ID S8DEJ4_9LAMI Unreviewed; 320 AA.
AC S8DEJ4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Hydroxyphenylpyruvate reductase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=M569_13592 {ECO:0000313|EMBL:EPS61208.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS61208.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS61208.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:EPS61208.1}.
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DR EMBL; AUSU01007010; EPS61208.1; -; Genomic_DNA.
DR AlphaFoldDB; S8DEJ4; -.
DR OrthoDB; 1327616at2759; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12156; HPPR; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453}.
FT DOMAIN 15..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPS61208.1"
SQ SEQUENCE 320 AA; 34662 MW; 3476C453DA321C84 CRC64;
HLRITAGMEK IGVLMMAPFN SYLEQELDKR FNLFRYWSRN PNELLAQHSE KIRAAVVNAG
IGVDAELIHA LPKLEIISSF SVGLDKIDLK TCEGKGIRVT NTPDVLTDDV ADLAIGLALS
VMRKLCACDR FVRSGAWKNG QFELATKFSG KRVGIIGLGR IGSAIAKRAE AFDCQINYYS
RSEKQIAVNY KYFSSVTDLA SNSDVLVVAC ALTPETTHIV NREVIEALGP DGVLINIARG
GHVDEAELVS ALVEGRLGGA GLDVFENEPD APEQLLGLDN VVLLSHVGSG TVETRKDMAD
LVLGNLQAYF SGHPLLTPVV
//
