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Database: UniProt
Entry: P73821
LinkDB: P73821
Original site: P73821 
ID   SERA_SYNY3              Reviewed;         554 AA.
AC   P73821;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-JAN-2019, entry version 134.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=PGDH;
DE            EC=1.1.1.95 {ECO:0000250|UniProtKB:P0A9T0};
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000250|UniProtKB:P0A9T0};
DE            EC=1.1.1.399 {ECO:0000250|UniProtKB:P0A9T0};
GN   Name=serA; OrderedLocusNames=sll1908;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-
CC       glycerate to 3-phosphonooxypyruvate, the first step of the
CC       phosphorylated L-serine biosynthesis pathway. Also catalyzes the
CC       reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
CC       {ECO:0000250|UniProtKB:P0A9T0}.
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         Evidence={ECO:0000250|UniProtKB:P0A9T0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.399;
CC         Evidence={ECO:0000250|UniProtKB:P0A9T0};
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; BA000022; BAA17878.1; -; Genomic_DNA.
DR   PIR; S75016; S75016.
DR   ProteinModelPortal; P73821; -.
DR   SMR; P73821; -.
DR   IntAct; P73821; 6.
DR   STRING; 1148.SYNGTS_1302; -.
DR   PaxDb; P73821; -.
DR   PRIDE; P73821; -.
DR   EnsemblBacteria; BAA17878; BAA17878; BAA17878.
DR   KEGG; syn:sll1908; -.
DR   HOGENOM; HOG000136693; -.
DR   InParanoid; P73821; -.
DR   KO; K00058; -.
DR   OMA; NIAGMQV; -.
DR   PhylomeDB; P73821; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000001425; 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    554       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076007.
FT   DOMAIN      482    554       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   NP_BIND     177    178       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     256    258       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     305    308       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    258    258       {ECO:0000250}.
FT   ACT_SITE    287    287       {ECO:0000250}.
FT   ACT_SITE    305    305       Proton donor. {ECO:0000250}.
FT   BINDING     197    197       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   BINDING     282    282       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
SQ   SEQUENCE   554 AA;  59222 MW;  1D25DCDE7A8DB1D9 CRC64;
     MNLAWLQGLS LGLLSPPAPA LLIFRSFTMA KVLVSDSIDQ VGIDILKQVA QVDVKTGLSE
     AEIIDIVPEY DAIMLRSATK VTEKIIQAGS QLKIIGRAGV GVDNIDVPAA TRQGIVVVNS
     PEGNTIAAAE HALAMMMALA RHIPDANKSV KESKWERKQF IGTEVYKKTL GVVGLGKIGS
     HVAGVAKAMG MKLLAYDPFI SQERADQIGC TLVDLDLLFS EADFITLHIP KTPETANLIN
     AETLAKMKPT ARIINCSRGG IIDEEALVTA IETAQIGGAA LDVFAQEPLG ESRLREFSNV
     ILTPHLGAST EEAQVNVAVD VAEQIRDVLL GLPARSAVNI PGLTPDVMEK LRPYLKLAET
     LGTLVGQLAG GRIDRLTVCL QGDLAEYTNS QPLVVAAIKG LLSQALRERV NYVNAAIEAK
     ERGIRVIETK DASVRDYSGS LHLKATGTMG EHSATGALLS NGEIRITDVD EFPINVPPNN
     YMLFTLHRDM PGIIGKIGSL LGSFNVNIAS MQVGRKIVRG DAIMALSLDD PLPDGLLSEI
     TKVAGIRDAY TVKL
//
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