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Database: UniProt
Entry: A0A1E7RSS8_9GAMM
LinkDB: A0A1E7RSS8_9GAMM
Original site: A0A1E7RSS8_9GAMM 
ID   A0A1E7RSS8_9GAMM        Unreviewed;       369 AA.
AC   A0A1E7RSS8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE            EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN   ORFNames=BIY45_02160 {ECO:0000313|EMBL:OEZ02353.1};
OS   Stenotrophomonas sp. BIIR7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1904462 {ECO:0000313|EMBL:OEZ02353.1, ECO:0000313|Proteomes:UP000175905};
RN   [1] {ECO:0000313|EMBL:OEZ02353.1, ECO:0000313|Proteomes:UP000175905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIIR7 {ECO:0000313|EMBL:OEZ02353.1,
RC   ECO:0000313|Proteomes:UP000175905};
RA   Sanchez-Castro I., Ruiz-Fresneda M.A., Bakkali M., Kampfer P., Busse H.J.,
RA   Lopez-Fernandez M., Martinez-Rodriguez P., Merroun M.L.;
RT   "Stenotrophomonas bentonitica sp. nov., isolated from bentonite
RT   formations.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC         NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001162};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005067}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007964}.
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:OEZ02353.1}.
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DR   EMBL; MKCZ01000003; OEZ02353.1; -; Genomic_DNA.
DR   RefSeq; WP_070206523.1; NZ_JAAZUH010000002.1.
DR   AlphaFoldDB; A0A1E7RSS8; -.
DR   STRING; 1904462.BIY45_02160; -.
DR   GeneID; 84661845; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000175905; Unassembled WGS sequence.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.70.260; -; 1.
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; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000175905};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT   DOMAIN          4..276
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   DOMAIN          297..369
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   369 AA;  40323 MW;  B5A5A25460A75015 CRC64;
     MQRPVVGIVG SAGAYGRWLR TFLEQRMGLE VIGHDPADPA SDGPELLLER AQVLVFSAPI
     RHTPALIAEY VQRSAGREAG RLWLDVTSVK SEPVAAMLRS QAEVAGLHPM TAPPKAPTLK
     GRVMVVCEAR LSAWQPWVAQ LCAALEAECV RATPEHHDQV MALVQAMVHA THLAQAGVLR
     DYAELLGPLQ DLMPYRSASF ELDTAIIARI LSLNPAIYED IQFGNPHVAP MLDRLLAQLQ
     TLRSQVEQGD DAARAAFRQQ LLADNREHQG AALLADGNYT FERVGYLLAD LTERNAISVH
     LPEDRPGSLR ELLHVFERHG VSLASIHSSR TPGGEVHFRM GFVPGSDLQA MQRAAVEIDA
     SGIGRVLPR
//
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