ID A0A263HBU2_9PAST Unreviewed; 372 AA.
AC A0A263HBU2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=T-protein {ECO:0000256|PIRNR:PIRNR001499};
GN Name=tyrA {ECO:0000313|EMBL:SUU36484.1};
GN ORFNames=NCTC10851_01238 {ECO:0000313|EMBL:SUU36484.1};
OS Actinobacillus seminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=722 {ECO:0000313|EMBL:SUU36484.1, ECO:0000313|Proteomes:UP000254507};
RN [1] {ECO:0000313|EMBL:SUU36484.1, ECO:0000313|Proteomes:UP000254507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10851 {ECO:0000313|EMBL:SUU36484.1,
RC ECO:0000313|Proteomes:UP000254507};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; UFSB01000001; SUU36484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263HBU2; -.
DR InParanoid; A0A263HBU2; -.
DR OrthoDB; 6198144at2; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000254507; 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|PIRNR:PIRNR001499};
KW Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR001499}.
SQ SEQUENCE 372 AA; 42281 MW; 271CF0124E3AD67D CRC64;
MDALNELRNE IDKLDRELLN LFAKRLELVK QVGEVKHQYG LPIYVPEREN AMLQARRQEA
ENIGVPADLI EDVLRRLMRE SYFREHHLGF KTVNEAIKKI VIVGGDGKLG SLFSRYLSAS
GYNVIALDRD GWNQAETILS GANVVIVSVP IDQTLQTIER LAPYLSEQTL LADLTSVKRA
PLAKMLEVHQ GPVLGLHPMF GPDIASMAKQ VVVRCDGRYP EQYQWLLSQM QIWGAKIYQV
AAEEHDQSMT YIQALRHFAT FTSGLHLSKQ PVQLSQLLAL SSPIYRLELA MIGRLFAQDA
ALYADIIMDK PENLAVIKSL KQSYEESLAF FEQGDRQGFI DCFNQVHAWF GEYSEQFLKE
SRQLLQQAND GR
//
