ID A0A0D1A8F8_9LACO Unreviewed; 400 AA.
AC A0A0D1A8F8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 Name=serA {ECO:0000313|EMBL:KIS03987.1};
GN ORFNames=WDC_0439 {ECO:0000313|EMBL:KIS03987.1};
OS Paucilactobacillus wasatchensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1335616 {ECO:0000313|EMBL:KIS03987.1, ECO:0000313|Proteomes:UP000032279};
RN [1] {ECO:0000313|EMBL:KIS03987.1, ECO:0000313|Proteomes:UP000032279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDC04 {ECO:0000313|EMBL:KIS03987.1,
RC ECO:0000313|Proteomes:UP000032279};
RA Oberg C.J., Culumber M., McMahon D.J., Broadbent J.R., Oberg T.S.,
RA Ortaki F.;
RT "Lactobacillus wasatchii sp. WDC04, a late gas producing bacteria isolated
RT from aged chedder cheese.";
RL Submitted (AUG-2013) 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:KIS03987.1}.
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DR EMBL; AWTT01000006; KIS03987.1; -; Genomic_DNA.
DR RefSeq; WP_044010166.1; NZ_AWTT01000006.1.
DR AlphaFoldDB; A0A0D1A8F8; -.
DR STRING; 1335616.WDC_0439; -.
DR PATRIC; fig|1335616.4.peg.440; -.
DR OrthoDB; 9805416at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000032279; 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; 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 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000032279}.
FT DOMAIN 319..393
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 400 AA; 43508 MW; 2C7C967171E22C66 CRC64;
MFAIKTYNVI SNVGLAVFPK NKYSINGVAE PDALLIRSQN LHRNVLPVSL LAIGRAGAGV
NNIPLQKASE NGVVVFNAPG ANANAVKELI VAVLILASRP VIPAIAWAKT LTDGEQADVT
LQAEAGKNHY RGAELAGKTL GVIGLGAVGS KVADTARQLG MNVIGYDPYI SVEHAWQVTS
DIKRASTLSE VLSQSDFVTI HIPYNEQNKN LIGANELLMM KKDAILLNYS RNGIVEEAPV
LAALNVGHLK QYWTDFASSE LLQHEKVVVT PHLGGTTQEA EDNCAQMVAQ TLRLYLESGE
IEHSVNYPAV RMPFNSPYRL TFLHQNVPNM LGRITTVLAE LNINIANMIN ASKGDFAYTL
IDVDAPMTAA LYEEFEQKCL AIDEIIRVRG LARPTQKEED
//
