ID A0A240UST4_9GAMM Unreviewed; 301 AA.
AC A0A240UST4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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};
GN ORFNames=B9H00_02555 {ECO:0000313|EMBL:ART64544.1}, C8D96_0622
GN {ECO:0000313|EMBL:RKD87164.1};
OS Kushneria marisflavi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Kushneria.
OX NCBI_TaxID=157779 {ECO:0000313|EMBL:ART64544.1, ECO:0000313|Proteomes:UP000194457};
RN [1] {ECO:0000313|EMBL:ART64544.1, ECO:0000313|Proteomes:UP000194457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW32 {ECO:0000313|EMBL:ART64544.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RKD87164.1, ECO:0000313|Proteomes:UP000285584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15357 {ECO:0000313|EMBL:RKD87164.1,
RC ECO:0000313|Proteomes:UP000285584};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (SEP-2018) 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; CP021358; ART64544.1; -; Genomic_DNA.
DR EMBL; RAPM01000001; RKD87164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240UST4; -.
DR KEGG; kma:B9H00_02555; -.
DR OrthoDB; 9786703at2; -.
DR Proteomes; UP000194457; Chromosome.
DR Proteomes; UP000285584; 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:UniProtKB-KW.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
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; IPR015815; HIBADH-related.
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; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000194457}.
FT DOMAIN 8..163
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 169..288
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 301 AA; 31138 MW; 930E222897294E0E CRC64;
MAHRLRAGVI GLGSMGMGMA SSLIRGGFDT QGCDINAGAL ERLAAEGGRP VANPAEMGRQ
VDIVFLVVVN AAQMREVLLG SHGLASTLSS GSIVVGCATA APDDVIALAA ELKEKGIDYL
DIPISGGAVK SAAGELTLMA SGPSEVFERA QPTLDAIAAT IFRLGEAPGQ GSQVKLVNQL
LAGVHIAAAA EAMAYGIKSG CDPQTLYEVI TKSAGNSWMF ENRVPHILDG DYTPRSAVDI
FVKDLGLVHD TARAGRFPLP MTAQALTMFS QASSMGFGRE DDAGVVRIFP GIDLPTQAAN
D
//
