ID A0A074X982_AURPU Unreviewed; 348 AA.
AC A0A074X982;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN ORFNames=M438DRAFT_326681 {ECO:0000313|EMBL:KEQ80289.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ80289.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ80289.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ80289.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584999; KEQ80289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074X982; -.
DR STRING; 1043002.A0A074X982; -.
DR HOGENOM; CLU_035008_5_1_1; -.
DR OrthoDB; 2783975at2759; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000030706; 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; 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; 2.
DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 2.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT DOMAIN 6..234
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 264..341
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 107..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 37746 MW; 9A6F1AD6D71E6836 CRC64;
MQSHEQIAYL GPKASYTHQA TLSAFDSDNY TFSPQTTIED VFYQVQAGKA AYGVVPFENS
TNGSVVFTLD LFADQSAKHP DIVVCGERYV EVHHCLLGHP AISGQGHATG PAKVLQEETK
SPSSSGHATP IPGNPNPTNS RAAPLTSLSH IKKLYSHPQA WGQCKTFLSC YLKGVERQDV
SSTSRAAELV AADDTHTSAA ISSGIAAQMT GLDFLARDIE DEKDNATRFF IIRRRSLEDT
SPSSVTTGKD ADNQQNARAF KSLLSFTVSH TDAGALANAL AVFGSHGINL TSINPRPSGE
APWHYMFFVE FSGKRGQLAV DDTLSGLDKV VRSWRWLGSW ENALQQKQ
//
