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SERA_ARCFU
ID   SERA_ARCFU              Reviewed;         527 AA.
AC   O29445;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=PGDH;
DE            EC=1.1.1.95;
GN   Name=serA; OrderedLocusNames=AF_0813;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(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}.
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DR   EMBL; AE000782; AAB90429.1; -; Genomic_DNA.
DR   PIR; E69351; E69351.
DR   RefSeq; WP_010878316.1; NC_000917.1.
DR   AlphaFoldDB; O29445; -.
DR   SMR; O29445; -.
DR   STRING; 224325.AF_0813; -.
DR   EnsemblBacteria; AAB90429; AAB90429; AF_0813.
DR   GeneID; 1484032; -.
DR   KEGG; afu:AF_0813; -.
DR   eggNOG; arCOG01754; Archaea.
DR   HOGENOM; CLU_019796_8_1_2; -.
DR   OMA; NIAGMQV; -.
DR   OrthoDB; 24697at2157; -.
DR   PhylomeDB; O29445; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000002199; 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..527
FT                   /note="D-3-phosphoglycerate dehydrogenase"
FT                   /id="PRO_0000076008"
FT   DOMAIN          453..527
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        259
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         228..230
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9T0"
FT   BINDING         254
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   527 AA;  57204 MW;  D2464729D04004A9 CRC64;
     MKVLVAEPIS EEAIDYMRKN GLEVEVKTGM SREELIREVP KYEAIVVRSQ TKVDAEVIQA
     AKNLKIIGRA GVGVDNIDIN AATQRGIVVV NAPGGNTIST AEHAIALMLA AARKIPQADR
     SVKEGKWERK KFMGIELRGK TAGVIGLGRV GFEVAKRCKA LEMNVLAYDP FVSKERAEQI
     GVKLVDFDTL LASSDVITVH VPRTKETIGL IGKGQFEKMK DGVIVVNAAR GGIVDEAALY
     EAIKAGKVAA AALDVYEKEP PSPDNPLLKL DNVVTTPHIA ASTREAQLNV GMIIAEDIVN
     MAKGLPVRNA VNLPSIEPSD FEFMMPFLTL AEKMGKIASV RLGGAIRKVK VTCSGKLATK
     NTEFVTRALL KGLFEPILSN EINLVSAKPV AVERGITIEE SKVESVEHYE SLLEVWVESN
     GKEMYLAGTC FGNEYRILKI DVYNVNFVPK GHYIISLHED KPGVIGRVGT LFGRNNINIA
     GMIVGRSGDK PGGIQLMLLL VDDPPTPEVL EEMTKLDGII DATYVEL
 
 
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