ID A0A1H6Z1A7_9BACT Unreviewed; 630 AA.
AC A0A1H6Z1A7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=SAMN05192553_10495 {ECO:0000313|EMBL:SEJ46446.1};
OS Cyclobacterium xiamenense.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=1297121 {ECO:0000313|EMBL:SEJ46446.1, ECO:0000313|Proteomes:UP000199403};
RN [1] {ECO:0000313|Proteomes:UP000199403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10761 {ECO:0000313|Proteomes:UP000199403};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 -!- 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}.
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DR EMBL; FNZH01000004; SEJ46446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6Z1A7; -.
DR STRING; 1416801.SAMN05192553_10495; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000199403; Unassembled WGS sequence.
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; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
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 Pfam; PF12710; HAD; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF56784; HAD-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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 561..630
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 57..84
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 630 AA; 70103 MW; 1594564A1C05A53D CRC64;
MTVTKKFIID FDSTFTKVEA LDILGEISLK DDPDKAQKLQ AIKDITDQGM EGKLTFRESL
VQRLNILDAN KEQINELITA LKKKVSDSFQ RNKEFLKENA DDIFIISNGF KDFVVPIVTG
YGIKPENVFA NEFVYDESGK ISGFNEDNPL SKNNGKPETI RSLNLEGDIY VIGDGYTDYE
IKASGVANKF YAFTENVHRP SVSSKADHIA PSLDEILYVN KMNKKFSYPK SRINVLLLEN
VHPIGIELMK QEGYNVEVIS SALSEEELAE KIKKVSVLGI RSKTQVTARV LENANRLIAI
GAFCIGTNQI DLETCQEKGI AVFNAPFSNT RSVVELAIAE IIFLMRGLTD KSSSMHQGKW
DKSATGSFEI RGKKLGIIGY GNIGSQLSVL AENMGLDVYY YDVIERLALG NATKIDSLEE
LLRTCDVISL HVDGRKENAL LIDREKLALM KKGAYLINLS RGHVVDVPAL KEALESQHLA
GASIDVFPSE PKNNSEPFVS ELIGLPNTIL TPHIGGSTLE AQENIARFVP GKIIEYINTG
NTFNSVNFPN IQLPFLQNAH RLIHIHLNEP GIMARINRVL ADCSINIVGQ YLKTNEKIGY
VITDIDKAYS SKVIDELKSL EGTIRFRVLY
//
