ID   HYI_MOUSE               Reviewed;         277 AA.
AC   Q8R1F5; A2A9C1; Q497S8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Putative hydroxypyruvate isomerase;
DE            EC=5.3.1.22;
GN   Name=Hyi;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the reversible isomerization between
CC       hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate
CC       semialdehyde). {ECO:0000250}.
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;
CC   -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM15196.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL627212; CAM15196.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC024619; AAH24619.1; -; mRNA.
DR   EMBL; BC100401; AAI00402.1; -; mRNA.
DR   RefSeq; NP_080877.3; NM_026601.3.
DR   AlphaFoldDB; Q8R1F5; -.
DR   SMR; Q8R1F5; -.
DR   STRING; 10090.ENSMUSP00000006562; -.
DR   PhosphoSitePlus; Q8R1F5; -.
DR   UCD-2DPAGE; Q8R1F5; -.
DR   MaxQB; Q8R1F5; -.
DR   PeptideAtlas; Q8R1F5; -.
DR   PRIDE; Q8R1F5; -.
DR   ProteomicsDB; 266937; -.
DR   DNASU; 68180; -.
DR   GeneID; 68180; -.
DR   KEGG; mmu:68180; -.
DR   UCSC; uc008ujr.3; mouse.
DR   CTD; 81888; -.
DR   MGI; MGI:1915430; Hyi.
DR   eggNOG; KOG4518; Eukaryota.
DR   InParanoid; Q8R1F5; -.
DR   PhylomeDB; Q8R1F5; -.
DR   BioGRID-ORCS; 68180; 1 hit in 19 CRISPR screens.
DR   ChiTaRS; Hyi; mouse.
DR   PRO; PR:Q8R1F5; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8R1F5; protein.
DR   GO; GO:0008903; F:hydroxypyruvate isomerase activity; IBA:GO_Central.
DR   GO; GO:0046487; P:glyoxylate metabolic process; IBA:GO_Central.
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.
PE   1: Evidence at protein level;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..277
FT                   /note="Putative hydroxypyruvate isomerase"
FT                   /id="PRO_0000289242"
FT   ACT_SITE        150
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT   ACT_SITE        249
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT   CONFLICT        127
FT                   /note="T -> A (in Ref. 2; AAH24619/AAI00402)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="G -> S (in Ref. 2; AAH24619/AAI00402)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   277 AA;  30449 MW;  EDAA961B61181444 CRC64;
     MAPLRFSANV SWLFPELPGL PERLHAAGRA GFKAAEVAWP YTESPQALAS AAQTAGLRLV
     LINTPRGDHE KGEMGLGAVP GRQAAFREGL EQAVLYAKAL GCPRIHLMAG RVPQGADRAA
     VKGEMETVFV ENLKHAAGVL AQENLVGLLE PINTRITDPQ YFLDTPRQAA AILQKVGRPN
     LQLQMDIFHW QIMDGNLTGN IREFLPTVGH VQVAQVPDRG EPGSSGELDF TYLFQLLEDE
     GYQGFVGCEY RPRGDTVEGL SWLRSYWDRR GHPRTGQ