ID   HPR_BLAHS               Reviewed;         322 AA.
AC   C0CMQ8;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Hydroxypyruvate reductase {ECO:0000303|PubMed:29867142};
DE            EC=1.1.1.81 {ECO:0000269|PubMed:29867142};
GN   Name=hpr {ECO:0000303|Ref.2};
GN   ORFNames=RUMHYD_02143 {ECO:0000312|EMBL:EEG48953.1};
OS   Blautia hydrogenotrophica (strain DSM 10507 / JCM 14656 / S5a33)
OS   (Ruminococcus hydrogenotrophicus).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=476272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10507 / JCM 14656 / S5a33;
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10507 / JCM 14656 / S5a33;
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Blautia hydrogenotrophica DSM 10507 (Ruminococcus
RT   hydrogenotrophicus DSM 10507).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=29867142; DOI=10.1038/s41589-018-0067-7;
RA   Carter M.S., Zhang X., Huang H., Bouvier J.T., Francisco B.S.,
RA   Vetting M.W., Al-Obaidi N., Bonanno J.B., Ghosh A., Zallot R.G.,
RA   Andersen H.M., Almo S.C., Gerlt J.A.;
RT   "Functional assignment of multiple catabolic pathways for D-apiose.";
RL   Nat. Chem. Biol. 14:696-705(2018).
CC   -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes the reduction
CC       of 3-hydroxypyruvate to glycerate. {ECO:0000269|PubMed:29867142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC         Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.81;
CC         Evidence={ECO:0000269|PubMed:29867142};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.14 mM for hydroxypyruvate {ECO:0000269|PubMed:29867142};
CC         Note=kcat is 61 sec(-1). {ECO:0000269|PubMed:29867142};
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; ACBZ01000114; EEG48953.1; -; Genomic_DNA.
DR   RefSeq; WP_005949244.1; NZ_GG657685.1.
DR   AlphaFoldDB; C0CMQ8; -.
DR   SMR; C0CMQ8; -.
DR   STRING; 476272.RUMHYD_02143; -.
DR   EnsemblBacteria; EEG48953; EEG48953; RUMHYD_02143.
DR   PATRIC; fig|476272.21.peg.1575; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_3_9; -.
DR   OrthoDB; 1638924at2; -.
DR   Proteomes; UP000003100; Unassembled WGS sequence.
DR   GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; NAD; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..322
FT                   /note="Hydroxypyruvate reductase"
FT                   /id="PRO_0000446041"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        288
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         160..161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         211..212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         238..240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
SQ   SEQUENCE   322 AA;  35325 MW;  49BF1A69D2DB35AC CRC64;
     MKIVVLDGYC LNPGDLDWKG LEALGECIVY DRTSLTDMEE VISRIGDADI VYTNKTPMPR
     EVFEKCPNIR FVGVLATGYN VVDVNTAKEK GIPVANIPTY GTASVGQFAI ALLLEICHHV
     GHHNQVVHEG KWESNPDWCF WDYPLIELDG KNMGIIGYGR IGQATGKIAQ ALGMKVLAYD
     AYKNPALENE NCRYVELDEL LSQSDVIALH CPLFPETEGI VNKENIAKMK DGVIILNNSR
     GPLIVEQDLV DALNSGKVAA AGLDVVSTEP IKGDNPLLGA KNCIITPHIS WAPKESRKRL
     MDIAVNNLEE FLKGSPVNVV NK