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Database: UniProt
Entry: Q58424
LinkDB: Q58424
Original site: Q58424 
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   16-JAN-2019, entry version 137.
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 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; 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.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., 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=3-phospho-D-glycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; L77117; AAB99020.1; -; Genomic_DNA.
DR   PIR; A64427; A64427.
DR   RefSeq; WP_010870531.1; NC_000909.1.
DR   ProteinModelPortal; 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   eggNOG; COG0111; LUCA.
DR   InParanoid; Q58424; -.
DR   KO; K00058; -.
DR   OMA; NIAGMQV; -.
DR   OrthoDB; 24697at2157; -.
DR   PhylomeDB; Q58424; -.
DR   BioCyc; MJAN243232:G1GKE-1108-MONOMER; -.
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; IBA:GO_Central.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.90; -; 1.
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   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 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; Complete proteome; NAD; Oxidoreductase;
KW   Reference proteome; Serine biosynthesis.
FT   CHAIN         1    524       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076009.
FT   DOMAIN      452    524       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   NP_BIND     149    150       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     229    231       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     278    281       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    231    231       {ECO:0000250}.
FT   ACT_SITE    260    260       {ECO:0000250}.
FT   ACT_SITE    278    278       Proton donor. {ECO:0000250}.
FT   BINDING     169    169       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   BINDING     255    255       NAD. {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
//
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