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Database: UniProt
Entry: A0A1G5BJF6_9FIRM
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ID   A0A1G5BJF6_9FIRM        Unreviewed;       388 AA.
AC   A0A1G5BJF6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=SAMN02910370_00620 {ECO:0000313|EMBL:SCX90266.1};
OS   Lachnospiraceae bacterium XPB1003.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520825 {ECO:0000313|EMBL:SCX90266.1, ECO:0000313|Proteomes:UP000199543};
RN   [1] {ECO:0000313|EMBL:SCX90266.1, ECO:0000313|Proteomes:UP000199543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XPB1003 {ECO:0000313|EMBL:SCX90266.1,
RC   ECO:0000313|Proteomes:UP000199543};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMVK01000002; SCX90266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5BJF6; -.
DR   STRING; 1520825.SAMN02910370_00620; -.
DR   OrthoDB; 9805416at2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000199543; 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; cd04901; ACT_3PGDH; 1.
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; 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.
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:UP000199543};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          319..388
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   388 AA;  41439 MW;  CFBDC77BBA141047 CRC64;
     MAYKYHCLNP IAQIGLDGFS ADYNKTDDVN EAEAILVRSA AMHDMELPEK LLTVARAGAG
     VNNIPLDKCA EKGVVVFNTP GANANAVKEL VLAGMLIASR DIVGGIEWVR SDADDENLAK
     AAEKEKKKFA GTEILGKKLG IIGLGAIGVK VANAAIALGM EVYGYDPYLS VKAAWGLNSN
     VHHVSDVNDI YKLCDYITIH VPLLDSTKGM INKDAIAQMK DGVIILNFAR DLLADENAVL
     DGIAAGKIRK YVSDFANPTT AGKDGVILLP HLGASTAEAE DNCAVMAVEE VRNFIENGNI
     INSVNYPNVD SGVCQTAARI TICHKNVANM ITKFTGIFGE LGINISNMVN KSKGDFAYTL
     IDADSAATDD IVTKLNAIDD VIRVRVIK
//
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