HPR_THEMA
ID HPR_THEMA Reviewed; 306 AA.
AC Q9X1C1; G4FFD7;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Hydroxypyruvate reductase;
DE Short=HPR;
DE EC=1.1.1.81;
GN OrderedLocusNames=TM_1401; ORFNames=THEMA_07310, Tmari_1408;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RG DOE Joint Genome Institute;
RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18156253; DOI=10.1128/jb.01469-07;
RA Yang C., Rodionov D.A., Rodionova I.A., Li X., Osterman A.L.;
RT "Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction of
RT related metabolic pathways.";
RL J. Bacteriol. 190:1773-1782(2008).
CC -!- FUNCTION: Involved in the degradation of L-serine via 3-
CC hydroxypyruvate. Catalyzes the non-reversible reduction of 3-
CC hydroxypyruvate to yield D-glycerate. {ECO:0000269|PubMed:18156253}.
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:18156253};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.81;
CC Evidence={ECO:0000269|PubMed:18156253};
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36472.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL50332.1; -; Genomic_DNA.
DR EMBL; CP007013; AHD18703.1; -; Genomic_DNA.
DR PIR; B72257; B72257.
DR RefSeq; NP_229202.1; NC_000853.1.
DR RefSeq; WP_004081620.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X1C1; -.
DR SMR; Q9X1C1; -.
DR STRING; 243274.THEMA_07310; -.
DR EnsemblBacteria; AAD36472; AAD36472; TM_1401.
DR EnsemblBacteria; AGL50332; AGL50332; Tmari_1408.
DR KEGG; tma:TM1401; -.
DR KEGG; tmi:THEMA_07310; -.
DR KEGG; tmm:Tmari_1408; -.
DR KEGG; tmw:THMA_1430; -.
DR PATRIC; fig|243274.17.peg.1408; -.
DR eggNOG; COG1052; Bacteria.
DR InParanoid; Q9X1C1; -.
DR OMA; VHHQTLG; -.
DR OrthoDB; 1638924at2; -.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
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 InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..306
FT /note="Hydroxypyruvate reductase"
FT /id="PRO_0000428996"
FT ACT_SITE 230
FT /evidence="ECO:0000250"
FT ACT_SITE 259
FT /evidence="ECO:0000250"
FT ACT_SITE 280
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 152..153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 228..230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 280..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 306 AA; 33451 MW; 49896899D111C039 CRC64;
MARYRVHVND PLDKEATQLL MNKEELEVTS EHLEKDELMK IIPEVDVLVV RSATKVTADI
IEAGKNLKII ARAGIGLDNI DVQKAKEKGI KVLNTPGASA PSVAELAMGL MLACARHIAR
ATVSLKEGKW EKKALKGKEL LGKTLGLIGF GNIGQEVAKR ALAFGMKIIA YDPAKPETDL
PVEYVDLDTL FKESDFISLH VPLTESTRHI INRESIAKMK DGVIIVNTAR GGTIDEEALY
EEVVSGKVYA AGLDVFEVEP PTDEIRRKLL SLDNVVATPH IGASTAEAQR RVGIELVEKI
FKELGI
