ID A0A498DDM9_9BACI Unreviewed; 528 AA.
AC A0A498DDM9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582, ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN ORFNames=D8M04_06090 {ECO:0000313|EMBL:RLL46770.1};
OS Oceanobacillus piezotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=2448030 {ECO:0000313|EMBL:RLL46770.1, ECO:0000313|Proteomes:UP000270219};
RN [1] {ECO:0000313|EMBL:RLL46770.1, ECO:0000313|Proteomes:UP000270219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-02 {ECO:0000313|EMBL:RLL46770.1,
RC ECO:0000313|Proteomes:UP000270219};
RA Yu L.;
RT "Oceanobacillus sp. YLB-02 draft genome.";
RL Submitted (OCT-2018) 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 ECO:0000256|RuleBase:RU363003};
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 ECO:0000256|RuleBase:RU363003}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU363003}.
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:RLL46770.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RCHR01000002; RLL46770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498DDM9; -.
DR OrthoDB; 9805416at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000270219; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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; cd04902; ACT_3PGDH-xct; 1.
DR CDD; cd12173; PGDH_4; 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; IPR029009; ASB_dom_sf.
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 InterPro; IPR006236; PGDH.
DR InterPro; IPR045626; PGDH_ASB_dom.
DR NCBIfam; TIGR01327; PGDH; 1.
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 Pfam; PF19304; PGDH_inter; 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 SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000270219};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 456..528
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 528 AA; 57390 MW; FEE0595DBB55BE22 CRC64;
MTYKVLISDP LSEDGIKPLT QAENIEIVMQ TDLTPEELEE KIVDFDALLV RSGTQVTRSV
ISKAKNLKII GRAGVGVDNI DLDAATEHGV IVVNAPNGNT NSAAEHTMAM IMAISRNIPQ
AYHALKNHKW DRKKYVGVEL RDKTLGVVGL GRIGAEVATR AKGQRMNVVA YDPFLTPEKA
EKMGIGYGTF EEVISQADFI TVHTPLLKET RHMVNAKAFQ LMKNGVYIVN CARGGIIDED
ALYDAIVSGK VAGAALDVFE EEPFVDHKLL ELPEVVATPH LGASTIEAQE IVAVDVSHDV
LRYLTGDTVK NPVNLPSVAK DVMTVIEPYF QLSEKLGAFL IDLVGEVAEE INLSYSGDLY
DIEVAPLTRN TVKGILKRHL GSSVNDVNAL YLAERKGITV NENKTSKTQG FTNLITVEVK
TKTQTRTVSG TLLNGLGSRI VKVDNYSVDV TPKGHMVVIQ HNDQPGVIGR MGSLLADHGI
NIATMQVDRS DIGGDAIMMV TIDRHLDDEA LDALKGLDVI KEVVAIDL
//