ID A0A1L7D5J2_9CORY Unreviewed; 297 AA.
AC A0A1L7D5J2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN ORFNames=CPHO_11645 {ECO:0000313|EMBL:APT93436.1};
OS Corynebacterium phocae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161895 {ECO:0000313|EMBL:APT93436.1, ECO:0000313|Proteomes:UP000185491};
RN [1] {ECO:0000313|EMBL:APT93436.1, ECO:0000313|Proteomes:UP000185491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M408/89/1 {ECO:0000313|EMBL:APT93436.1,
RC ECO:0000313|Proteomes:UP000185491};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT 44612(T)), isolated from the common seal (Phoca vitulina).";
RL Submitted (AUG-2014) 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 -!- 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; CP009249; APT93436.1; -; Genomic_DNA.
DR RefSeq; WP_075736023.1; NZ_VXKJ01000049.1.
DR AlphaFoldDB; A0A1L7D5J2; -.
DR STRING; 161895.CPHO_11645; -.
DR KEGG; cpho:CPHO_11645; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000185491; Chromosome.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
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 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; PS00857; PREPHENATE_DEHYDR_1; 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:UP000185491}.
FT DOMAIN 4..179
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 193..274
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 172
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 297 AA; 31800 MW; 889C970A0CB9DDCF CRC64;
MSLTVAYLGP AGTFTEAALH QFELGEVAGI PVSSPGEALD LVRSGKADRA VVAVENSVDG
AVTATFDALV AGKRVQIYQE TSLEVAFAIM SAPGMTGPQT ITTHPVAYQQ IRKWVEHNLP
GVSFMPATSN AAAAQMVAEG KADLAAAPAH AAEIYGLDIL HNQVADVAGA TTRFILVGPP
GKPTPRTGSD VTSVVFTLPN EPGTLVDSLQ EFAYRGVDMA RIESRPTRTE MGTYRFYVDI
DGHLDDPPVA EALRALYLRA KELIFVGSWP VEGRTTRHDE QKLRAANTWV ARMREGQ
//
