ID A0A2X4X9K0_9NOCA Unreviewed; 308 AA.
AC A0A2X4X9K0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ECO:0000313|EMBL:SQI33254.1};
GN ORFNames=NCTC10994_02501 {ECO:0000313|EMBL:SQI33254.1};
OS Rhodococcus coprophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI33254.1, ECO:0000313|Proteomes:UP000249091};
RN [1] {ECO:0000313|EMBL:SQI33254.1, ECO:0000313|Proteomes:UP000249091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI33254.1,
RC ECO:0000313|Proteomes:UP000249091};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; LS483468; SQI33254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X4X9K0; -.
DR STRING; 1219011.GCA_001895045_02711; -.
DR KEGG; rcr:NCTC10994_02501; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000249091; Chromosome 1.
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:UP000249091}.
FT DOMAIN 9..191
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 205..279
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 184
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 308 AA; 32602 MW; D3F63D8519F36426 CRC64;
MRNLVGVPRI AYFGPSGTFT EMALDRFENL GAFDAPVERV VAASPPAALE LLRNGEVDGA
VVPIESSVEG SVPPTMDALS LGARLQIVAE TELDIAFTVV TRPGVAPEDV ATVGAYPVAA
AQVRKWIADN LPAAEIVTAS SNAGAAEDVA SGKVDAGVAT ALAGQRLGLA VLADGVADFA
GARTRFVLVT RPGPIPERTG CDRTSVILQL PNVPGSLVRA MTELATRGID LTRIESRPTR
KDYGTYFFHL DWVGHIDDPL VAEALKALHR FAQVRFLGSW AAVSEHGVPP VSDDDDAQWL
ERLRCGEE
//
