TYRA_STAS1
ID TYRA_STAS1 Reviewed; 363 AA.
AC Q49XG5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Prephenate dehydrogenase;
DE Short=PDH;
DE EC=1.3.1.12;
GN Name=tyrA; OrderedLocusNames=SSP1387;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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 -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008934; BAE18532.1; -; Genomic_DNA.
DR RefSeq; WP_002483353.1; NZ_MTGA01000038.1.
DR AlphaFoldDB; Q49XG5; -.
DR SMR; Q49XG5; -.
DR STRING; 342451.SSP1387; -.
DR EnsemblBacteria; BAE18532; BAE18532; SSP1387.
DR GeneID; 66867610; -.
DR KEGG; ssp:SSP1387; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_2_1_9; -.
DR OMA; MWRDICL; -.
DR OrthoDB; 533829at2; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000006371; Chromosome.
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 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; IPR003099; Prephen_DH.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF02153; PDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD;
KW Oxidoreductase; Reference proteome; Tyrosine biosynthesis.
FT CHAIN 1..363
FT /note="Prephenate dehydrogenase"
FT /id="PRO_0000282666"
FT DOMAIN 2..291
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT DOMAIN 296..363
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT BINDING 3..33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 363 AA; 40963 MW; 130EB5895E8F90DF CRC64;
MKQILFVGLG LIGGSLASNL RYYHDDIEIT AFDADTSQLD KALSIGIIDY QSTDYKTSVE
NADIIIYATP VQQTVKYLQD LPNYQLKKHV IITDTGSTKS TIQQYEQFLL NHDIHLVGGH
PMAGSHKSGV LNAKKHLFEN AFYILVHNET DNDAAFEEIQ HLLQTTSAKF ISTTAEEHDF
VTGIVSHVPH IIASSLVHLN AQHVEDSSLV KTLAAGGFRD ITRIASSNPI MWRDITIENK
NTILRILKEW KNQMSDVINI IEHNNPDELY DFFNDAKVYR DQLPLKQQGA LSVEYDLYVD
IPDKPGMISK VTNILSLHNI SISNLRILEV REDIYGALRV SFKNPQDRKD GADALSDFDT
YFD
