ID   A0A1Q7MHQ7_9CREN        Unreviewed;       361 AA.
AC   A0A1Q7MHQ7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUI97_07590 {ECO:0000313|EMBL:OLD12175.1};
OS   Crenarchaeota archaeon 13_1_40CM_3_52_17.
OC   Archaea; Thermoproteota.
OX   NCBI_TaxID=1805096 {ECO:0000313|EMBL:OLD12175.1, ECO:0000313|Proteomes:UP000185971};
RN   [1] {ECO:0000313|EMBL:OLD12175.1, ECO:0000313|Proteomes:UP000185971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLD12175.1}.
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DR   EMBL; MNGN01000053; OLD12175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7MHQ7; -.
DR   STRING; 1805096.AUI97_07590; -.
DR   Proteomes; UP000185971; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProt.
DR   GO; GO:0070403; F:NAD+ binding; 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:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF48600; Chorismate mutase II; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   4: Predicted;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..89
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          99..361
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   361 AA;  39890 MW;  24A72419AF60A8BB CRC64;
     MDEVARIRDR IDELDQEIVR LLKNRHENAK ALGRIKSQRG LDYRDPEREK IILSRIERAA
     TSLDLDPKLI RPIFEQILAL SVQAQQDRPE KSAKRLDQVR ILIVGGTGGM GRFFARFASL
     QGAKVKLAGR EINKTRTAAK EMEVEPGTIL DAASSDIVIL SVPTGETVRV ATETGSLMTT
     GSLLTDLSSV KTGISDRVAE KIPKGVEYMS LHPLFGPGTD HLHGQTIIAV SYRPGQKWSK
     LARAFQGGGS KVVTMSAVQH DRAMAYVQGL HHFALISLGL GLDGMGGEPR TQSLRETESR
     IVSFLSNWDT IVGTQLLNPF VPHVRQKFLE LVGNLAEIRS TQTSGVKKRL TSNVQKWTRK
     L
//