ID A0A421GD16_9STRA Unreviewed; 1017 AA.
AC A0A421GD16;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Prephenate dehydratase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BBI17_009263 {ECO:0000313|EMBL:RLN31997.1}, BBO99_00009242
GN {ECO:0000313|EMBL:RLN73803.1}, JM16_009062
GN {ECO:0000313|EMBL:KAG2506869.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN73803.1, ECO:0000313|Proteomes:UP000285624};
RN [1] {ECO:0000313|EMBL:KAG2506869.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2506869.1};
RX PubMed=26981359;
RA Studholme D.J., McDougal R.L., Sambles C., Hansen E., Hardy G., Grant M.,
RA Ganley R.J., Williams N.M.;
RT "Genome sequences of six Phytophthora species associated with forests in
RT New Zealand.";
RL Genom Data 7:54-56(2015).
RN [2] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN31997.1}, and Chile4
RC {ECO:0000313|EMBL:RLN73803.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2506869.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2506869.1};
RA Studholme D.J.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:RLN73803.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPWV03000666; KAG2506869.1; -; Genomic_DNA.
DR EMBL; MAYM02000900; RLN31997.1; -; Genomic_DNA.
DR EMBL; MBDN02000664; RLN73803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421GD16; -.
DR STRING; 325452.A0A421GD16; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR Proteomes; UP000785171; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13631; PBP2_Ct-PDT_like; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR046826; PDH_N.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR InterPro; IPR003099; Prephen_DH.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF02153; PDH_N; 1.
DR Pfam; PF00800; PDT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000285624}.
FT DOMAIN 6..184
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 203..287
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 327..609
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT REGION 570..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 112948 MW; 8A4F3CA2C5917083 CRC64;
MKGEVKVAYQ GMPGAYSEKA TRQLLGSSTN VVAVGYPSFD EAFQAVQRDE ADFGVLPIEN
SLGGSIHANY DLLLKHELHI VGEYDLRVEH SLLALPGVKK EDIKTVISHP QALAQCAYSI
TSMGAQPRAE YDTAGSAKML ADNQWKDTAA VASDLAAEYY GLQVLQRNFE DDAGNFTRFL
LLSKKEEFAL DAKADTEFKT SLVFSFMDSN EKGQLYKALS AFSLRDIDLS KIESRPWGHT
AEQQYQDTLE SSDFSLSAES QTDKDIINAL RHLREFCKFV RVLGSYPTKG KLIGDVKKKL
EAVGAYQANP ITASPAALPQ EHHPVRLNIG IYGFGNFGQF LAKAMAKSHE VRATSRTDYS
TVAAQLGCKY YSSETQLDQF FVGLDVLVLG VSILSFESVL SKIPKHLLEN LVIVDVLSVK
THPKQIMLKD LPESSSILCT HPMFGPESGK YSWRGLPMMF EKVRVVSGEH NHVMDNFLRI
FETELCRMLE MTCESHDEYA ASSQFLTHLT GRILSVQGVQ NTPIDTRGFK NLVRLVEDTC
KDSFDLFQGL YKFNPNSEQQ IQKFRESLDE VTHQLGSKPP NTSTSSSRAD APMAEKYPQN
PLLGKIAASK TVVIHGMAKQ LEAEGKQVWS LCVGEPDFAP AERVLKAGMM SMEQGKVKYT
DVKGTVELRT LIAQYLEICK GVKYDPMTEI LVSNGAKQTV YQALLTVCKP GEQVLIPAPY
WVSYPEMVKL TGGEPVILQT KLSENYLIDP VELEKSLTAN PRVKVMMVCN PSNPAGTVHS
PAQLESIAAI LRKPQFCHIL VIADEIYEQL VYQDEGEPTR LHQSFALLPE MYERTLTVNG
FSKSHAMPGL RIGYLAAPKY FVQVCTKLQG QLTSCASSIG QATAVEAMKF ELECVSQNKQ
RMTETLAIMD AKRKYIVKRL QAMPQVGFAY PTSAFYVFLD MSSYFDGKQG VTADKSEVVK
DADDYCEYLL RHYHVALVPG SAFGIKNGLR ISYACSMETI EHALDGLEQS LASLTFE
//
