ID A0A1W2BQW8_9FIRM Unreviewed; 278 AA.
AC A0A1W2BQW8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
DE Short=PDT {ECO:0000256|RuleBase:RU361254};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
GN Name=pheA {ECO:0000256|RuleBase:RU361254};
GN ORFNames=SAMN04488500_10889 {ECO:0000313|EMBL:SMC75357.1};
OS Sporomusa malonica.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=112901 {ECO:0000313|EMBL:SMC75357.1, ECO:0000313|Proteomes:UP000192738};
RN [1] {ECO:0000313|EMBL:SMC75357.1, ECO:0000313|Proteomes:UP000192738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5090 {ECO:0000313|EMBL:SMC75357.1,
RC ECO:0000313|Proteomes:UP000192738};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361254};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741, ECO:0000256|RuleBase:RU361254}.
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DR EMBL; FWXI01000008; SMC75357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2BQW8; -.
DR STRING; 112901.SAMN04488500_10889; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000192738; Unassembled WGS sequence.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13633; PBP2_Sa-PDT_like; 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 InterPro; IPR018528; Preph_deHydtase_CS.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF01842; ACT; 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; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU361254};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|RuleBase:RU361254};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361254};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222,
KW ECO:0000256|RuleBase:RU361254};
KW Reference proteome {ECO:0000313|Proteomes:UP000192738}.
FT DOMAIN 4..181
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 195..272
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 278 AA; 30029 MW; F05A07255DDB4015 CRC64;
MTRTVGYLGP QGTYCEEIVL SLYGKEEACL KPFAGIDAAI RAVATGEVDE GIVPVENSLE
GSVNITLDTI AHDVNLYITK EVVLPVRHNL LAKKGCQEIA AIVSHPQALA QCRKTLGILY
PEAKLKPVES TAEAARIVAA SDGLYAAVGS LKAGEIYGLT VLAADIQDNN ANSTRFIGLE
RKQASSTTGK CKTTLVCQIN GERPGSLYNI LEEFAKREVN LTRIESRPAR TGLGMYIFFF
DIEGSTAESN IAAAISAVEE KCLWYKNFGS YPVYTINK
//