ID A0A0T6AL39_9BACT Unreviewed; 267 AA.
AC A0A0T6AL39;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Prephenate dehydrogenase, prephenate dehydrogenase {ECO:0000313|EMBL:KRT75803.1};
DE EC=1.3.1.12 {ECO:0000313|EMBL:KRT75803.1};
GN ORFNames=XU14_C0095G0006 {ECO:0000313|EMBL:KRT75803.1};
OS Armatimonadetes bacterium CSP1-3.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=1640515 {ECO:0000313|EMBL:KRT75803.1, ECO:0000313|Proteomes:UP000051026};
RN [1] {ECO:0000313|EMBL:KRT75803.1, ECO:0000313|Proteomes:UP000051026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-3 {ECO:0000313|EMBL:KRT75803.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT75803.1}.
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; LDXQ01000095; KRT75803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AL39; -.
DR Proteomes; UP000051026; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; 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:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
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 InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
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; PF20463; PDH_C; 1.
DR Pfam; PF02153; PDH_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
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 ECO:0000313|EMBL:KRT75803.1}.
FT DOMAIN 7..267
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 267 AA; 28446 MW; 9720933226B50942 CRC64;
MTVPAAGRIA IVGLGLIGGS LGMRIRELGL ARVIGVDNDY AVTKRAEERG AADETHLELE
RVRDAEVIII AVPPEQTVNV AREAAGFAAE GAVLTDVTSV KAPIVAQLAG LERVRYVGGH
PMFGTEGRGI DAAGADLPAG HPYIFTPVAS TPTDAVNTML MLAQDLGMRP VLLTPDEHDR
VVAEVSHLPY LLALLLSYGT DPPARDVAGP AFRDATRVAA TPPDLMVEIL RLNRVHVLAA
VDHFSRGLVQ MREALARGHI KQAVRFR
//