ID L0LY92_ENTBF Unreviewed; 296 AA.
AC L0LY92;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=D782_0571 {ECO:0000313|EMBL:AGB76629.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB76629.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB76629.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB76629.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
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; CP003938; AGB76629.1; -; Genomic_DNA.
DR AlphaFoldDB; L0LY92; -.
DR STRING; 693444.D782_0571; -.
DR KEGG; ebf:D782_0571; -.
DR PATRIC; fig|693444.3.peg.556; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_0_6; -.
DR OrthoDB; 9786703at2; -.
DR UniPathway; UPA00565; UER00631.
DR Proteomes; UP000011002; 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:UP000011002}.
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; 30673 MW; 536F91C1EEB45AA9 CRC64;
MTMKVGFIGL GIMGKPMSKN LIKAGYSLVV SDRNPEVIAE LIALGAETAS TAKGIAEQCD
VIITMLPNSP HVKEVALGEG GIIEGAKPGT VLIDMSSIAP LASREISDAL KAKGVDMLDA
PVSGGEPKAI DGTLSVMVGG DKAIFDKYYD LMKAMAGSVV HTGEIGAGNV TKLANQVIVA
LNIAAMSEAL TLATKAGVNP DLVFQAIRGG LAGSTVLEAK APMVMDRNFK PGFRIDLHIK
DLANALDTSH GVGAQLPLTA AVMEMMQALR ADGLGTADHS ALACYYEKLA KVEVTR
//
