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Database: UniProt
Entry: A0A0Q4NNB7_9GAMM
LinkDB: A0A0Q4NNB7_9GAMM
Original site: A0A0Q4NNB7_9GAMM 
ID   A0A0Q4NNB7_9GAMM        Unreviewed;       373 AA.
AC   A0A0Q4NNB7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=T-protein {ECO:0000256|PIRNR:PIRNR001499};
GN   Name=tyrA {ECO:0000313|EMBL:KQN64792.1};
GN   ORFNames=ASF13_02715 {ECO:0000313|EMBL:KQN64792.1};
OS   Erwinia sp. Leaf53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN64792.1, ECO:0000313|Proteomes:UP000050856};
RN   [1] {ECO:0000313|EMBL:KQN64792.1, ECO:0000313|Proteomes:UP000050856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf53 {ECO:0000313|EMBL:KQN64792.1,
RC   ECO:0000313|Proteomes:UP000050856};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN64792.1, ECO:0000313|Proteomes:UP000050856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf53 {ECO:0000313|EMBL:KQN64792.1,
RC   ECO:0000313|Proteomes:UP000050856};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQN64792.1}.
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DR   EMBL; LMLK01000001; KQN64792.1; -; Genomic_DNA.
DR   RefSeq; WP_056232260.1; NZ_LMLK01000001.1.
DR   AlphaFoldDB; A0A0Q4NNB7; -.
DR   STRING; 1736225.ASF13_02715; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000050856; 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, ECO:0000313|EMBL:KQN64792.1};
KW   NAD {ECO:0000256|PIRNR:PIRNR001499};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR001499};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050856};
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   373 AA;  41967 MW;  EDE143914D9AE8BA CRC64;
     MVAELTALRD QIDETDKALL DLLAKRLALV AEVGEVKSRY GLPIYVPERE ASMLASRRKE
     AEQLGVPPDL IEDVLRRVMR ESYTSENDKG FKTLNPGLRS VVIVGGRGQM GRLFERMLTL
     SGYQVEILDK EDWHRADALL ANAGMVIVSV PIHLTEQVIA ELPPLPQDCI LVDLCSVKNK
     PLQAMLAAHG GPVLGLHPMF GPDSGSLAKQ VVVWCDGRQP EAYQWFLEQI QVWGARLHRI
     SAVEHDQNMA FIQALRHFAT FAYGLHLAEE NVQLDQLLAL SSPIYRLELA MVGRLFAQDP
     QLYADIIMSS ESNLALIKRY YKRFGEAIGL LEQGDKQAFI ASFRRVEQWF GDHAQRFQAE
     SRILLKQAND SRP
//
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