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Database: UniProt
Entry: A0A177INA0_9CORY
LinkDB: A0A177INA0_9CORY
Original site: A0A177INA0_9CORY 
ID   A0A177INA0_9CORY        Unreviewed;       304 AA.
AC   A0A177INA0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN   ORFNames=AYJ05_06025 {ECO:0000313|EMBL:OAH30308.1};
OS   Corynebacterium stationis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1705 {ECO:0000313|EMBL:OAH30308.1, ECO:0000313|Proteomes:UP000076947};
RN   [1] {ECO:0000313|Proteomes:UP000076947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA-15 {ECO:0000313|Proteomes:UP000076947};
RA   Kaur G., Nair G.R., Mayilraj S.;
RL   Submitted (FEB-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAH30308.1}.
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DR   EMBL; LSTQ01000008; OAH30308.1; -; Genomic_DNA.
DR   RefSeq; WP_066838387.1; NZ_LSTQ01000008.1.
DR   AlphaFoldDB; A0A177INA0; -.
DR   STRING; 1705.CA21670_11625; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000076947; Unassembled WGS sequence.
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:UP000076947}.
FT   DOMAIN          4..185
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          199..274
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            178
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   304 AA;  32841 MW;  62068A56F3887670 CRC64;
     MTSTVAFLGP AGTFTEAALV AFEKAGAVSD VQQLPVNSPS EAFQAVREGR ADFACVAIEN
     SVDGAVTTTF DAFTEGDALQ VYQEVDLEVA FAIMVKKGLS LDDVHTIATH PVAYQQVRGW
     LTENIPDAKF QPASSNGAAA EAVSRGEVDA AAAPERAAEI FGLDVLANSV ADVKGATTRF
     VLVGKPGRPT ERTGNDRTSV VFTVPHEPGS LASILQEFSY RNVDMLRIES RPTRKKFGTY
     NFFIDLAGHI EDEPLSEALR ALWLRTENLR FIGSWPAADQ SGPKLDTTEF DKATAWVEKV
     REGR
//
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