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Database: UniProt
Entry: A0A0S2DDW5_LYSEN
LinkDB: A0A0S2DDW5_LYSEN
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ID   A0A0S2DDW5_LYSEN        Unreviewed;       520 AA.
AC   A0A0S2DDW5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   Name=serA {ECO:0000313|EMBL:ALN56689.1};
GN   ORFNames=FE772_07110 {ECO:0000313|EMBL:QCW25467.1}, GLE_1332
GN   {ECO:0000313|EMBL:ALN56689.1};
OS   Lysobacter enzymogenes.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=69 {ECO:0000313|EMBL:ALN56689.1, ECO:0000313|Proteomes:UP000061569};
RN   [1] {ECO:0000313|EMBL:ALN56689.1, ECO:0000313|Proteomes:UP000061569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3 {ECO:0000313|EMBL:ALN56689.1,
RC   ECO:0000313|Proteomes:UP000061569};
RA   Kobayashi D.Y.;
RT   "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT   antibioticus ATCC 29479.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QCW25467.1, ECO:0000313|Proteomes:UP000308311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC36 {ECO:0000313|EMBL:QCW25467.1,
RC   ECO:0000313|Proteomes:UP000308311};
RA   Feng T.;
RT   "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT   Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL   Submitted (MAY-2019) 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}.
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DR   EMBL; CP013140; ALN56689.1; -; Genomic_DNA.
DR   EMBL; CP040656; QCW25467.1; -; Genomic_DNA.
DR   RefSeq; WP_057946694.1; NZ_CP110813.1.
DR   STRING; 69.GLE_1332; -.
DR   KEGG; lez:GLE_1332; -.
DR   PATRIC; fig|69.6.peg.1314; -.
DR   OMA; NIAGMQV; -.
DR   OrthoDB; 9805416at2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000061569; Chromosome.
DR   Proteomes; UP000308311; Chromosome.
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; 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; 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   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; 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|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061569};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW   ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN          451..520
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   520 AA;  53819 MW;  D4CC0111D84ABBF2 CRC64;
     MKVLACDGIH EDGLTLFREA GWDVVVSDPI KDPAALTEAL KGVDAVLVRS ATKVPAEALA
     QAANLRVIGR AGAGVDTIDV DAATARGIAV MNAPDGNTLA AAEHAISLLF ALARHIPRAD
     AGMKAGEWPK NGLTGFELEG KKLGVIGLGR IGGTVARKAQ GIGMEVAAHD PFLPASAAGK
     GSVPLKTLEE LLAWADVVTL HIPRTKETTN LLSEASMRSM KKGAYLVNAA RGGLVDEAAL
     LTLIEEGHIA GAALDTFVTE PLPADSPLRA NPKLILTPHL GASTSEAQQA VSTILARQII
     DFVATGAVAG CVNLPPLTAE AAREVGPWMP LMSALGRLAA RLVPAPTRLE ITYAGRTEAL
     DTRPLSRLLV AALLGTASGR VTPVNALQEA AARGLTVSET LGGNGDGFDR LLKLRVIGEK
     RTREIEATLH RGPRVVRLDG VEIEFDPQAH VLLLRNEDRP GMIGAVGSTL GAAGVNIVNF
     ALGAAGDGQA RAAITVDRPV DDAQLAALRA TPGILSLAQV
//
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