ID A0Y9R6_9GAMM Unreviewed; 409 AA.
AC A0Y9R6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=GP2143_16481 {ECO:0000313|EMBL:EAW32870.1};
OS marine gamma proteobacterium HTCC2143.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; BD1-7 clade.
OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW32870.1, ECO:0000313|Proteomes:UP000004931};
RN [1] {ECO:0000313|EMBL:EAW32870.1, ECO:0000313|Proteomes:UP000004931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW32870.1,
RC ECO:0000313|Proteomes:UP000004931};
RX PubMed=20601481; DOI=10.1128/JB.00683-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the oligotrophic marine Gammaproteobacterium HTCC2143,
RT isolated from the Oregon Coast.";
RL J. Bacteriol. 192:4530-4531(2010).
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:EAW32870.1}.
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DR EMBL; AAVT01000001; EAW32870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Y9R6; -.
DR STRING; 247633.GP2143_16481; -.
DR eggNOG; COG0111; Bacteria.
DR OrthoDB; 9805416at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000004931; 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 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000004931}.
FT DOMAIN 340..409
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 409 AA; 44159 MW; 1E8074A4061E8E78 CRC64;
MSQTSLDKSK IKFLLLEGVH QSAVDTLKAA GYSNIVCHPK ALSEQQLKEE LADAHFVGIR
SRTQLTDDIF STAKKLIAVG CFCIGTNQVD LKAATEKGVV IFNAPFSNTR SVAELVIAEA
ILLLRGVAEK NALAHRGIWQ KSASGSFEIR GKQLGIIGYG SIGMQLGVIA ESLGMQVVFY
DVVSKLPLGN AMQVPSLNGL LAKSDIVSLH VPETGSTRNM IGEQELTQIK PGAILINASR
GTVIDIDALA AALESGRLSG AAIDVFPVEP RSNDDEFLSP LRKFDNVFLT PHIGGSTMEA
QENIGLEVAE KMARYSDNGT STSSVNFPEV ALPAHTDMHR LLHTHRNTPG VMSAINKVFA
ENNINIRAQY LQTTQDIGYV VIDIDAEYSE LALKKLSAIE GTIRCRVLF
//
