ID   TYRA_ENTAG              Reviewed;         373 AA.
AC   Q02287;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=T-protein;
DE   Includes:
DE     RecName: Full=Chorismate mutase;
DE              Short=CM;
DE              EC=5.4.99.5;
DE   Includes:
DE     RecName: Full=Prephenate dehydrogenase;
DE              Short=PDH;
DE              EC=1.3.1.12;
GN   Name=tyrA;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1512561; DOI=10.1099/00221287-138-7-1309;
RA   Xia T., Zhao G., Fischer R.S., Jensen R.A.;
RT   "A monofunctional prephenate dehydrogenase created by cleavage of the 5'
RT   109 bp of the tyrA gene from Erwinia herbicola.";
RL   J. Gen. Microbiol. 138:1309-1316(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC         ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC         NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       prephenate/arogenate dehydrogenase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X60420; CAA42950.1; -; Genomic_DNA.
DR   EMBL; M74135; AAA24868.1; -; Genomic_DNA.
DR   PIR; S29934; S29934.
DR   RefSeq; WP_010248465.1; NZ_WSSZ01000007.1.
DR   AlphaFoldDB; Q02287; -.
DR   SMR; Q02287; -.
DR   STRING; 549.BW31_02110; -.
DR   GeneID; 66824882; -.
DR   eggNOG; COG0287; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   OrthoDB; 533829at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00122; UER00961.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR008244; Chor_mut/prephenate_DH_T.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR011277; CM_T.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003099; Prephen_DH.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF02153; PDH; 1.
DR   PIRSF; PIRSF001499; Chor_mut_pdh_Tpr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01799; CM_T; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Isomerase; Multifunctional enzyme; NAD; Oxidoreductase;
KW   Tyrosine biosynthesis.
FT   CHAIN           1..373
FT                   /note="T-protein"
FT                   /id="PRO_0000119196"
FT   DOMAIN          1..90
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   DOMAIN          99..361
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
SQ   SEQUENCE   373 AA;  41847 MW;  C6E3C3B877A0628C CRC64;
     MVAELTALRD QIDSVDKALL DLLAKRLELV AEVGEVKSRY GLPIYVPERE ASMLASRRKE
     AEALGVPPDL IEDVLRRVMR ESYTSENDKG FKTLCPELRP VVIVGGKGQM GRLFEKMLGL
     SGYTVKTLDK EDWPQAETLL SDAGMVIISV PIHLTEQVIA QLPPLPEDCI LVDLASVKNR
     PLQAMLAAHN GPVLGLHPMF GPDSGSLAKQ VVVWCDGRQP EAYQWFLEQI QVWGARLHRI
     SAVEHDQNMA FIQALRHFAT FAYGLHLAEE NVNLDQLLAL SSPIYRLELA MVGRLFAQDP
     QLYADIIMSS ESNLALIKRY YQRFGEAIAL LEQGDKQAFI ASFNRVEQWF GDHAKRFLVE
     SRSLLRSAND SRP