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Database: UniProt
Entry: Q02287
LinkDB: Q02287
Original site: Q02287 
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   16-OCT-2013, entry version 85.
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; Enterobacteriales;
OC   Enterobacteriaceae; Pantoea.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1512561;
RA   Xia T., Zhao G., Fischer R.S., Jensen R.A.;
RT   "A monofunctional prephenate dehydrogenase created by cleavage of the
RT   5' 109 bp of the tyrA gene from Erwinia herbicola.";
RL   J. Gen. Microbiol. 138:1309-1316(1992).
CC   -!- CATALYTIC ACTIVITY: Chorismate = prephenate.
CC   -!- CATALYTIC ACTIVITY: Prephenate + NAD(+) = 4-hydroxyphenylpyruvate
CC       + CO(2) + NADH.
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
CC       biosynthesis; prephenate from chorismate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Contains 1 chorismate mutase domain.
CC   -!- SIMILARITY: Contains 1 prephenate/arogenate dehydrogenase domain.
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DR   EMBL; X60420; CAA42950.1; -; Genomic_DNA.
DR   EMBL; M74135; AAA24868.1; -; Genomic_DNA.
DR   PIR; S29934; S29934.
DR   ProteinModelPortal; Q02287; -.
DR   SMR; Q02287; 90-368.
DR   PRIDE; Q02287; -.
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:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase activity; IEA:UniProtKB-EC.
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   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR008244; Chor_mut/prephenate_DH_T.
DR   InterPro; IPR002701; Chorismate_mutase.
DR   InterPro; IPR020822; Chorismate_mutase_type_II.
DR   InterPro; IPR011277; CM_T.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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   TIGRFAMs; TIGR01799; CM_T; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Isomerase; Multifunctional enzyme; NAD; Oxidoreductase;
KW   Tyrosine biosynthesis.
FT   CHAIN         1    373       T-protein.
FT                                /FTId=PRO_0000119196.
FT   DOMAIN        1     90       Chorismate mutase.
FT   DOMAIN       99    361       Prephenate/arogenate dehydrogenase.
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
//
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