642}.
FT DOMAIN 1..91
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 104..284
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 298..375
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT SITE 277
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 381 AA; 43010 MW; 5E38D78DC62B5994 CRC64;
MPNQNLINLR ERITEIDEQL LTLLSKRSDI ATEVAKTKLA LHKPIRDEIR EAELLSALIE
KSNALGLDQN YIARVFRLII EDSVQKQQKW MNQELSSTDS SASRVAFLGP KGSYSHLAAR
AFGHSHFDKT IECSCHRFDD IFEMVETGHA EYAVVPIENT SSGAINEVYD LLQSTSLSIV
GEKIMPIEHC FMGIKPINLD EITTVYSHPQ PFQQCSQFLS KYPHWKIVYC ESTAAAMEMV
YNEQNSSHVA IGSEAGGQIY GLNLIEKVPT NQGQNMTRFV VLHRKPKTIP LHIPTKSTFL
MATGQHAGAL VEALIILKNH NIVMSKLESR PMKGNPWEEM FYIDVQANLI SEEFQEAITH
LKSETRFFKV LGSYPVDGIL F
//
