ID Q7VQF6_BLOFL Unreviewed; 377 AA.
AC Q7VQF6;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=T-protein {ECO:0000256|PIRNR:PIRNR001499};
GN Name=tyrA {ECO:0000313|EMBL:CAD83697.1};
GN OrderedLocusNames=Bfl178 {ECO:0000313|EMBL:CAD83697.1};
OS Blochmannia floridanus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=203907 {ECO:0000313|EMBL:CAD83697.1, ECO:0000313|Proteomes:UP000002192};
RN [1] {ECO:0000313|EMBL:CAD83697.1, ECO:0000313|Proteomes:UP000002192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kramerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83697.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VQF6; -.
DR STRING; 203907.Bfl178; -.
DR KEGG; bfl:Bfl178; -.
DR eggNOG; COG0287; Bacteria.
DR eggNOG; COG1605; Bacteria.
DR HOGENOM; CLU_036672_1_1_6; -.
DR OrthoDB; 6198144at2; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000002192; 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; 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:CAD83697.1};
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..364
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 377 AA; 43922 MW; 12E04E602BA4516B CRC64;
MMDRLNFLRS EIDKIDQSLL NLLSKRLSLV SQVGEIKSQL GLFIYDPERE KMILSQRKQE
ALKLGISPNL VRDILRRIMR ESYSYENEKG FKKLYPSSRP VVIIGGNGRM GQFFFKMLTL
SGYQVRILDQ DDWIHAKSIL TNVGVVFISV PIYSVIKVIN QLPHLSNDCI IVDLSSVKKS
SLTAILKIHT GPVLGLHPMF SPDTTITASM IKKVVICCDG RYPQEYQWLL QQLKLWGAKV
YYCNFIEHDK YMSFIQSLCH FTIFVMGYHL FKENIDLKKI LSFSSPMFQL ELILIGRLFT
QNPQLYADII MSSKNNIIVI KRYYKRLGKM LMLLEQNNKE EFINQFKKIK CWLDSYAGIF
LKDSSNLLKY INDIQEY
//
