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Database: UniProt
Entry: Q9X1C1
LinkDB: Q9X1C1
Original site: Q9X1C1 
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   16-JAN-2019, entry version 121.
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 / MSB8 / DSM 3109 / JCM 10099).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
RA   Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
RA   McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
RA   Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
RA   Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
RA   Salzberg S.L., 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 / MSB8 / DSM 3109 / JCM 10099;
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
RT   lifestyle.";
RL   PLoS Genet. 9:E1003485-E1003485(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
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
RT   of 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.
CC       {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;
CC         EC=1.1.1.81; Evidence={ECO:0000269|PubMed:18156253};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16659, ChEBI:CHEBI:17180, ChEBI:CHEBI:57783,
CC         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}.
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   ProteinModelPortal; Q9X1C1; -.
DR   SMR; Q9X1C1; -.
DR   STRING; 243274.TM1401; -.
DR   EnsemblBacteria; AAD36472; AAD36472; TM_1401.
DR   EnsemblBacteria; AGL50332; AGL50332; Tmari_1408.
DR   EnsemblBacteria; AHD18703; AHD18703; THEMA_07310.
DR   GeneID; 898075; -.
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; ENOG4108JQ1; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   InParanoid; Q9X1C1; -.
DR   KO; K22982; -.
DR   OMA; PHIAWAY; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; TMAR243274:G1H0Q-1463-MONOMER; -.
DR   Proteomes; UP000008183; Chromosome.
DR   Proteomes; UP000013901; Chromosome.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
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   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    306       Hydroxypyruvate reductase.
FT                                /FTId=PRO_0000428996.
FT   NP_BIND     152    153       NAD. {ECO:0000250}.
FT   NP_BIND     228    230       NAD. {ECO:0000250}.
FT   NP_BIND     280    283       NAD. {ECO:0000250}.
FT   ACT_SITE    230    230       {ECO:0000250}.
FT   ACT_SITE    259    259       {ECO:0000250}.
FT   ACT_SITE    280    280       Proton donor. {ECO:0000250}.
FT   BINDING     172    172       NAD. {ECO:0000250}.
FT   BINDING     254    254       NAD. {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
//
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