ID A0A385C7Z1_9GAMM Unreviewed; 410 AA.
AC A0A385C7Z1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=BEN71_17115 {ECO:0000313|EMBL:AXQ23684.1};
OS Acinetobacter wuhouensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1879050 {ECO:0000313|EMBL:AXQ23684.1, ECO:0000313|Proteomes:UP000257257};
RN [1] {ECO:0000313|EMBL:AXQ23684.1, ECO:0000313|Proteomes:UP000257257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHA60 {ECO:0000313|EMBL:AXQ23684.1,
RC ECO:0000313|Proteomes:UP000257257};
RX PubMed=30117799; DOI=10.1099/ijsem.0.002963;
RA Hu Y., Feng Y., Qin J., Radolfova-Krizova L., Maixnerova M., Zhang X.,
RA Nemec A., Zong Z.;
RT "Acinetobacter wuhouensis sp. nov., isolated from hospital sewage.";
RL Int. J. Syst. Evol. Microbiol. 68:3212-3216(2018).
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; CP031716; AXQ23684.1; -; Genomic_DNA.
DR RefSeq; WP_068975085.1; NZ_CP031716.1.
DR AlphaFoldDB; A0A385C7Z1; -.
DR STRING; 1879050.GCA_001696605_02491; -.
DR KEGG; awu:BEN71_17115; -.
DR OrthoDB; 9805416at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000257257; 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; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 341..410
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 410 AA; 43984 MW; 68FD07047CD784B9 CRC64;
MSQHLSLPKD KIRFLLLEGV HQNAIDTLNA AGYTNIDFRK TALEGEALKE AVKDAHFIGI
RSRTQLTEEI FEAANKLIAV GCFCIGTNQV NLNAAMIRGI PVFNAPYSNT RSVAELVLAE
AILLLRGVPA KSASTHRGGW NKSAVGSFET RGKTLGIVGY GSIGSQLSVL AESMGMHVIY
YDAVTKLPMG NARQVGSLDE LLANADVVTL HVPDVPSTKN FFAKEQFAKM KEGSIFLNAA
RGTCVVIEDL ADAIKSGHIA GAAVDVFPKE PKANGEEFVS PLRGLDNVIL TPHVGGSTME
AQANIGLEVA EKFVAYSDKG MTLSAVNFPE IALPLTEGKH RLLHIHKNVP GVLSKINNLF
AEHGINISGQ SLMTKGDVGY LVMDVDATAS QEALDTLHEV EGTIRVRVLF
//
