ID A0A087N3B5_9BACI Unreviewed; 534 AA.
AC A0A087N3B5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=CH76_05920 {ECO:0000313|EMBL:KFL43618.1};
OS Lysinibacillus sp. BF-4.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1473546 {ECO:0000313|EMBL:KFL43618.1, ECO:0000313|Proteomes:UP000029097};
RN [1] {ECO:0000313|EMBL:KFL43618.1, ECO:0000313|Proteomes:UP000029097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BF-4 {ECO:0000313|EMBL:KFL43618.1,
RC ECO:0000313|Proteomes:UP000029097};
RA Antwerpen M.H., Georgi E., Zimmermann P., Hoermansdorfer S., Meyer H.,
RA Grass G.;
RT "Genome sequence of strain, BF-4, a Lysinibacillus-like bacillus isolated
RT during an anthrax outbreak in Bavaria.";
RL Submitted (MAR-2014) 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:KFL43618.1}.
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DR EMBL; JPUW01000011; KFL43618.1; -; Genomic_DNA.
DR RefSeq; WP_036144147.1; NZ_JPUW01000011.1.
DR AlphaFoldDB; A0A087N3B5; -.
DR eggNOG; COG0111; Bacteria.
DR OrthoDB; 9805416at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000029097; 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:UP000029097};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 462..534
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 534 AA; 57734 MW; F9534BFD0E619A1D CRC64;
MTSLDQINIL IADPLSEDGI FPLREEKDLN LNVVVDTGLS QEELIAKIGD FHVLLVRSQT
TVTPEVIKAA KNLKLIGRAG VGVDNIDLQA ATEHGVIVVN APDGNTNSAA EHSIAMMTSL
ARYIPQAYNS LKNGKWDRKS YVGVELKNKT LGVIGMGRIG AEVAYRAKGQ RMKVVAYDPF
LTEERAKELG VTKGTVDEVV AAADFVTVHT PLLPETRNII NKERFAIMKD GVRIINCARG
GIVNEDDLYD AIKEGKVAGA ALDVFIEEPA TDNKLLTLPQ VIATPHLGAS TIEAQESVAV
DVSNDIIKFF TTGTVTNPVN MPSIPKELLA QVEPFFELAE KLGTFVTQLT TEPVKEINLS
YAGDVANYDV RPLTSNALKG LLSKNHGNHV NDVNARYLTE RIGVKINEHK TTTAKGFTSL
ITIEIKTANE VHSVAGTLLN GLGARIVKVE DYVVDVTPEG HLLYIRNTDK PGAIGRVATK
LAEKDINIAT MQVGRAQVGG KAVMMLSVDN EVTAEDLNFV AELTNIDEVK AISL
//
