ID W0I1A9_9GAMM Unreviewed; 295 AA.
AC W0I1A9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:AHF78260.1};
GN ORFNames=Sant_3268 {ECO:0000313|EMBL:AHF78260.1};
OS Sodalis praecaptivus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF78260.1, ECO:0000313|Proteomes:UP000019028};
RN [1] {ECO:0000313|EMBL:AHF78260.1, ECO:0000313|Proteomes:UP000019028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AHF78260.1,
RC ECO:0000313|Proteomes:UP000019028};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(2014).
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; CP006569; AHF78260.1; -; Genomic_DNA.
DR AlphaFoldDB; W0I1A9; -.
DR KEGG; sod:Sant_3268; -.
DR PATRIC; fig|1239307.3.peg.3598; -.
DR HOGENOM; CLU_035117_1_0_6; -.
DR OrthoDB; 9786703at2; -.
DR UniPathway; UPA00565; UER00631.
DR Proteomes; UP000019028; 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:UP000019028}.
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 295 AA; 30699 MW; CD13FC8303158E34 CRC64;
MKIGFIGLGI MGKPMSKNLL KAGYALVVLD RNTESVEDVV AAGAERATSP KAVAEQCEVI
ITMLPNSPHV KEVVLGENGV IEGAKAGSVV IDMSSIAPLA SREIAAALAA KQIQMLDAPV
SGGEPKAIDG TLSVMVGGDK GIFERHVDML KSMAGSVVHT GDIGAGNVTK LANQVIVALN
IAAMSEAMVL ATKAGVDPEL VYQAIRGGLA GSTVLDAKAP MVLDRNFKPG FRIDLHIKDL
ANALDTSHGV GAQLPLTAAV MEMMQALKQD DLGNADHSAL ACYYEKLAHV VVQRQ
//
