ID A0A080M9J5_9PROT Unreviewed; 363 AA.
AC A0A080M9J5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-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:KFB77923.1};
GN ORFNames=AW06_000715 {ECO:0000313|EMBL:KFB77923.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB77923.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB77923.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:KFB77923.1}.
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DR EMBL; JDST02000013; KFB77923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M9J5; -.
DR STRING; 1453999.AW06_000715; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000021315; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000021315}.
FT DOMAIN 3..95
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 95..270
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 282..359
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 9..36
FT /evidence="ECO:0000256|SAM:Coils"
FT SITE 263
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 363 AA; 39868 MW; 60556DDAB56C86ED CRC64;
MSGDLQSELA LVRQQIDGLD RQLLDLLNRR ARYAQQVGEI KARHGEAGFI YRPEREAQVL
QRIQEINPGP LSNESVTWFF REVMSACLSL EQPLGIAFLG PLGTFSESAA IKHFGHAARP
MPQISIDDVF REVESCHADY AVVPIENSTE GAVGRTLDLL LTTPLKVCGE VVLRIHQHLL
SNERSLGEVV KVYSHAQSLA QCHEWLNRSL PNVQRIPVGS NAQAAQLAAT EAGVAAIAGQ
AAAERYRLPE LASNIEDEPN NTTRFVVLGR HDAGPSGRDK TSLIMSAHNQ TGALSKLLAP
FSDAGVSLTR LESRPARHTL WAYVFFVDVE GHRDDVAVRS ALTELARRAP YLKLLGSYPV
AVY
//
