ID U5WCR6_9ACTN Unreviewed; 318 AA.
AC U5WCR6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872, 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=AFR_42565 {ECO:0000313|EMBL:AGZ46767.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ46767.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ46767.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ46767.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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; CP006272; AGZ46767.1; -; Genomic_DNA.
DR RefSeq; WP_023563098.1; NC_022657.1.
DR AlphaFoldDB; U5WCR6; -.
DR STRING; 1246995.AFR_42565; -.
DR KEGG; afs:AFR_42565; -.
DR PATRIC; fig|1246995.3.peg.8614; -.
DR eggNOG; COG0077; Bacteria.
DR HOGENOM; CLU_035008_0_0_11; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
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; cd13632; PBP2_Aa-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; IPR008242; Chor_mutase/pphenate_deHydtase.
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 PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51671; ACT; 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:UP000017746}.
FT DOMAIN 8..186
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 201..278
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 179
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 318 AA; 33144 MW; 2B1B3359FDFB4A6D CRC64;
MPGTPPTRFV YLGPEGTFTE QALRTISAAE HGIRTPARSV PEALEAVRTG EADAALVPLE
NSVGGAVPVT LDELGTGSPL VITREVVLPV EFVLAAPALV PLAGIRSVAA HPQASAQCRN
WLLANLPDAV VVDVLSNAAA AISAASGEHD AAICAPIGVP RNNLTVLADK IADHADAVTR
FALLSRPAAP APPTGDDITS LAVMIDHDRV GALLSVLTEL AVRGINLSRI ESRPTGEQLG
VYVFFLDCGG HVAEPRLGEA LQGLRRICAE VRFLGSYPRH RWSKAAAAEP APSQPGLTNA
DFADSAAWLT RLRSGEPS
//