GARR_ECOLI
ID GARR_ECOLI Reviewed; 294 AA.
AC P0ABQ2; P23523; Q2M984;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
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, ECO:0000269|PubMed:9772162};
DE AltName: Full=Tartronate semialdehyde reductase {ECO:0000255|HAMAP-Rule:MF_02032, ECO:0000303|PubMed:9772162};
DE Short=TSAR {ECO:0000255|HAMAP-Rule:MF_02032, ECO:0000303|PubMed:9772162};
GN Name=garR {ECO:0000255|HAMAP-Rule:MF_02032, ECO:0000303|PubMed:10762278};
GN Synonyms=yhaE; OrderedLocusNames=b3125, JW5526;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1705543; DOI=10.1128/jb.173.5.1813-1816.1991;
RA Komine Y., Inokuchi H.;
RT "Precise mapping of the rnpB gene encoding the RNA component of RNase P in
RT Escherichia coli K-12.";
RL J. Bacteriol. 173:1813-1816(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9772162; DOI=10.1021/bi981124f;
RA Hubbard B.K., Koch M., Palmer D.R., Babbitt P.C., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily:
RT characterization of the (D)-glucarate/galactarate catabolic pathway in
RT Escherichia coli.";
RL Biochemistry 37:14369-14375(1998).
RN [5]
RP GENE NAME, AND INDUCTION.
RX PubMed=10762278; DOI=10.1128/jb.182.9.2672-2674.2000;
RA Monterrubio R., Baldoma L., Obradors N., Aguilar J., Badia J.;
RT "A common regulator for the operons encoding the enzymes involved in D-
RT galactarate, D-glucarate, and D-glycerate utilization in Escherichia
RT coli.";
RL J. Bacteriol. 182:2672-2674(2000).
CC -!- FUNCTION: Catalyzes the reduction of tatronate semialdehyde to D-
CC glycerate. {ECO:0000255|HAMAP-Rule:MF_02032,
CC ECO:0000269|PubMed:9772162}.
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 ECO:0000269|PubMed:9772162};
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 ECO:0000269|PubMed:9772162};
CC -!- PATHWAY: Carbohydrate acid metabolism; galactarate degradation; D-
CC glycerate from galactarate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_02032,
CC ECO:0000269|PubMed:9772162}.
CC -!- INDUCTION: Induced by D-galactarate, D-glucarate and D-glycerate.
CC {ECO:0000269|PubMed:10762278}.
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=AAA57928.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA14238.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77172.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D90212; BAA14238.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18997; AAA57928.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76159.3; -; Genomic_DNA.
DR EMBL; AP009048; BAE77172.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_417594.3; NC_000913.3.
DR AlphaFoldDB; P0ABQ2; -.
DR SMR; P0ABQ2; -.
DR BioGRID; 4259488; 48.
DR DIP; DIP-9742N; -.
DR STRING; 511145.b3125; -.
DR jPOST; P0ABQ2; -.
DR PaxDb; P0ABQ2; -.
DR PRIDE; P0ABQ2; -.
DR EnsemblBacteria; AAC76159; AAC76159; b3125.
DR EnsemblBacteria; BAE77172; BAE77172; BAE77172.
DR GeneID; 947631; -.
DR KEGG; ecj:JW5526; -.
DR KEGG; eco:b3125; -.
DR PATRIC; fig|511145.12.peg.3218; -.
DR EchoBASE; EB1163; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_1_6; -.
DR InParanoid; P0ABQ2; -.
DR PhylomeDB; P0ABQ2; -.
DR BioCyc; EcoCyc:TSA-REDUCT-MON; -.
DR BioCyc; MetaCyc:TSA-REDUCT-MON; -.
DR SABIO-RK; P0ABQ2; -.
DR UniPathway; UPA00565; UER00631.
DR PRO; PR:P0ABQ2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008679; F:2-hydroxy-3-oxopropionate reductase activity; IDA:EcoCyc.
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:0042838; P:D-glucarate catabolic process; IDA:EcoCyc.
DR GO; GO:0046392; P:galactarate catabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..294
FT /note="2-hydroxy-3-oxopropionate reductase"
FT /id="PRO_0000173059"
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
