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 03-APR-2013, entry version 83.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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:EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase activity; IEA: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; 6DGDH_C_like; 1.
DR SUPFAM; SSF48600; Chorismate_mut; 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
//
