ID Q74DW7_GEOSL Unreviewed; 542 AA.
AC Q74DW7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
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 Name=serA {ECO:0000313|EMBL:AAR34574.1};
GN OrderedLocusNames=GSU1198 {ECO:0000313|EMBL:AAR34574.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR34574.1, ECO:0000313|Proteomes:UP000000577};
RN [1] {ECO:0000313|EMBL:AAR34574.1, ECO:0000313|Proteomes:UP000000577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA
RC {ECO:0000313|Proteomes:UP000000577};
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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}.
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DR EMBL; AE017180; AAR34574.1; -; Genomic_DNA.
DR RefSeq; NP_952251.1; NC_002939.5.
DR RefSeq; WP_010941855.1; NC_002939.5.
DR AlphaFoldDB; Q74DW7; -.
DR SMR; Q74DW7; -.
DR STRING; 243231.GSU1198; -.
DR EnsemblBacteria; AAR34574; AAR34574; GSU1198.
DR KEGG; gsu:GSU1198; -.
DR PATRIC; fig|243231.5.peg.1193; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_8_1_7; -.
DR InParanoid; Q74DW7; -.
DR OrthoDB; 9793626at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000000577; Chromosome.
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; 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; 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|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000000577};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 457..529
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 542 AA; 58758 MW; E3039EB5248B15D8 CRC64;
MKIIVTDEVA QEGLALLAQD PRVELDVKLG LKKEELLAII GDYDVIITRS GTTVNRELLD
AGKKLRLVAR AGVGIDNVDV DYASSRGVIV VNAPFGNTNS AAEHAMALLL SFCRNVTRAN
GSLKSGEWKR APFTGYELKG KTAGVIGLGK VGGRVATRLK AFECDVLACD PYIAVKRAHD
LGVKLVSHDE IYKNCDIITV HTPLTDETRN MIGERELAMM KDGVIIVNAA RGGIIEEAAL
LKYLESGKVA GAAVDVFSEE PPKSEYLKKL IGHERVVVTP HLGANTFEAQ VNVAVDVSRE
ILNYLDDQPL ENAVNIPRFD LALMDQMRPF LNLMNTLCEF GIQLLDANIS KIVFGFSGSI
AHYDCTPLTV CGLASILNRM VDQDVNMVNA SLIAEGMGIV VEESKTTHAD AFSNLITIVV
EGEGGKRRTI SGTLFEGLPR IVRLRDYSMD FAPEEHMLLL HYADRPGMIG KIGTIMGQHE
INIASMNLGR SEKKGEAMVI LSLDSAVPPQ VLEEVRAATD ATFIKAIHMP GARCSRSCGC
TA
//
