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Database: UniProt
Entry: R6T3E9_9FIRM
LinkDB: R6T3E9_9FIRM
Original site: R6T3E9_9FIRM 
ID   R6T3E9_9FIRM            Unreviewed;       383 AA.
AC   R6T3E9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582};
DE            EC=1.1.1.399 {ECO:0000256|ARBA:ARBA00013001};
DE            EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000256|ARBA:ARBA00030455};
GN   ORFNames=BN714_02086 {ECO:0000313|EMBL:CDC66725.1};
OS   Ruminococcus sp. CAG:57.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262962 {ECO:0000313|EMBL:CDC66725.1, ECO:0000313|Proteomes:UP000018131};
RN   [1] {ECO:0000313|EMBL:CDC66725.1, ECO:0000313|Proteomes:UP000018131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:57 {ECO:0000313|Proteomes:UP000018131};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate
CC       to 3-phosphonooxypyruvate, the first step of the phosphorylated L-
CC       serine biosynthesis pathway. Also catalyzes the reversible oxidation of
CC       2-hydroxyglutarate to 2-oxoglutarate. {ECO:0000256|ARBA:ARBA00003800}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC         + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000256|ARBA:ARBA00001878};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.399; Evidence={ECO:0000256|ARBA:ARBA00000646};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDC66725.1}.
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DR   EMBL; CBFS010000163; CDC66725.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6T3E9; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000018131; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd12174; PGDH_like_3; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
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   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018131};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          318..383
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   383 AA;  40432 MW;  972E584FDEE57D31 CRC64;
     MYNILTLNKI AACGTDIFDK AKYTVSDNAE NPTAIMVRSA KMHDMEMPES LLAIARAGAG
     VNNIPVEKCA EQGIVVFNTP GANSNAVKEL AICALLLSSR KITEAAAWAA SLKGTPDAPK
     TVEGGKSKFA GPEILGKTLG VIGLGAIGGK IANAAVALGM DVIGYDPFLS VNAAIQLEPA
     VKVTADINDI YKNSDYITIH VPYTPDTKNT IDEAQIAMMK DGVRLINLAR GELINSAAVV
     KAIKDGKVAK YVTDFADDVV LGEENVIVLP HLGASTPESE DNCATMAAHE LIDYIEKGTI
     KNSVNFPNAE LAKTGDHLVC VLHKNVPALI AQITSVVSDK GANIENLVNK SKKDWAYTML
     DVTGDVDADA FKSIEGVVGV RVL
//
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