ID I0KDF7_9BACT Unreviewed; 643 AA.
AC I0KDF7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=FAES_4160 {ECO:0000313|EMBL:CCH02160.1};
OS Fibrella aestuarina BUZ 2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH02160.1, ECO:0000313|Proteomes:UP000011058};
RN [1] {ECO:0000313|EMBL:CCH02160.1, ECO:0000313|Proteomes:UP000011058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX PubMed=22689241; DOI=10.1128/JB.00550-12;
RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT Bacterium.";
RL J. Bacteriol. 194:3555-3555(2012).
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}.
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DR EMBL; HE796683; CCH02160.1; -; Genomic_DNA.
DR RefSeq; WP_015333259.1; NC_020054.1.
DR AlphaFoldDB; I0KDF7; -.
DR STRING; 1166018.FAES_4160; -.
DR KEGG; fae:FAES_4160; -.
DR PATRIC; fig|1166018.3.peg.1114; -.
DR eggNOG; COG0111; Bacteria.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_029190_0_0_10; -.
DR OrthoDB; 1522997at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000011058; Chromosome.
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; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011058}.
FT DOMAIN 574..643
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 643 AA; 71185 MW; 91AADF61C07FB653 CRC64;
MLTQSPTLNS TASAPDQTYY IIDFDSTFTK VEALDVLGEI SLSGRPDRDD VLDQIRTITD
RGMAGELSLA QSIQQRLKLL NAHRDQLPAL VERLSTMVSD SFQRNRVFLT EHADRIFIVS
SGFKEFIVPI VTALGIKAEN VYANTFHFDE AGSIVGCDET NPLSQDKGKV KLIRELNFDG
DVYVIGDGYT DYEIRESGLA NRFYAFTENV VRPSVVAKAD HVAASLDEFL FDNKLSRSQS
YPKSRIKVLL LENVHPIALA LFEKEGFILD VRKGALDEDE LIEALQGVHI LGIRSKTNVT
RRVLDNAPKL MTIGAFCIGT NQIDLTAATE KGIAVFNAPY SNTRSVVELA VGEMIMLIRN
IVPKSNKMHE GIWDKSATNS FEVRGKKLGL VGYGNIGTQL SVVAEALGME VYFYDVVDKL
ALGNARKCAS LDELLAVSDV ITLHTDGRKE NKNLIGAREF GMMKQGVIFL NLSRGHIVDV
PALVEAIKSG KVAGAGVDVF PYEPKTNNEE FLNELRGLPN VILTPHIGGS TEEAQANIGQ
FVPTKLLAYM NNGSTYGSVN FPELQLPLLH DSHRLLHIHA NVPGILAKMN NIFAKYHINI
QGQYLKTNET IGYVISDISK EYADEVVQEL KDIDNTIRFR LLY
//
