ID A0A256Y008_9ARCH Unreviewed; 564 AA.
AC A0A256Y008;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN ORFNames=B6U87_02955 {ECO:0000313|EMBL:OYT33775.1};
OS Candidatus Aenigmarchaeota archaeon ex4484_52.
OC Archaea; Candidatus Aenigmarchaeota.
OX NCBI_TaxID=2012504 {ECO:0000313|EMBL:OYT33775.1, ECO:0000313|Proteomes:UP000216807};
RN [1] {ECO:0000313|Proteomes:UP000216807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K.W., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001162};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005067}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007964}.
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:OYT33775.1}.
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DR EMBL; NJDR01000044; OYT33775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256Y008; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000216807; 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:UniProtKB-EC.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13630; PBP2_PDT_1; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 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 InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
DR InterPro; IPR046826; PDH_N.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR003099; Prephen_DH.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF20463; PDH_C; 1.
DR Pfam; PF02153; PDH_N; 1.
DR Pfam; PF00800; PDT; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 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 PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 8..270
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 301..474
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 488..564
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 564 AA; 64630 MW; 95CB06CB06BAD2F4 CRC64;
MIFNMEKTII GIIGGTNGLG NWFKYFFEKN KYKLIISGRK TRLTNIDLAK KSDIVIVAVP
IHSTIDVIAE ILPYLKDNAL LMDITSLKIN PINEMKKAKK TIGIVGLHPL FGPLITSIEN
QYIAVNEIRE NKLWKKIKKL FLENKAQLIY IDSKEHDRKM ALMQALLHFM NLCYTKTLFN
NNLNIEGKFS TPVFRLQSII IGRILGQNPY LYADLQMQNP MFDEILNSFV NVINKNKKII
ETKNKKKFVE EFNDLKNQMQ NFIKTSEIKT SSILDDMEKT KEQISFSFQK TPKTTSEIIE
KIGYLGPSGT HTHFAATKIF KNKSLLPVNT IGEIFEKIAN HQLDSAIIPA ENSTNGIVYE
TYDNLVNTNI CVLTSFRQII HHNLIARCKN INSIKKIVSH PQAIAQTRIW LKQKIPSAKI
IFTSSTTNAI QKYKDKSVAF IGSKIAAKEY NLNILKENIE NSKNNTTEFY AIAEDGTPAE
YFTQTKTLMA VTIYNRVGVL KDFLSVFSKY SINLTKLFSR PSQVKQWDYY FFIEAQIKPN
NKIINKIQEE LKKYCPLVKI LGGT
//
