ID   A0A1D6LWQ2_MAIZE        Unreviewed;       976 AA.
AC   A0A1D6LWQ2;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE            EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN   ORFNames=ZEAMMB73_Zm00001d037333 {ECO:0000313|EMBL:AQK83648.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK83648.1};
RN   [1] {ECO:0000313|EMBL:AQK83648.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK83648.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes oxidation of L-threonate to 2-oxo-tetronate. Can
CC       use either NAD(+) or NADP(+) as cosubstrate, with a preference for
CC       NAD(+). {ECO:0000256|ARBA:ARBA00037062}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH;
CC         Xref=Rhea:RHEA:52548, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57561, ChEBI:CHEBI:57945, ChEBI:CHEBI:136669;
CC         EC=1.1.1.411; Evidence={ECO:0000256|ARBA:ARBA00036958};
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. L-threonate
CC       dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00037979}.
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DR   EMBL; CM000782; AQK83648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6LWQ2; -.
DR   ExpressionAtlas; A0A1D6LWQ2; baseline and differential.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.40.50.10840; Putative sugar-binding, N-terminal domain; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR010737; 4-carb_acid_sugar_kinase_N.
DR   InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR   Pfam; PF14833; NAD_binding_11; 2.
DR   Pfam; PF03446; NAD_binding_2; 2.
DR   Pfam; PF07005; SBD_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF142764; YgbK-like; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}.
FT   DOMAIN          8..164
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          179..284
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   DOMAIN          328..486
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          493..613
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   DOMAIN          661..898
FT                   /note="Four-carbon acid sugar kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07005"
SQ   SEQUENCE   976 AA;  104936 MW;  D8FBC7E0A7410F0B CRC64;
     MSLTAAPVAF IGLDELSVEL AASFLRSGAC VRSFTPEAER SPSAALAELN GLLQCASPVE
     AARDAALVVV LSDAGGVDEL FFGVEGIAKG LCAGSIVLIH STLLPSQLEK LEQELTDQKK
     DVFLLDGYIF TGLSDELKQQ IIIVASGRQD IAEKASKFFH GLYKTIYFAE GEFCTSRKIR
     MVNDLLEGIH FVASIEAMYL GVRAGIHPTI IYDIISNAAG SSRIFVELVP KLLSEDPLLI
     DFLKSTRKKA SHVMDMSKSV TFPLPLLGVA YQQLVHGSSA VTGDGSASPL KVWEASFGVN
     IVDAAGEQIY DASKLADQLV AESKAAKRIG FIGLGAMGFG MASHLLKSGF CVVAYDVYKP
     TMARFADLGG STKGSPEEIA KDVEILIIMV ANESQADSVL FGNAGAVPVL SAGTSVILSS
     TVSPGFVIHL NRRLEAECRQ IKLVDAPVSG GVKRAADGTL TIMTSGTDEA LHCTGSVLSA
     LSEKLYVIKG GCGAASSVKM VNQLLAGVHI ASAAEAMSFA ARLNLRTRRV FEIMQHARGY
     SWMFGNRVPH MLDNDYTPYS AVDIFVKDLG IVSCESSNSR IPVHVSSIAH QLFISGSASG
     WGRYDDAAVV KVYETLTGVK VEGKAPMLSK EDVLQSLPSE WPEDPIDNLV PIASHSSKKF
     LVVLDDDPTG TQTVHDIEVL TEWPVEALVE QFLKLPTCFF ILTNSRSMTA DKAMLLVQTI
     CKNLKAAAEK VPGVSYTIVL RGDSTLRGHF PEEADAAVSV LGEMDAWIIC PFFLQGGRYT
     INDIHYVADS DRLIPAGETE FAKDAVFGYK SSNLRQWVEE KTKGRVLENQ VSTISITLLR
     KQGPTAVCEH LCSLEKGSVC IVNAASDRDM AVFASGMIQA ELKGKRFLCR TAASFVSARI
     GIKPKPPICP NDLGLKRALT GGLIIVGSYV PKTTKQVDEL RSQFGQSLRV IEGWAWVPLD
     LPEHPLMGLA IPNCSI
//