SERA_METJA
ID SERA_METJA Reviewed; 524 AA.
AC Q58424;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE Short=PGDH;
DE EC=1.1.1.95;
GN Name=serA; OrderedLocusNames=MJ1018;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; L77117; AAB99020.1; -; Genomic_DNA.
DR PIR; A64427; A64427.
DR RefSeq; WP_010870531.1; NC_000909.1.
DR AlphaFoldDB; Q58424; -.
DR SMR; Q58424; -.
DR STRING; 243232.MJ_1018; -.
DR PRIDE; Q58424; -.
DR EnsemblBacteria; AAB99020; AAB99020; MJ_1018.
DR GeneID; 1451915; -.
DR KEGG; mja:MJ_1018; -.
DR eggNOG; arCOG01754; Archaea.
DR HOGENOM; CLU_019796_8_1_2; -.
DR InParanoid; Q58424; -.
DR OMA; NIAGMQV; -.
DR OrthoDB; 24697at2157; -.
DR PhylomeDB; Q58424; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000000805; 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 Gene3D; 3.30.1330.90; -; 1.
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 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; SSF143548; SSF143548; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR01327; PGDH; 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; NAD; Oxidoreductase; Reference proteome;
KW Serine biosynthesis.
FT CHAIN 1..524
FT /note="D-3-phosphoglycerate dehydrogenase"
FT /id="PRO_0000076009"
FT DOMAIN 452..524
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT ACT_SITE 231
FT /evidence="ECO:0000250"
FT ACT_SITE 260
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 149..150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT BINDING 229..231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT BINDING 255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT BINDING 278..281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9T0"
SQ SEQUENCE 524 AA; 56924 MW; 5C561BB68C170793 CRC64;
MVKILVTDPL HEDAIKILEE VGEVEVATGL TKEELLEKIK DADVLVVRSG TKVTRDVIEK
AEKLKVIGRA GVGVDNIDVE AATEKGIIVV NAPDASSISV AELTMGLMLA AARNIPQATA
SLKRGEWDRK RFKGIELYGK TLGVIGLGRI GQQVVKRAKA FGMNIIGYDP YIPKEVAESM
GVELVDDINE LCKRADFITL HVPLTPKTRH IIGREQIALM KKNAIIVNCA RGGLIDEKAL
YEALKEGKIR AAALDVFEEE PPKDNPLLTL DNVIGTPHQG ASTEEAQKAA GTIVAEQIKK
VLRGELAENV VNMPNIPQEK LGKLKPYMLL AEMLGNIVMQ VLDGSVNRVE LIYSGELAKE
KTDLIKRAFL KGLLSPILLA GINLVNAPII AKNRNINVVE SSTSEEKYGN AIKITAESDK
KKFSIVGAII NNKPVILEVD GYEVSFIPEG VLAIIKHIDR PGTIGRVCIT LGDYGINIAS
MQVGRKEPGG ESVMLLNLDH TVPEEVIEKI KEIPNIKDVA VINL
