ID   SERA_METTH              Reviewed;         525 AA.
AC   O27051;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=PGDH;
DE            EC=1.1.1.95;
GN   Name=serA; OrderedLocusNames=MTH_970;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000666; AAB85466.1; -; Genomic_DNA.
DR   PIR; H69229; H69229.
DR   AlphaFoldDB; O27051; -.
DR   SMR; O27051; -.
DR   STRING; 187420.MTH_970; -.
DR   EnsemblBacteria; AAB85466; AAB85466; MTH_970.
DR   KEGG; mth:MTH_970; -.
DR   PATRIC; fig|187420.15.peg.953; -.
DR   HOGENOM; CLU_019796_8_1_2; -.
DR   OMA; NIAGMQV; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000005223; 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..525
FT                   /note="D-3-phosphoglycerate dehydrogenase"
FT                   /id="PRO_0000076010"
FT   DOMAIN          453..525
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        279
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT   BINDING         171
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT   BINDING         230..232
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT   BINDING         256
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT   BINDING         279..282
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9T0"
SQ   SEQUENCE   525 AA;  56991 MW;  DDD63FCFF812B1C5 CRC64;
     MSRMKVLIAD SINEKGISEL EEVAEVVVNT TITPEELLDA IKDFDAIVVR SRTKVTREVI
     EAAPRLKIIA RAGVGVDNVD VKAATDRGIM VINAPESTSI TVAEHSIGLM LALARKIAIA
     DRSVKEGKWE KNRFMGIELN GKTLGIIGMG RIGSQVVVRT KAFGMDIMVY DPYISKEAAE
     EMGVTVTDLE TLLRESDIVT IHVPLTPETR HLISEDEFKL MKDTAFIVNC ARGGIIDEDA
     LYRALKDGEI AGAALDVFEE EPPEGSPLLE LENVVLTPHI GASTSEAQRD AAIIVANEIK
     TVFQGGAPRN VLNMPVMDSE TYKSLKPYIE LAEKMGAIIA QALPGNIEKL DVTYCGELAE
     MQFDILTRTM LQAILNPILT EPVNLINAPS IAKKRGIMVT EARRSESDGY RSIIIATAES
     DRGGFSVEAT HIKEPTIIGI NGYRVDVKPE GTMIIARYRD LPGTIGAIGT KLGQHGINIA
     TMQVGRKEIG GEAVMVLKVD QSVPAEVIEE VKKLDNVDDA VAIEI