ID A0A2X2ELH2_RAOPL Unreviewed; 386 AA.
AC A0A2X2ELH2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:RWT15960.1};
GN ORFNames=DN603_27275 {ECO:0000313|EMBL:RWT15960.1}, SAMEA2273876_05052
GN {ECO:0000313|EMBL:SAQ10939.1};
OS Raoultella planticola (Klebsiella planticola).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX NCBI_TaxID=575 {ECO:0000313|EMBL:RWT15960.1, ECO:0000313|Proteomes:UP000288843};
RN [1] {ECO:0000313|EMBL:SAQ10939.1, ECO:0000313|Proteomes:UP000078124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2880STDY5682802 {ECO:0000313|EMBL:SAQ10939.1,
RC ECO:0000313|Proteomes:UP000078124};
RG Pathogen Informatics;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RWT15960.1, ECO:0000313|Proteomes:UP000288843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GEO_47_Down_B {ECO:0000313|EMBL:RWT15960.1,
RC ECO:0000313|Proteomes:UP000288843};
RA Mathys D.A., Mollenkopf D.F., Feicht S.M., Adams R.J., Albers A.L.,
RA Stuever D.M., Daniels J.B., Wittum T.E.;
RT "Carbapenemase-producing Enterobacteriaceae present in wastewater treatment
RT plant effluent and nearby surface waters in the US.";
RL Submitted (JUN-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:RWT15960.1}.
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DR EMBL; QKOX01000044; RWT15960.1; -; Genomic_DNA.
DR EMBL; FLAC01000029; SAQ10939.1; -; Genomic_DNA.
DR RefSeq; WP_004866518.1; NZ_VNVX01000041.1.
DR AlphaFoldDB; A0A2X2ELH2; -.
DR GeneID; 72409189; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000078124; Unassembled WGS sequence.
DR Proteomes; UP000288843; 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, ECO:0000313|EMBL:RWT15960.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RWT15960.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
FT DOMAIN 1..92
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 105..285
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 299..376
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT SITE 278
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 386 AA; 42866 MW; 7428D166AF0FF4FC CRC64;
MTEENPLLAL RDKISALDEK LLALLAERRG LAVEVGKAKL ASHRPVRDID RERDLLERLI
TLGKSHHLDA HYITRLFQLI IEDSVLTQQT LLQQHLNKIN PHSARVAFLG PKGSYSHLAA
RQYAARHFEQ FIESGCAKFA DIFNQVETGQ ADYAVVPIEN TSSGGINDVY DLLQHTSLSI
VGELTIPIDH CVLVSASTDP QHIQTVYSHP QPFQQCSQYL SRYPHWKIEY TESTSAAMEK
VAQANSPGVA ALGSEAGGAL YGLQVLEHCQ ANQTQNITRF LVLARKAVNV SEQVPAKTTL
LMATGQQAGA LVEALLVLRN HNLIMTKLES RPIHGNPWEE MFYLDIQANL ESMPMRKALK
ELAEITRSMK VLGCYPGENV VPVDPI
//
