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Database: UniProt
Entry: Q04U43_LEPBJ
LinkDB: Q04U43_LEPBJ
Original site: Q04U43_LEPBJ 
ID   Q04U43_LEPBJ            Unreviewed;       305 AA.
AC   Q04U43;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Bifunctional prephenate dehydrogenase/chorismate mutase {ECO:0000313|EMBL:ABJ75577.1};
GN   Name=tyrA {ECO:0000313|EMBL:ABJ75577.1};
GN   OrderedLocusNames=LBJ_0933 {ECO:0000313|EMBL:ABJ75577.1};
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ75577.1, ECO:0000313|Proteomes:UP000000656};
RN   [1] {ECO:0000313|EMBL:ABJ75577.1, ECO:0000313|Proteomes:UP000000656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197 {ECO:0000313|EMBL:ABJ75577.1,
RC   ECO:0000313|Proteomes:UP000000656};
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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DR   EMBL; CP000350; ABJ75577.1; -; Genomic_DNA.
DR   RefSeq; WP_011670564.1; NC_008510.1.
DR   AlphaFoldDB; Q04U43; -.
DR   KEGG; lbj:LBJ_0933; -.
DR   PATRIC; fig|355276.3.peg.2677; -.
DR   HOGENOM; CLU_055968_2_0_12; -.
DR   Proteomes; UP000000656; Chromosome 1.
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:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          6..305
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   305 AA;  34106 MW;  6646FA7E87CBBDBA CRC64;
     MKSKFSNILI YGLGLMGASL SLALKKKGIS AHVTGVVSSS KSKAKGESLK SADAIFTSEE
     FHSSKNWKDY DFIIFGVPVD LTAGLISELP TDFSGMITDL GSTKKDIIHA VETRFPGGYN
     YVSSHPMCGS EESGLEFANA SLYEGRLCIL TSPKNAKPEI KNRLENFWRF VGAETIEISA
     EEHDSILSYL SHSPHILSSI MADWAANQKT VKRYTDLSPI PLNGGGFRDM TRIAGSNPKM
     WAAIFGSNRN EIYKSLLDYR DRLDIILEKL NPKNVIDPKE WERFMETSRR SRDYILKSQD
     DSKKR
//
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