ID   A0A0S7CV44_9MICC        Unreviewed;       374 AA.
AC   A0A0S7CV44;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:GAP57880.1};
GN   ORFNames=AHiyo1_08260 {ECO:0000313|EMBL:GAP57880.1};
OS   Arthrobacter sp. Hiyo1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1588020 {ECO:0000313|EMBL:GAP57880.1};
RN   [1] {ECO:0000313|EMBL:GAP57880.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hiyo1 {ECO:0000313|EMBL:GAP57880.1};
RX   PubMed=26764021; DOI=10.1186/s12864-016-2380-4;
RA   Hiraoka S., Machiyama A., Ijichi M., Inoue K., Oshima K., Hattori M.,
RA   Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Genomic and metagenomic analysis of microbes in a soil environment
RT   affected by the 2011 Great East Japan Earthquake tsunami.";
RL   BMC Genomics 17:53-53(2016).
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   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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DR   EMBL; DF952468; GAP57880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7CV44; -.
DR   Proteomes; UP000063628; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd04902; ACT_3PGDH-xct; 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; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR045626; PGDH_ASB_dom.
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; 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; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          300..374
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   374 AA;  39452 MW;  AF3C29CFDC57248D CRC64;
     MAARLQGFET EILAYDPYIT SARAAQLGVK LVTLDELLEK SDFITIHMPK TPETVGMLGA
     DAFKKMKETA YVVNVARGGL IDEEALHEAL EDGQIAGAGI DVFVKEPSTD LPFFGMDNVI
     VTPHLGASTD EAQEKAGVSV AKSVRLALAG ELVPDAVNVA GGVIASDVRP GIPLIEKLGR
     IFTALTHASL TQIDVEVAGE ISSLDVKVLE LAALKGVFAD VVTEQVSYVN APVIAEQRGI
     NTRLITTPEA EDYRNVLTIR GALSDGSQIS VAGTLTGPKQ VQKLVGVNGY DVEIPISEHL
     VVVSYADRPG VIGTIGHILG MNNINIGGMQ VARQSEGGQV LALLTIDTSV PQQVLEAIKA
     GIGADMVREV DLED
//