ID V2X697_MONRO Unreviewed; 490 AA.
AC V2X697;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 10-JUN-2026, entry version 39.
DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:ESK89302.1};
GN ORFNames=Moror_1240 {ECO:0000313|EMBL:ESK89302.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK89302.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK89302.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89302.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK89302.1}.
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DR EMBL; AWSO01000570; ESK89302.1; -; Genomic_DNA.
DR AlphaFoldDB; V2X697; -.
DR STRING; 1381753.V2X697; -.
DR KEGG; mrr:Moror_1240; -.
DR HOGENOM; CLU_031403_1_0_1; -.
DR OrthoDB; 5399569at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:TreeGrafter.
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:0006571; P:L-tyrosine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR050812; Preph/Arog_dehydrog.
DR InterPro; IPR003099; Prephen_DH.
DR InterPro; IPR012385; Prephenate_DH_fun.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF27505; 6PGD_Tyr1_C; 1.
DR PIRSF; PIRSF036510; PDH_fung; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 19..302
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 490 AA; 54903 MW; AD66EE98506024A5 CRC64;
MDQPSPPVVS PKDDAEKQPT LGLIGMGAMG KMYANLLSKA AWKKIHVCDL PEKYESLKNQ
FADVPGVNVM KDGHAVARSA DFMIYSVEAE FIDRVVAEYG PSTKLNAIVA GQTSVKAPEK
DAFEKYLPPD TQIISCHSLH GPTVSPLGQP LVLIKHRGTD HALHVVEDIL RSFGSRYVYL
SYEEHDLVTA NTQAVTHAAF LSMGAAWACE QSYPWEHGLY VGGMETVKVN LTLRIYSNAW
HVYAGLAILN PKAREQINQY ATSATELYKL MVVAGTGRSG NGDAERERKL RQRVDWARET
VFGDSPKNRN PILLSQDILD RFSLGQLPVN NGKDNGGDSA SRYRPNSHLS LLAMVDCWAH
LGIKPFDHLQ LAATPLFRLF LGVAEHLFLS PLLLDSAIHS AIYDTWHRSN DLEFVLAARG
WSQCVNYGSF EVYRKRFDET RSFFESRFEE AGVLGSKMIK AVMESELKRE ESQETQRRLR
PAELHTLFHR
//
