ID   TYRA_SHEON              Reviewed;         379 AA.
AC   Q8EH68;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=SO_1362;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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 {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       prephenate/arogenate dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AE014299; AAN54427.1; -; Genomic_DNA.
DR   RefSeq; NP_716982.1; NC_004347.2.
DR   RefSeq; WP_011071570.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EH68; -.
DR   SMR; Q8EH68; -.
DR   STRING; 211586.SO_1362; -.
DR   PaxDb; Q8EH68; -.
DR   DNASU; 1169183; -.
DR   KEGG; son:SO_1362; -.
DR   PATRIC; fig|1028802.3.peg.19; -.
DR   eggNOG; COG0287; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   HOGENOM; CLU_036672_1_1_6; -.
DR   OMA; EHDHGMT; -.
DR   OrthoDB; 533829at2; -.
DR   PhylomeDB; Q8EH68; -.
DR   BioCyc; SONE211586:G1GMP-1260-MON; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome;
KW   Tyrosine biosynthesis.
FT   CHAIN           1..379
FT                   /note="T-protein"
FT                   /id="PRO_0000398177"
FT   DOMAIN          3..94
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   DOMAIN          103..366
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
SQ   SEQUENCE   379 AA;  42876 MW;  F999D5BDAFD50AB7 CRC64;
     MNEKTTSELE HLRGLIDGVD QQLLHLLRKR LDLVAQVGTV KHAAGLPIYA PQREAAMLAK
     RREEAQTMGI APQLIEDILR RLMRESYLNE KDVGFKQVKN DLGSVVIVGG KGQLGGLFQQ
     MLRLSGYQVK VLDKDDWQQA ECLFADAGLV LVTVPIAITC DIIREKLTQL PRDCILADLT
     SIKTEPMQAM LAAHKGPVVG FHPMFGPDVG SLAKQVVVVC HGREADKYQW LLEQIAIWGA
     RIVEAEPECH DNAMQLVQAM RHFSTFVYGL NLCKEEADIE TLLKFSSPIY RLELAMVGRL
     FAQSPELYAD IIFAQQESQH AIGDYLDNYR EALELLKRGD REEFINQFQM VAKWFGDFAP
     QFQRESRMML QSVSDMKTN