ID TYRA_ECOLI Reviewed; 373 AA.
AC P07023; P78205; P78206;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 24-JAN-2024, entry version 189.
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; OrderedLocusNames=b2600, JW2581;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6396419; DOI=10.1016/0022-2836(84)90269-9;
RA Hudson G.S., Davidson B.E.;
RT "Nucleotide sequence and transcription of the phenylalanine and tyrosine
RT operons of Escherichia coli K12.";
RL J. Mol. Biol. 180:1023-1051(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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}.
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DR EMBL; M10431; AAA24331.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75649.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16485.2; -; Genomic_DNA.
DR PIR; A30274; KMECTD.
DR RefSeq; NP_417091.1; NC_000913.3.
DR RefSeq; WP_000225229.1; NZ_LN832404.1.
DR AlphaFoldDB; P07023; -.
DR SMR; P07023; -.
DR BioGRID; 4261238; 17.
DR DIP; DIP-11059N; -.
DR IntAct; P07023; 1.
DR STRING; 511145.b2600; -.
DR jPOST; P07023; -.
DR PaxDb; 511145-b2600; -.
DR EnsemblBacteria; AAC75649; AAC75649; b2600.
DR GeneID; 947115; -.
DR KEGG; ecj:JW2581; -.
DR KEGG; eco:b2600; -.
DR PATRIC; fig|1411691.4.peg.4139; -.
DR EchoBASE; EB1032; -.
DR eggNOG; COG0287; Bacteria.
DR eggNOG; COG1605; Bacteria.
DR HOGENOM; CLU_036672_1_1_6; -.
DR InParanoid; P07023; -.
DR OMA; EHDHGMT; -.
DR OrthoDB; 6198144at2; -.
DR PhylomeDB; P07023; -.
DR BioCyc; EcoCyc:CHORISMUTPREPHENDEHYDROG-MONOMER; -.
DR BioCyc; MetaCyc:CHORISMUTPREPHENDEHYDROG-MONOMER; -.
DR SABIO-RK; P07023; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00122; UER00961.
DR PRO; PR:P07023; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:EcoCyc.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IDA:EcoCyc.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IDA:EcoCyc.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IDA:EcoCyc.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR046825; PDH_C.
DR InterPro; IPR046826; PDH_N.
DR InterPro; IPR003099; Prephen_DH.
DR NCBIfam; TIGR01799; CM_T; 1.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF20463; PDH_C; 1.
DR Pfam; PF02153; PDH_N; 1.
DR PIRSF; PIRSF001499; Chor_mut_pdh_Tpr; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome;
KW Tyrosine biosynthesis.
FT CHAIN 1..373
FT /note="T-protein"
FT /id="PRO_0000119195"
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; 42043 MW; 481D0A03DE2AC832 CRC64;
MVAELTALRD QIDEVDKALL NLLAKRLELV AEVGEVKSRF GLPIYVPERE ASMLASRRAE
AEALGVPPDL IEDVLRRVMR ESYSSENDKG FKTLCPSLRP VVIVGGGGQM GRLFEKMLTL
SGYQVRILEQ HDWDRAADIV ADAGMVIVSV PIHVTEQVIG KLPPLPKDCI LVDLASVKNG
PLQAMLVAHD GPVLGLHPMF GPDSGSLAKQ VVVWCDGRKP EAYQWFLEQI QVWGARLHRI
SAVEHDQNMA FIQALRHFAT FAYGLHLAEE NVQLEQLLAL SSPIYRLELA MVGRLFAQDP
QLYADIIMSS ERNLALIKRY YKRFGEAIEL LEQGDKQAFI DSFRKVEHWF GDYAQRFQSE
SRVLLRQAND NRQ
//
