ID U5DCW7_AMBTC Unreviewed; 373 AA.
AC U5DCW7;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=S-adenosyl-L-homocysteine hydrolase NAD binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMTR_s00071p00183090 {ECO:0000313|EMBL:ERN20040.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN20040.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; KI392062; ERN20040.1; -; Genomic_DNA.
DR AlphaFoldDB; U5DCW7; -.
DR STRING; 13333.U5DCW7; -.
DR EnsemblPlants; ERN20040; ERN20040; AMTR_s00071p00183090.
DR Gramene; ERN20040; ERN20040; AMTR_s00071p00183090.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_3_1; -.
DR OMA; MRIACYG; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central.
DR CDD; cd12175; 2-Hacid_dh_11; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42938:SF25; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT DOMAIN 52..367
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 149..339
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 373 AA; 40999 MW; 73FA7557030079F6 CRC64;
MLPFFLFKKP SIVLNYLLSP LSSRSNTVKK VGKMEGNAIT KILFCSSHFP SAHEYTRECL
QKYPFIQVDD VDIDDVPNVI GDYHICIPRM MRLDSEVISR AKQMKLIMQY GVGLEGVDID
AATMAGIRVA RIPSNMTGNS FSCAEHAIYL VLGLLRKQKE MEIAVQERKL GWPAGETLFG
KTVFILGYGN IGVDLAARLK PFGVKILATK RSWSSVSQDS RTHDGLDRNG KFNNGVVGKK
GDMGSIYDFA GEADIVFACI NLNKDTAGIV NHKFLTSMRK GALLVNVARG GVLDYQAVKY
HLESGHLGGL AIDVAWTEPF DPEDPILKFP NVLITPHIAG VTEYSYRKMA KIVAESALQV
HSGAPLTGIE CVN
//
