ID A0A437M3T0_9PROT Unreviewed; 413 AA.
AC A0A437M3T0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=EOD42_19010 {ECO:0000313|EMBL:RVT92302.1};
OS Rhodovarius crocodyli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodovarius.
OX NCBI_TaxID=1979269 {ECO:0000313|EMBL:RVT92302.1, ECO:0000313|Proteomes:UP000282957};
RN [1] {ECO:0000313|EMBL:RVT92302.1, ECO:0000313|Proteomes:UP000282957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP-6 {ECO:0000313|EMBL:RVT92302.1,
RC ECO:0000313|Proteomes:UP000282957};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVT92302.1}.
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DR EMBL; SACL01000007; RVT92302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437M3T0; -.
DR OrthoDB; 9793626at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000282957; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF01842; ACT; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000282957}.
FT DOMAIN 341..412
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 413 AA; 44358 MW; CA036A1AF0E4774C CRC64;
MSELLSLSKD RIRILLLEGI NDTAVSFFEQ NGYATVTRLK KALDGEELKE ALKGVHILGI
RSRTQVTEEV LEAADRLVAV GCFCIGTNQV DLKAARERGV VVFNAPFSNT RSVAELVMGE
VITLLRGVFP KSVAAHAGVW SKTADGYHEV RGRTLGIVGY GSIGSQLSVL AEAFGMRVLF
HDTQAKLPHG NASRCTSLDE LLMWSDIVTM HVPETPATMG MIGADQFAKM RPGAIFINNA
RGTVVDLHAL ADALKSGHLA GAAVDVFPEE PARNGDPFET PLQGIENVIL TPHIGGSTEE
AQARIGEEVA GKLVDYSDTG ATMGAVNFPQ VALPPQATGV RFMHVHHNVP GILNGINNVF
AKRGLNIAGQ YLQTDGDVGY VVVDAGATRD SQAILQELRE LPGTMRARLL YER
//
