ID   A0A1F7ZP72_9EURO        Unreviewed;       445 AA.
AC   A0A1F7ZP72;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE            EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
DE   Flags: Fragment;
GN   ORFNames=ABOM_010319 {ECO:0000313|EMBL:OGM40928.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM40928.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM40928.1, ECO:0000313|Proteomes:UP000179179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX   PubMed=27664179;
RA   Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT   "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT   bombycis.";
RL   Genome Biol. Evol. 0:0-0(2016).
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}.
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:OGM40928.1}.
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DR   EMBL; LYCR01000126; OGM40928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7ZP72; -.
DR   STRING; 109264.A0A1F7ZP72; -.
DR   OrthoDB; 1121581at2759; -.
DR   Proteomes; UP000179179; Unassembled WGS sequence.
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; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
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; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT   DOMAIN          14..170
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          182..302
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   DOMAIN          323..441
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OGM40928.1"
SQ   SEQUENCE   445 AA;  46806 MW;  951026275D672062 CRC64;
     NIYLSLTVIM SKPTIGFVGL GAMGFGMATH LVHEGYPVHG FDVFPASVQR FQAVGGIPAA
     SLRESAEGKS FYVCMVASAP QVQSVLFADE GIVQYLPQNA TLLLCSTVPA SYAQSVAAEL
     QSRGRGDILF IDSPVSGGAK RAADGTLSIM AGGTDEALES GRDLLQTMSA PSKLYLVPGG
     IGAGSNMKMV HQVLAAIHIL GASEAMGLAA QLGLDARETA DKIIGSDAWT WMHENRFPRM
     VEEDWNPGAS ALTIILKDAG IITTSARQHR FPIPLCTAAE QIYISALLQG YGPKDDSAMV
     RQYFPTPIAS VTASAEDKSA ALQLVLDLMQ GVNLVAAAEA VAFARYLKVD LAQFHELVSA
     AAGASKMFMT KGLEMIKGQI GKEAPAGSQT VDEAITRLEA VVQQARDLHC PLHLGNAALN
     VLFTARRAGL GAEGATSVIK VFGTE
//