ID A0A1Q9YBI5_9FIRM Unreviewed; 360 AA.
AC A0A1Q9YBI5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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 AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000256|ARBA:ARBA00031520};
DE AltName: Full=p-protein {ECO:0000256|ARBA:ARBA00031175};
GN ORFNames=BM735_10530 {ECO:0000313|EMBL:OLU37382.1};
OS Erysipelotrichaceae bacterium NYU-BL-F16.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=1917462 {ECO:0000313|EMBL:OLU37382.1, ECO:0000313|Proteomes:UP000186748};
RN [1] {ECO:0000313|EMBL:OLU37382.1, ECO:0000313|Proteomes:UP000186748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-F16 {ECO:0000313|EMBL:OLU37382.1,
RC ECO:0000313|Proteomes:UP000186748};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-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}.
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:OLU37382.1}.
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DR EMBL; MPJX01000220; OLU37382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9YBI5; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000186748; 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; 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; IPR011279; Chorismate_mutase_GmP.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR001086; Preph_deHydtase.
DR NCBIfam; TIGR01805; CM_mono_grmpos; 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; 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 1..88
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 92..267
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 278..355
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT SITE 260
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 360 AA; 40747 MW; 5001DFF385971BBD CRC64;
MNKLENAREK INEIDKKIAG LFEARMDAVK DVIAYKQEND LPVFDGNRER TLIERNRKMI
QNPDYLSMYE DFLQFMLTQS KAYQKSLIAQ DVIAYSGIKG AFAHMISEKI FEGNPKLAFN
SFEEVIDAVV DHKVEFGVIP FENTNSGLVG EVLDLLYQKP VYIVKVADLK VDQCLLGLPE
ASLKDIEWVY SKDQALMQSR EFLESLGVKS VPYPNTALAA QYVAREQDKT KAAIGARENA
ALYNLKVLAS HIEETATNTT RFLVVAASPN TQKKDHLAMI FTTSDEVGAL SKVINRIAEH
GINMDTLQSR PIKERPFEYF FYVQCTGNLE EENLSSLMKS MEDVVSNVKI LGTYEILEKQ
//
