ID Q2YK82_BRUA2 Unreviewed; 412 AA.
AC Q2YK82;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582};
DE EC=1.1.1.399 {ECO:0000256|ARBA:ARBA00013001};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
DE AltName: Full=2-oxoglutarate reductase {ECO:0000256|ARBA:ARBA00030455};
GN Name=serA-2 {ECO:0000313|EMBL:CAJ12949.1};
GN OrderedLocusNames=BAB2_0783 {ECO:0000313|EMBL:CAJ12949.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ12949.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ12949.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ12949.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
RN [2] {ECO:0007829|PDB:3K5P}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-243 AND 245-412.
RG Seattle Structural Genomics Center for Infectious Disease (SSGCID);
RA Edwards T.E., Abendroth J., Smith E.R.;
RT "Crystal structure of amino acid-binding ACT: D-isomer specific 2-
RT hydroxyacid dehydrogenase catalytic domain from Brucella melitensis.";
RL Submitted (OCT-2009) to the PDB data bank.
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 -!- 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 -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; AM040265; CAJ12949.1; -; Genomic_DNA.
DR RefSeq; WP_002967316.1; NZ_KN046823.1.
DR PDB; 3K5P; X-ray; 2.15 A; A=1-412.
DR PDBsum; 3K5P; -.
DR AlphaFoldDB; Q2YK82; -.
DR SMR; Q2YK82; -.
DR STRING; 359391.BAB2_0783; -.
DR GeneID; 55592142; -.
DR KEGG; bmf:BAB2_0783; -.
DR PATRIC; fig|359391.11.peg.475; -.
DR HOGENOM; CLU_019796_9_2_5; -.
DR PhylomeDB; Q2YK82; -.
DR UniPathway; UPA00135; UER00196.
DR EvolutionaryTrace; Q2YK82; -.
DR Proteomes; UP000002719; Chromosome II.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; cd04901; ACT_3PGDH; 1.
DR CDD; cd12176; PGDH_3; 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; 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 PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 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 PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3K5P};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719}.
FT DOMAIN 341..412
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 412 AA; 44664 MW; ACD5DFB6869B0078 CRC64;
MTERLSLSRD RINVLLLEGI SQTAVEYFKS SGYTNVTHLP KALDKADLIK AISSAHIIGI
RSRTQLTEEI FAAANRLIAV GCFSVGTNQV ELKAARKRGI PVFNAPFSNT RSVAELVIGE
IIMLMRRIFP RSVSAHAGGW EKTAIGSREV RGKTLGIVGY GNIGSQVGNL AESLGMTVRY
YDTSDKLQYG NVKPAASLDE LLKTSDVVSL HVPSSKSTSK LITEAKLRKM KKGAFLINNA
RGSVVDLEAL AKVLQEGHLA GAAIDVFPVE PASNGERFST PLQGLENVIL TPHIGGSTEE
AQERIGTEVT RKLVEYSDVG STVGAVNFPQ VQLPPRPTGT RFMHVHENRP GILNSLMNVF
SHHHINIASQ FLQTDGEVGY LVMEADGVGE ASDAVLQEIR EIPGTIRARL LY
//
