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Database: UniProt
Entry: A0A498DDM9_9BACI
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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}.
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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
//
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