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Database: UniProt
Entry: A0A2P8AYI0_9ACTN
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ID   A0A2P8AYI0_9ACTN        Unreviewed;       532 AA.
AC   A0A2P8AYI0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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_2 {ECO:0000313|EMBL:PSK65531.1};
GN   ORFNames=B0E53_02535 {ECO:0000313|EMBL:PSK65531.1};
OS   Micromonospora sp. MH33.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1945509 {ECO:0000313|EMBL:PSK65531.1, ECO:0000313|Proteomes:UP000240342};
RN   [1] {ECO:0000313|EMBL:PSK65531.1, ECO:0000313|Proteomes:UP000240342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MH33 {ECO:0000313|EMBL:PSK65531.1,
RC   ECO:0000313|Proteomes:UP000240342};
RA   Thatcher L.F., Myers C.A., O'Sullivan C.A., Roper M.;
RT   "Draft genome sequences of Micromonospora sp. MH33 and MH99.";
RL   Submitted (FEB-2017) 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:PSK65531.1}.
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DR   EMBL; MUYZ01000062; PSK65531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8AYI0; -.
DR   OrthoDB; 9793626at2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000240342; 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; 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; 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|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU363003}; NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240342};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW   ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN          457..532
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   532 AA;  54561 MW;  1486A3DB539B02CF CRC64;
     MNPVVLIAEE LAPAAIEVLA HDFDVRHVDG TDRPALLSAL SEADAVIVRS ATQIDAEAVA
     AAPRLKVVAR AGVGLDNVEV PAATARGVMV VNAPTSNIVS AAEQAVALLL AVARNTASAS
     AALKAGEWKR SKYTGVEIQG KTVGVVGLGR IGVLFAQRIA AFGTRLIAYD PYIQPARAAQ
     LGVRLVGLEE LLRESDFISI HLPKTPETVG LIGEKELAIV KPGVRIVNAA RGGLVDEQAL
     ANAIAEGRVA GAGVDVYAKE PCTSSPLFAF DNVVATPHLG ASTHEAQDKA GLAVAKSVKL
     ALQGEFVPDA VNVQAGGVVA EDVRPLLPLA EKLGRAFTAV AGGVAASVTV EVRGEIVTND
     VSVLKLAATK GLFSSVVEEQ VTYVNAPHLA AERGVEVTLA TQAETVDHPN LVTVRGALPD
     GRTVSVSGTV AHTGARDVLK LTEVDGFDVE IGAEGILVFL RYADRPGVVG TVGTLLGEAG
     VNIAAMQVAR REAGGETLMT LTVDQALGAD LLTSAADSIG AVAASAADLR DE
//
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