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Database: UniProt
Entry: A0A2N3Q1G6_9PROT
LinkDB: A0A2N3Q1G6_9PROT
Original site: A0A2N3Q1G6_9PROT 
ID   A0A2N3Q1G6_9PROT        Unreviewed;       410 AA.
AC   A0A2N3Q1G6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=CWS72_01250 {ECO:0000313|EMBL:PKU26500.1};
OS   Telmatospirillum siberiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Telmatospirillum.
OX   NCBI_TaxID=382514 {ECO:0000313|EMBL:PKU26500.1, ECO:0000313|Proteomes:UP000233293};
RN   [1] {ECO:0000313|Proteomes:UP000233293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=26-4b1 {ECO:0000313|Proteomes:UP000233293};
RA   Hausmann B., Pjevac P., Schreck K., Herbold C.W., Daims H., Wagner M.,
RA   Pester M., Loy A.;
RT   "Draft genome sequence of Telmatospirillum siberiense 26-4b1T, an
RT   acidotolerant peatland alphaproteobacterium potentially involved in sulfur
RT   cycling.";
RL   Submitted (DEC-2017) 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:PKU26500.1}.
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DR   EMBL; PIUM01000001; PKU26500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3Q1G6; -.
DR   OrthoDB; 9793626at2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000233293; 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; cd12176; PGDH_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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10996:SF286; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 1-RELATED; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233293}.
FT   DOMAIN          340..410
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   410 AA;  44631 MW;  DC31DA160EF44875 CRC64;
     MVKLSLSKDK IRILLLEGVH ENAVREFHEA GYNNVELLPH ALGEAELVEK IQGVHMLGIR
     SATKLTDKVL AAANRLFCVG CFCIGTNQVR LDTARRAGIP VFNAPYSNTR SVAELVIGEI
     VMLLRGIPDK SRLAHEGKWL KSAKDSFELR GKTLGIVGYG HIGSQLSVMA EAMGMRVRYF
     DTEKQLAIGN AQPCSKLKEL LSISDVVTLH VPATPQTKNM IGEKELRAMR KGSYLINASR
     GNVVVIEALV KALEDKHLLG AAIDVFPSEP GSNADAFDSP LRGLSNVILT PHVAGSTHEA
     QANIGLEVAE KLIKYSDNGS TFGAVNFVEV SLPVKASGGR FLHIHANVPG MLRRINELFS
     SRNLNVSAQY LQTDPEVGYV VVDIDGEVDE AEVMAELQAL EGTIRARYLY
//
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