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Database: UniProt
Entry: A0A0L9T6T1_PHAAN
LinkDB: A0A0L9T6T1_PHAAN
Original site: A0A0L9T6T1_PHAAN 
ID   A0A0L9T6T1_PHAAN        Unreviewed;       251 AA.
AC   A0A0L9T6T1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LR48_Vigan247s000600 {ECO:0000313|EMBL:KOM26288.1};
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM26288.1, ECO:0000313|Proteomes:UP000053144};
RN   [1] {ECO:0000313|Proteomes:UP000053144}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX   PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA   Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA   Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA   Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA   Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT   "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT   high starch and low fat accumulation and domestication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; KQ258312; KOM26288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L9T6T1; -.
DR   STRING; 3914.A0A0L9T6T1; -.
DR   EnsemblPlants; KOM26288; KOM26288; LR48_Vigan247s000600.
DR   Gramene; KOM26288; KOM26288; LR48_Vigan247s000600.
DR   OMA; CTEMAIY; -.
DR   Proteomes; UP000053144; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT   DOMAIN          29..241
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          157..217
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   251 AA;  27474 MW;  E0E7789D536A4A7C CRC64;
     MESNGNLVKH VEKQTTRVLF CGPHFPASHE YTAEYLQNHP STKVDVLSFE DVRKDIANYN
     VCIVKSIRLD SDIISCTAQM QLIMQYGVGL EGVDIDAATK HGIKVARIPS DVTGNSTSCT
     EMAIYLMLGL LRKHNELQVS IQQKKLGELI TETLFGKTGA LLVNIARGGI VDYEAVINNL
     ESGHLGGLGT DVAWTEPFNP DDQIFKFKNV IMTPHVAGVT EHSYRSMAKA VGEVVLQLHA
     GLPLTGIELV N
//
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