GARR_ECOL6
ID GARR_ECOL6 Reviewed; 294 AA.
AC P0ABQ3; P23523;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0000255|HAMAP-Rule:MF_02032};
DE EC=1.1.1.60 {ECO:0000255|HAMAP-Rule:MF_02032};
DE AltName: Full=Tartronate semialdehyde reductase {ECO:0000255|HAMAP-Rule:MF_02032};
DE Short=TSAR {ECO:0000255|HAMAP-Rule:MF_02032};
GN Name=garR {ECO:0000255|HAMAP-Rule:MF_02032}; OrderedLocusNames=c3880;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Catalyzes the reduction of tatronate semialdehyde to D-
CC glycerate. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02032};
CC -!- PATHWAY: Carbohydrate acid metabolism; galactarate degradation; D-
CC glycerate from galactarate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_02032}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 2-hydroxy-3-
CC oxopropionate reductase subfamily. {ECO:0000255|HAMAP-Rule:MF_02032}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN82321.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN82321.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P0ABQ3; -.
DR SMR; P0ABQ3; -.
DR STRING; 199310.c3880; -.
DR EnsemblBacteria; AAN82321; AAN82321; c3880.
DR KEGG; ecc:c3880; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_0_6; -.
DR OMA; AWVQSTT; -.
DR UniPathway; UPA00565; UER00631.
DR Proteomes; UP000001410; 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:0103032; F:tartronate semialdehyde reductase activity; IEA:RHEA.
DR GO; GO:0046392; P:galactarate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046487; P:glyoxylate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 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; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR InterPro; IPR006398; Tartro_sem_red.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01505; tartro_sem_red; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..294
FT /note="2-hydroxy-3-oxopropionate reductase"
FT /id="PRO_0000173060"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02032"
FT BINDING 4..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02032"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02032"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02032"
SQ SEQUENCE 294 AA; 30427 MW; 17DA392C2253278C CRC64;
MKVGFIGLGI MGKPMSKNLL KAGYSLVVAD RNPEAIADVI AAGAETASTA KAIAEQCDVI
ITMLPNSPHV KEVALGENGI IEGAKPGTVL IDMSSIAPLA SREISEALKA KGIDMLDAPV
SGGEPKAIDG TLSVMVGGDK AIFDKYYDLM KAMAGSVVHT GEIGAGNVTK LANQVIVALN
IAAMSEALTL ATKAGVNPDL VYQAIRGGLA GSTVLDAKAP MVMDRNFKPG FRIDLHIKDL
ANALDTSHGV GAQLPLTAAV MEMMQALRAD GLGTADHSAL ACYYEKLAKV EVTR
