ID Q8Y3L1_LISMO Unreviewed; 395 AA.
AC Q8Y3L1;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 131.
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 OrderedLocusNames=lmo2824 {ECO:0000313|EMBL:CAD01037.1};
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963 {ECO:0000313|EMBL:CAD01037.1, ECO:0000313|Proteomes:UP000000817};
RN [1] {ECO:0000313|EMBL:CAD01037.1, ECO:0000313|Proteomes:UP000000817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591984; CAD01037.1; -; Genomic_DNA.
DR PIR; AG1427; AG1427.
DR RefSeq; NP_466346.1; NC_003210.1.
DR RefSeq; WP_009918143.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y3L1; -.
DR STRING; 169963.gene:17595541; -.
DR PaxDb; 169963-lmo2824; -.
DR EnsemblBacteria; CAD01037; CAD01037; CAD01037.
DR GeneID; 984944; -.
DR KEGG; lmo:lmo2824; -.
DR PATRIC; fig|169963.11.peg.2895; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_9_0_9; -.
DR OrthoDB; 9805416at2; -.
DR PhylomeDB; Q8Y3L1; -.
DR BioCyc; LMON169963:LMO2824-MONOMER; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000000817; Chromosome.
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; 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 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:UP000000817}.
FT DOMAIN 317..390
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 395 AA; 43193 MW; C62CAFFB83029012 CRC64;
MFNIQTFNAI AKEGLKTFDL EKYVIDANQP ADGILLRSYN LHDFDFPETV KAVARAGAGV
NNIPVENCSE KGIVVFNTPG ANANAVKELV LASLFVSARP ILEGTEWVKE LPAEDDVEQK
VEAGKKAFAG TELAGKKLGI IGLGAIGALV ANDALSLGMD VVGYDPFVSV DTAWRISKEV
ERAMTIEEVL ATCDYLTVHV PLTDKTRGMF NADTLQLVKD NAVLLNFSRG ELVDSASVKE
ALDDGLLRLY ITDFATKELL NHKKVHVFPH LGASTEEAET NCAKMAAKEL QSYLETGSIK
NSVNFPNVEM PYNGHPRIGI CHKNIPNMVG QITTELGKYS LNILDMINRS KNEYAYTLID
IDKETQANLE QLKQDLLAVQ GVLRVRVIEP LGVTV
//
