ID A0A248KG61_9ENTR Unreviewed; 296 AA.
AC A0A248KG61;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0000256|HAMAP-Rule:MF_02032};
DE EC=1.1.1.60 {ECO:0000256|HAMAP-Rule:MF_02032};
DE AltName: Full=Tartronate semialdehyde reductase {ECO:0000256|HAMAP-Rule:MF_02032};
DE Short=TSAR {ECO:0000256|HAMAP-Rule:MF_02032};
GN Name=garR {ECO:0000256|HAMAP-Rule:MF_02032};
GN ORFNames=CEW81_03210 {ECO:0000313|EMBL:ASG62678.1};
OS Kluyvera genomosp. 3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kluyvera.
OX NCBI_TaxID=2774055 {ECO:0000313|EMBL:ASG62678.1, ECO:0000313|Proteomes:UP000197098};
RN [1] {ECO:0000313|EMBL:ASG62678.1, ECO:0000313|Proteomes:UP000197098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YDC799 {ECO:0000313|EMBL:ASG62678.1,
RC ECO:0000313|Proteomes:UP000197098};
RA Ito R., Pacey M.P., Doi Y.;
RT "Origin of plasmid-mediated fosfomycin resistance gene fosA3.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of tatronate semialdehyde to D-
CC glycerate. {ECO:0000256|HAMAP-Rule:MF_02032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NAD(+) = 2-hydroxy-3-oxopropanoate + H(+) +
CC NADH; Xref=Rhea:RHEA:18845, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57978; EC=1.1.1.60;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 2-hydroxy-3-oxopropanoate + H(+) +
CC NADPH; Xref=Rhea:RHEA:18841, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57978, ChEBI:CHEBI:58349; EC=1.1.1.60;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02032};
CC -!- PATHWAY: Carbohydrate acid metabolism; galactarate degradation; D-
CC glycerate from galactarate: step 3/3. {ECO:0000256|HAMAP-
CC Rule:MF_02032}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 2-hydroxy-3-
CC oxopropionate reductase subfamily. {ECO:0000256|HAMAP-Rule:MF_02032}.
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DR EMBL; CP022114; ASG62678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248KG61; -.
DR KEGG; kgo:CEW81_03210; -.
DR UniPathway; UPA00565; UER00631.
DR Proteomes; UP000197098; Chromosome.
DR GO; GO:0008679; F:2-hydroxy-3-oxopropionate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046392; P:galactarate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046487; P:glyoxylate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_02032; Tartronate_sem_reduc; 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 InterPro; IPR006398; Tartro_sem_red.
DR NCBIfam; TIGR01505; tartro_sem_red; 1.
DR PANTHER; PTHR43060:SF3; 2-HYDROXY-3-OXOPROPIONATE REDUCTASE; 1.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 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 NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_02032};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02032}; Reference proteome {ECO:0000313|Proteomes:UP000197098}.
FT DOMAIN 4..163
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 166..283
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 172
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02032,
FT ECO:0000256|PIRSR:PIRSR000103-1"
FT BINDING 6..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02032"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02032"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02032"
SQ SEQUENCE 296 AA; 30720 MW; CB68C604760597BB CRC64;
MTMKVGFIGL GIMGKPMSKN LLKAGYSLVV ADRNSETIAE VIAAGAETAT TPKAIAEQCD
VIITMLPNSP HVKEVALGEN GIIEGAKPGT VLIDMSSIAP LASREISDAL KAKGIDMLDA
PVSGGEPKAI DGTLSVMVGG DKAIFDKYYD LMKAMAGSVV HTGEIGAGNV TKLANQVIVA
LNIAAMSEAL TLATKAGVNP DLVYQAIRGG LAGSTVLDAK APMVMDRNFK PGFRIDLHIK
DLANALDTSH GVGAQLPLTA AVMEMMQALR ADGLGTADHS ALACYYEKLA KVEVTR
//
