ID D5KSA2_PSEAI Unreviewed; 300 AA.
AC D5KSA2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=P072206A_0005 {ECO:0000313|EMBL:ADF47456.1};
OS Pseudomonas aeruginosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287 {ECO:0000313|EMBL:ADF47456.1};
RN [1] {ECO:0000313|EMBL:ADF47456.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P072206 {ECO:0000313|EMBL:ADF47456.1};
RX PubMed=20566763; DOI=10.1128/AAC.00110-10;
RA Uemura S., Yokota S., Mizuno H., Sakawaki E., Sawamoto K., Maekawa K.,
RA Tanno K., Mori K., Asai Y., Fujii N.;
RT "Acquisition of a transposon encoding extended-spectrum beta-lactamase SHV-
RT 12 by Pseudomonas aeruginosa isolates during the clinical course of a burn
RT patient.";
RL Antimicrob. Agents Chemother. 54:3956-3959(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU592828; ADF47456.1; -; Genomic_DNA.
DR RefSeq; WP_002903955.1; NZ_JAGEYJ010000096.1.
DR AlphaFoldDB; D5KSA2; -.
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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 7..166
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 170..289
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 176
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 300 AA; 30507 MW; C06314613C588020 CRC64;
MAAHTNVCVI GLGSMGMGAA RACLQAGLNT WGVDINPDNC RALLAAGAKG AGPSAVPFAA
ELDAVVLLVV NAAQVRGILF GESGLAAHLK PGTVVMVSST IASADAQAIA EALAEYQLLM
LDAPVSGGAV KAAAGDMTVM ASGSDAAFAR LAPVLDAVAG KVYRIGSDIG LGSTVKIIHQ
LLAGVHIAVA AEAMALAARA GIPLETMYDV VTHAAGNSWM FENRMQHVLD GDYSPKSAVD
IFVKDLGLVN DTARALTFPL PLATTALNMF TSASNAGFGR EDDSAVIKIF NGITLPGHKQ
//
