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Database: UniProt
Entry: W0LGF2_9GAMM
LinkDB: W0LGF2_9GAMM
Original site: W0LGF2_9GAMM 
ID   W0LGF2_9GAMM            Unreviewed;       294 AA.
AC   W0LGF2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   ECO:0000313|EMBL:AHG21040.1};
GN   ORFNames=Z042_16595 {ECO:0000313|EMBL:AHG21040.1};
OS   Chania multitudinisentens RB-25.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Chania.
OX   NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG21040.1, ECO:0000313|Proteomes:UP000019030};
RN   [1] {ECO:0000313|EMBL:AHG21040.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG21040.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Robson E.H.J.;
RT   "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill site.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AHG21040.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG21040.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Chan K.-G.;
RL   Submitted (MAR-2015) 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; CP007044; AHG21040.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0LGF2; -.
DR   STRING; 1441930.Z042_16595; -.
DR   KEGG; sfo:Z042_16595; -.
DR   PATRIC; fig|1441930.4.peg.3275; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_035117_1_1_6; -.
DR   OrthoDB; 9786703at2; -.
DR   UniPathway; UPA00565; UER00631.
DR   Proteomes; UP000019030; 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:UP000019030}.
FT   DOMAIN          2..161
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          164..281
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02032,
FT                   ECO:0000256|PIRSR:PIRSR000103-1"
FT   BINDING         4..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02032"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02032"
FT   BINDING         238
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02032"
SQ   SEQUENCE   294 AA;  30484 MW;  01B32494FB495A65 CRC64;
     MKIGFIGLGI MGKPMSKNLL KAGYSLVVMD RNTDVVTELV ALGAEVAVTP KAVAAQSDIV
     ITMLPNSPQV REVALGENGI IEGAKAGMVL IDMSSIAPLA SREISAALAA KQIAMLDAPV
     SGGEPKAIDG TLSVMVGGDK EVFERCFEVM KTMAGSVVHT GDIGAGNVTK LANQVIVALN
     IAAMSEALVL ATKAGVNPDL VYQAIRGGLA GSTVLDAKAP MVMDRNFKPG FRIDLHIKDL
     ANALDTSHGV GAQLPLTAAV MEMMQALRAD GLGNADHSAL ACYYEKLAKA EVTR
//
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