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Database: UniProt
Entry: M5XZ14_PRUPE
LinkDB: M5XZ14_PRUPE
Original site: M5XZ14_PRUPE 
ID   M5XZ14_PRUPE            Unreviewed;       374 AA.
AC   M5XZ14;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PRUPE_1G556800 {ECO:0000313|EMBL:ONI35844.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI35844.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI35844.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CM007651; ONI35844.1; -; Genomic_DNA.
DR   RefSeq; XP_007223301.1; XM_007223239.1.
DR   AlphaFoldDB; M5XZ14; -.
DR   EnsemblPlants; ONI35844; ONI35844; PRUPE_1G556800.
DR   GeneID; 18789385; -.
DR   Gramene; ONI35844; ONI35844; PRUPE_1G556800.
DR   KEGG; pper:18789385; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   HOGENOM; CLU_019796_1_3_1; -.
DR   OMA; MRIACYG; -.
DR   OrthoDB; 6392at2759; -.
DR   Proteomes; UP000006882; Chromosome g1.
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; 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:UP000006882}.
FT   DOMAIN          57..366
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          153..340
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   374 AA;  41222 MW;  CE5D35310A1E3A49 CRC64;
     MVLRSRLLAK AISRTSTYHR LMSCSANILG KVERMVDNDE KKITRVLFCG PHFPASHTYT
     REYLKEYPFV QVDDVPLDDV PGVIQNYNIC IVKTMKFDSI LLSHAEKMKL IMQYGVGLEG
     VDIDSATEFG IKVARIPSHV TGNAASCAEM AIYLMLGLLR KQNEMQIAIK QRKVGDPIGD
     MLLGKTVFIL GFGNIGIDLA KRLRPFGVKI IATKRSWATH SLVSCLSNVQ NGPVNDFVDE
     KGGHEDIHKF ASKADIVVCC LCLNSDTVGV VNKPFISSMR KGSLLVNIAR GGLLDYEAVS
     YYLESGHLGG LGIDVAWTEP FDPDDPILKF SNVLITPHVA GVTEYSYRSM SKVVGDVAIQ
     LHEGRPLTGI EFVN
//
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