ID U3BGD9_VIBPR Unreviewed; 298 AA.
AC U3BGD9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=VPR01S_19_00260 {ECO:0000313|EMBL:GAD68744.1};
OS Vibrio proteolyticus NBRC 13287.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD68744.1, ECO:0000313|Proteomes:UP000016570};
RN [1] {ECO:0000313|EMBL:GAD68744.1, ECO:0000313|Proteomes:UP000016570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD68744.1,
RC ECO:0000313|Proteomes:UP000016570};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL Submitted (SEP-2013) 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}.
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:GAD68744.1}.
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DR EMBL; BATJ01000019; GAD68744.1; -; Genomic_DNA.
DR RefSeq; WP_021706712.1; NZ_BATJ01000019.1.
DR AlphaFoldDB; U3BGD9; -.
DR STRING; 1219065.VPR01S_19_00260; -.
DR eggNOG; COG2084; Bacteria.
DR Proteomes; UP000016570; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000016570}.
FT DOMAIN 7..165
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 298 AA; 30726 MW; 362BB4C57857ABBD CRC64;
MHKVQSVAVI GLGSMGMGVA QSCLRASFDV YGVDVNPQAL ETLATSGATA TATSATAFAQ
DLDAVIVLVV NAQQVRSVLF ESGLAAALKP STPIMVCATI SAEDARSIAA DLADYSLPML
DAPISGGAVK ATAGELTVMA AGAPSVFEQL ESVLSAVASQ VYTVGTEIGM GSTVKIIHQL
LAGVHIAAGA EAMAMAARAN IPLDLMYDVV THAAGNSWMF ENRMKHVVDG DYTPKSMVDI
FVKDLGLVTD TAKSLHFPLP LASTALNMFT TASNAGHGKE DDSAVIKIFP GITLPTKE
//
