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Database: UniProt
Entry: P43900
LinkDB: P43900
Original site: P43900 
ID   CMPDT_HAEIN             Reviewed;         385 AA.
AC   P43900;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE   AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE   AltName: Full=P-protein {ECO:0000250|UniProtKB:P0A9J8};
DE   Includes:
DE     RecName: Full=Chorismate mutase {ECO:0000250|UniProtKB:P0A9J8};
DE              Short=CM {ECO:0000250|UniProtKB:P0A9J8};
DE              EC=5.4.99.5 {ECO:0000250|UniProtKB:P0A9J8};
DE   Includes:
DE     RecName: Full=Prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE              Short=PDT {ECO:0000250|UniProtKB:P0A9J8};
DE              EC=4.2.1.51 {ECO:0000250|UniProtKB:P0A9J8};
GN   Name=pheA; OrderedLocusNames=HI_1145;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate and the decarboxylation/dehydration of prephenate to
CC       phenylpyruvate. {ECO:0000250|UniProtKB:P0A9J8}.
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:0000250|UniProtKB:P0A9J8};
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:0000250|UniProtKB:P0A9J8};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000250|UniProtKB:P0A9J8}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P0A9J8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J8}.
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DR   EMBL; L42023; AAC22800.1; -; Genomic_DNA.
DR   PIR; B64186; B64186.
DR   RefSeq; NP_439303.1; NC_000907.1.
DR   RefSeq; WP_005647570.1; NC_000907.1.
DR   AlphaFoldDB; P43900; -.
DR   SMR; P43900; -.
DR   STRING; 71421.HI_1145; -.
DR   PRIDE; P43900; -.
DR   EnsemblBacteria; AAC22800; AAC22800; HI_1145.
DR   KEGG; hin:HI_1145; -.
DR   PATRIC; fig|71421.8.peg.1195; -.
DR   eggNOG; COG0077; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   HOGENOM; CLU_035008_1_0_6; -.
DR   OMA; PLMIYRE; -.
DR   PhylomeDB; P43900; -.
DR   BioCyc; HINF71421:G1GJ1-1178-MON; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.20.59.10; -; 1.
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   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; SSF48600; SSF48600; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   TIGRFAMs; TIGR01797; CM_P_1; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..385
FT                   /note="Bifunctional chorismate mutase/prephenate
FT                   dehydratase"
FT                   /id="PRO_0000119188"
FT   DOMAIN          1..92
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   DOMAIN          105..285
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          299..376
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   SITE            278
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   385 AA;  44001 MW;  2289BC7FF73C44EC CRC64;
     MALELSDIRQ QITQIDRSLL KLLSERHRLA FDVVRSKEIS QKSLRDVERE QQLLQELVQF
     AENENYQLEA QYITSIFQKI IEDSVLTQQV YLQNKLNEQR NQNLHIAFLG KRGSYSNLAA
     RNYAARYQKQ FVELGCQSFE QVFEKVQTGE ADFGVLPLEN TTSGAINEVY DLLQHTDLSL
     VGELAYPIKH CVLVNDKTDL NQIDTLYSHP QVIQQCSQFI HSLDRVHIEY CESSSHAMQL
     VASLNKPNIA ALGNEDGGKL YGLSVLKTNI ANQENNITRF IVVAKEPREV SSQIPTKTLL
     LMTTSQQAGA LVDALLVFKK HQINMTKLES RPIYGKPWEE MFYLEIEANI HHPDTKQALE
     ELKNYSNYLK ILGCYPSEIV KPVSV
//
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