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Database: UniProt
Entry: A0A0W7U6E7_9GAMM
LinkDB: A0A0W7U6E7_9GAMM
Original site: A0A0W7U6E7_9GAMM 
ID   A0A0W7U6E7_9GAMM        Unreviewed;       375 AA.
AC   A0A0W7U6E7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=T-protein {ECO:0000256|PIRNR:PIRNR001499};
GN   Name=tyrA {ECO:0000313|EMBL:KUE81653.1};
GN   ORFNames=ATO46_01580 {ECO:0000313|EMBL:KUE81653.1};
OS   Aeromonas schubertii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=652 {ECO:0000313|EMBL:KUE81653.1, ECO:0000313|Proteomes:UP000054876};
RN   [1] {ECO:0000313|EMBL:KUE81653.1, ECO:0000313|Proteomes:UP000054876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE81653.1,
RC   ECO:0000313|Proteomes:UP000054876};
RA   Liu L., Li Q., Zhang F., Shi B.;
RT   "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR001499}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000256|PIRNR:PIRNR001499}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR001499}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUE81653.1}.
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DR   EMBL; LPUO01000001; KUE81653.1; -; Genomic_DNA.
DR   RefSeq; WP_050665853.1; NZ_LPUO01000001.1.
DR   AlphaFoldDB; A0A0W7U6E7; -.
DR   STRING; 652.WL1483_4344; -.
DR   OrthoDB; 6198144at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000054876; Unassembled WGS sequence.
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; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
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; IEA:UniProtKB-UniPathway.
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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001499};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001499};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR001499};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR001499};
KW   NAD {ECO:0000256|PIRNR:PIRNR001499};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR001499};
KW   Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR001499}.
FT   DOMAIN          1..90
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          99..361
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   375 AA;  41414 MW;  A131239FD9D0C1C3 CRC64;
     MAKELDVLRD KIDEVDRELV TLLARRLALV GEVGEVKSRH GLPIYAPDRE AAMLARRREE
     AEAHGVPGDL VEDVLRRIMR ESYASEKETG FKCIKPDLRH VVVVGGGGAL GGLFVHMLRL
     SGYRVEVLEK EDWADSESLL ANAGMVMVAV PIDVTEAVIG QLGRLPEDCL LVDLTSVKQG
     PMAAMLAAHP GPVLGLHPMF GPDVASLAKQ VIVCCAGRDP LASEWLCQQM TIWGARLVAV
     SAAEHDQAMT LIQALRHFAT FAYGRHLAEE GADLEQLLRL SSPIYRLELA MVGRLFAQDP
     ALYADIILSS PQNLAMIRRY YEEFGRSLAL LEQGQREGFV EAFNRVADYF GEHASQFLRE
     SKQLLAQAND RRHLG
//
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