ID W0TF75_KLUMD Unreviewed; 311 AA.
AC W0TF75;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN Name=PHA2 {ECO:0000313|EMBL:BAO42010.1};
GN ORFNames=KLMA_70162 {ECO:0000313|EMBL:BAO42010.1};
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335 {ECO:0000313|EMBL:BAO42010.1, ECO:0000313|Proteomes:UP000065495};
RN [1] {ECO:0000313|EMBL:BAO42010.1, ECO:0000313|Proteomes:UP000065495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275
RC {ECO:0000313|Proteomes:UP000065495};
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi, Tsuchikane K., Limtong S.,
RA Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
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; AP012219; BAO42010.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TF75; -.
DR VEuPathDB; FungiDB:KLMA_70162; -.
DR OrthoDB; 2783975at2759; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000065495; Chromosome 7.
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; cd13532; PBP2_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 PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 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; 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}.
FT DOMAIN 3..197
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 221..304
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 311 AA; 35749 MW; 898188B74B95FD98 CRC64;
MVKVLYLGPA GTYSHQAVLQ QFADEELIPT NSIPSCFKTL IEDEDIDYGV VPLENSTNGQ
VVFTYDLFRD FMQSEEEPKL EVVGEQYVDI AHCLIAPAPL EVDKLRKIGT IYSHPQVWGQ
VKDYLADLEK KYGKFTKIDC NSTSEAVTKC IQEWDSKERI TLAIGSRASA KLNKGFIVDS
GINDIKGNTT RFLILRRRKP NNRLVTDCLP PNTDSKKVNL VTFVTKQDDP GSLVDVLNVL
KDQRLNMCSI SSRPFHADSL AGRKWQYCFF IEFYHSETTD YELLMEKFDE YCAKWIHWGR
FYRNPSYYQV S
//