ID R9P2I2_PSEHS Unreviewed; 1047 AA.
AC R9P2I2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Prephenate dehydratase domain-containing protein {ECO:0000259|PROSITE:PS51171};
GN ORFNames=PHSY_002988 {ECO:0000313|EMBL:GAC95412.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC95412.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; DF238795; GAC95412.1; -; Genomic_DNA.
DR RefSeq; XP_012188999.1; XM_012333609.1.
DR AlphaFoldDB; R9P2I2; -.
DR STRING; 1305764.R9P2I2; -.
DR GeneID; 24108278; -.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_316196_0_0_1; -.
DR OrthoDB; 2783975at2759; -.
DR Proteomes; UP000014071; Unassembled WGS sequence.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd13532; PBP2_PDT_like; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR028245; PIL1/LSP1.
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 Pfam; PF13805; Pil1; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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 Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW Reference proteome {ECO:0000313|Proteomes:UP000014071}.
FT DOMAIN 534..773
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT REGION 49..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 110519 MW; 2DD5E512DBE29E72 CRC64;
MIHAARSPIH LDCAHTIEPL LPSHFHHTST SGHSRARIMA SFFQKARERA EAAAQQLQAH
HAASSTSKTG DASASGDPAA PNSASASGFT YTGSVPHLFR QGLASVDPRY ESTRQFHLLN
QAVKSFNIDH EAAGREAKAL AKATFVWGQH HLPEKREDGV GDEMLVDVAD RLAFVWHEIG
QLETAHSQRS EQARSRLKRF EKAEMELGQR RANRSKLKKE LHALVPERAI AAGSERIQNT
EKRLQDLLND DQADEEYLSR TKRESVKEGY AAMFDSLIEL GEKMALAARY GKLLTTLVPT
DKSPFPATVK HRGDTIPLWE SASRTAEVRA ALASALTSFR PDLSLPSLPS DSAFSATGSL
GRADTVTYAS SHKSELQNDQ ATTASAAAAP LAEPPSPRRS SGSSDRGDLL QSGLAASQNS
GSGSTQKLNL SPTALPAPLL PPRPQRGSSS TASDTLRSAT ANPFADSAAA SAATSVPGST
APQDEEHLPP PGPPGPTVAE TGVIPTGPGG PKSGTLRPRR SSVSQRSASI SAGAVAYLGP
TGTYSHQAAL KVFGEAGTNL IPMQSITGAI DFVRRGTPGN AKIAIVPVEN STFGPVRDTL
DNLLGISNGD RHAFRPEDGA QLHVVGEACL SVDHALLCGP KTYHHLLQLQ GDTDPNAPIR
DDTLSNITNV ISHEQALGQC SHYLTRYLPQ AKKKAVESTA AAAVTALEFE AGTAPGRSST
SIDHAHESLG FSSNSLVAAV GAEAAVSAIG VRVLRSRIQD VKDNRTRFLV LASEPLAALL
SVNALPAAMS RLYHASSVAG TTGRSLLSVR DALASDLAAE AGSYGSDSAS VLDKLMVQLS
QLGSVAVRKV DRRPASIGEA SSDGSSSVWR SSYLLELQYP GASASIAEAK IRQLIADLTH
SAATAAGGSA PVHYLGSWIV DAITLRGQPT VSVSGQTPQR STVTGSSSSS FSPSTLGASS
QMTERERKET EARQEADEVQ RHAAQARFNR QQQQAELYGV GVQPSGSSAA GSRVQPMAGL
EESEAEPRLD EEENLPVYQP LDPASRS
//
