ID Q49YV9_STAS1 Unreviewed; 267 AA.
AC Q49YV9;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN OrderedLocusNames=SSP0876 {ECO:0000313|EMBL:BAE18021.1};
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE18021.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE18021.1, ECO:0000313|Proteomes:UP000006371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41
RC {ECO:0000313|Proteomes:UP000006371};
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=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00000913};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741}.
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DR EMBL; AP008934; BAE18021.1; -; Genomic_DNA.
DR RefSeq; WP_011302755.1; NZ_MTGA01000031.1.
DR AlphaFoldDB; Q49YV9; -.
DR KEGG; ssp:SSP0876; -.
DR PATRIC; fig|342451.11.peg.875; -.
DR eggNOG; COG0077; Bacteria.
DR HOGENOM; CLU_035008_0_2_9; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000006371; Chromosome.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001086; Preph_deHydtase.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF00800; PDT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW Reference proteome {ECO:0000313|Proteomes:UP000006371}.
FT DOMAIN 2..175
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 188..265
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 267 AA; 29506 MW; AEA013E4CF92FCA3 CRC64;
MKLYYLGPKG TFSYLAATQY KSESEIEFVP KSNLYEVVAS VSEDSQSIAV VPIENSIEGT
INIVADALTQ QNIYAQSELH LDIQFALYGS ENATVNDIST VYSIGPAISQ TSQYIQAHGF
DIAYVDSTIK SLDKISQNVG AIAPLGSGEA YGYTSIAQNI EDYPHNVTRF LVVSNQPKHI
EQATDTMLLI TPKFDKPGLL ASILNTFVLF NINLSWIESR PLKTQLGMYH FFVQADTPIS
EDLSKVIKIL NTLDFQVTII GTFNKLN
//
