HYI_ECOLI
ID HYI_ECOLI Reviewed; 258 AA.
AC P30147; Q2MBS0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Hydroxypyruvate isomerase;
DE EC=5.3.1.22;
DE AltName: Full=Glyoxylate-induced protein;
GN Name=hyi; Synonyms=gip, ybbG; OrderedLocusNames=b0508, JW0496;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=8440684; DOI=10.1016/s0021-9258(18)53559-6;
RA Chang Y.-Y., Wang A.-Y., Cronan J.E. Jr.;
RT "Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia
RT coli glyoxylate carboligase. An enzyme of the acetohydroxy acid synthase-
RT pyruvate oxidase family.";
RL J. Biol. Chem. 268:3911-3919(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=10561547; DOI=10.1016/s0167-4838(99)00216-2;
RA Ashiuchi M., Misono H.;
RT "Biochemical evidence that Escherichia coli hyi (orf b0508, gip) gene
RT encodes hydroxypyruvate isomerase.";
RL Biochim. Biophys. Acta 1435:153-159(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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).
CC -!- FUNCTION: Catalyzes the reversible isomerization between
CC hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate
CC semialdehyde). Does not catalyze the isomerization of D-fructose to D-
CC glucose or that of D-xylulose to D-xylose. Also does not catalyze
CC racemization of serine, alanine, glycerate or lactate.
CC {ECO:0000269|PubMed:10561547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypyruvate = 2-hydroxy-3-oxopropanoate;
CC Xref=Rhea:RHEA:11952, ChEBI:CHEBI:17180, ChEBI:CHEBI:57978;
CC EC=5.3.1.22; Evidence={ECO:0000269|PubMed:10561547};
CC -!- ACTIVITY REGULATION: Not stimulated by addition of pyridoxal 5'-
CC phosphate (0.1 mM), FAD, NAD(+), NADP(+) or ATP (1 mM each). EDTA (10
CC mM) and metal ions (1 mM) such as Ca(2+), Co(2+), Mg(2+), Ni(2+),
CC Zn(2+) do not affect the enzyme activity.
CC {ECO:0000269|PubMed:10561547}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.5 mM for hydroxypyruvate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:10561547};
CC Vmax=14.3 umol/min/mg enzyme (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:10561547};
CC pH dependence:
CC Optimum pH is 6.8-7.2. {ECO:0000269|PubMed:10561547};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10561547}.
CC -!- INDUCTION: By glyoxylate.
CC -!- DISRUPTION PHENOTYPE: Does not affect growth on glycolate or
CC glyoxylate. {ECO:0000269|PubMed:8440684}.
CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
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DR EMBL; L03845; AAA23865.1; -; Genomic_DNA.
DR EMBL; AB028043; BAA89011.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40261.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73610.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76286.1; -; Genomic_DNA.
DR PIR; JT0746; JT0746.
DR RefSeq; NP_415041.1; NC_000913.3.
DR RefSeq; WP_000943544.1; NZ_SSZK01000024.1.
DR AlphaFoldDB; P30147; -.
DR SMR; P30147; -.
DR BioGRID; 4259863; 8.
DR BioGRID; 850546; 5.
DR DIP; DIP-9994N; -.
DR IntAct; P30147; 12.
DR STRING; 511145.b0508; -.
DR jPOST; P30147; -.
DR PaxDb; P30147; -.
DR PRIDE; P30147; -.
DR EnsemblBacteria; AAC73610; AAC73610; b0508.
DR EnsemblBacteria; BAE76286; BAE76286; BAE76286.
DR GeneID; 946186; -.
DR KEGG; ecj:JW0496; -.
DR KEGG; eco:b0508; -.
DR PATRIC; fig|1411691.4.peg.1769; -.
DR EchoBASE; EB1543; -.
DR eggNOG; COG3622; Bacteria.
DR HOGENOM; CLU_050006_1_2_6; -.
DR InParanoid; P30147; -.
DR OMA; YVQYDIY; -.
DR PhylomeDB; P30147; -.
DR BioCyc; EcoCyc:G6277-MON; -.
DR BioCyc; MetaCyc:G6277-MON; -.
DR PRO; PR:P30147; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008903; F:hydroxypyruvate isomerase activity; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0046487; P:glyoxylate metabolic process; IDA:FlyBase.
DR InterPro; IPR017643; Hydroxypyruvate_isomerase.
DR InterPro; IPR026040; HyI-like.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR PIRSF; PIRSF006241; HyI; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR03234; OH-pyruv-isom; 1.
PE 1: Evidence at protein level;
KW Isomerase; Reference proteome.
FT CHAIN 1..258
FT /note="Hydroxypyruvate isomerase"
FT /id="PRO_0000209106"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 240
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
SQ SEQUENCE 258 AA; 29377 MW; 3F001A47FADE5918 CRC64;
MLRFSANLSM LFGEYDFLAR FEKAAQCGFR GVEFMFPYDY DIEELKHVLA SNKLEHTLHN
LPAGDWAAGE RGIACIPGRE EEFRDGVAAA IRYARALGNK KINCLVGKTP AGFSSEQIHA
TLVENLRYAA NMLMKEDILL LIEPINHFDI PGFHLTGTRQ ALKLIDDVGC CNLKIQYDIY
HMQRMEGELT NTMTQWADKI GHLQIADNPH RGEPGTGEIN YDYLFKVIEN SDYNGWVGCE
YKPQTTTEAG LRWMDPYR
