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 01-MAY-2013, entry version 71.
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.,
RA Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
RA Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
RA White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
RA Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
RA 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: 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 (By similarity).
CC -!- SIMILARITY: Contains 1 chorismate mutase domain.
CC -!- SIMILARITY: Contains 1 prephenate/arogenate dehydrogenase domain.
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DR EMBL; AE014299; AAN54427.1; -; Genomic_DNA.
DR RefSeq; NP_716982.1; NC_004347.2.
DR ProteinModelPortal; Q8EH68; -.
DR STRING; 211586.SO_1362; -.
DR DNASU; 1169183; -.
DR EnsemblBacteria; AAN54427; AAN54427; SO_1362.
DR GeneID; 1169183; -.
DR KEGG; son:SO_1362; -.
DR PATRIC; 23522378; VBISheOne101494_1311.
DR eggNOG; COG0287; -.
DR HOGENOM; HOG000275725; -.
DR KO; K14187; -.
DR OMA; QRFGEAI; -.
DR ProtClustDB; PRK11199; -.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Cytoplasm; Isomerase; Multifunctional enzyme; NAD;
KW Oxidoreductase; Reference proteome; Tyrosine biosynthesis.
FT CHAIN 1 379 T-protein.
FT /FTId=PRO_0000398177.
FT DOMAIN 3 94 Chorismate mutase.
FT DOMAIN 103 366 Prephenate/arogenate dehydrogenase.
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
//
