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Database: UniProt
Entry: E0TBV1_PARBH
LinkDB: E0TBV1_PARBH
Original site: E0TBV1_PARBH 
ID   E0TBV1_PARBH            Unreviewed;       527 AA.
AC   E0TBV1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   28-FEB-2018, entry version 47.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   OrderedLocusNames=PB2503_01827 {ECO:0000313|EMBL:ADM08444.1};
OS   Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 /
OS   KCTC 12087).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Parvularculales;
OC   Parvularculaceae; Parvularcula.
OX   NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM08444.1, ECO:0000313|Proteomes:UP000001302};
RN   [1] {ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RA   Kang D.-M., Oh H.-M., Cho J.-C.;
RT   "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3-
CC       phosphonooxypyruvate + NADH. {ECO:0000256|RuleBase:RU363003}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC       {ECO:0000256|RuleBase:RU363003}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU363003}.
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DR   EMBL; CP002156; ADM08444.1; -; Genomic_DNA.
DR   RefSeq; WP_013299418.1; NC_014414.1.
DR   ProteinModelPortal; E0TBV1; -.
DR   STRING; 314260.PB2503_01827; -.
DR   EnsemblBacteria; ADM08444; ADM08444; PB2503_01827.
DR   KEGG; pbr:PB2503_01827; -.
DR   eggNOG; ENOG4108JQ1; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136693; -.
DR   KO; K00058; -.
DR   OMA; NIAGMQV; -.
DR   OrthoDB; POG091H02MK; -.
DR   BioCyc; PBER314260:G1GNO-267-MONOMER; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000001302; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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; IPR029009; ASB_dom_sf.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
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   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 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 {ECO:0000256|RuleBase:RU363003};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001302};
KW   NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001302};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN        4    314       2-Hacid_dh. {ECO:0000259|Pfam:PF00389}.
FT   DOMAIN      108    282       2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}.
SQ   SEQUENCE   527 AA;  55666 MW;  81F99DF18169D69F CRC64;
     MKRVLISDKL SEDAVEVLKT RGIEVTFEPG LGKDPEKLKA ALPGHHGIAI RSATKMTAEM
     IEAGTDLKVI GRAGIGVDNV DIDAATATGI AVMNTPFGNA TTTAEHAIAM MLSLARQIPQ
     ANESTHQGKW EKSRFMGREI TGKTLGLIGC GNIGSIVADR AQGLHMKVVA FDPFLTEARA
     IDLGVERVEL DDLLKRADFI TLHTPLTDQT RNILSKQALA KTKKGVRIIN CARGGLVDEE
     ALYDGLESGH IAGAALDVFE KEPATEHKLF GRDDVICTPH LGAATTEAQE NVAIQIAEQI
     ADYLLTGAVT NALNMPSVSA EEAPKLRPYI DLAGRLGGLA GQLAPGAVTG VEMAFAGTAA
     SLNPAPMTAA ALTAVLRPAM REAVNSVNAG QLAKQRGIQV SETRTETSPN FGSTVSVKLT
     TDKGELSVTG ALFGGEPRAV RIGNVRLESN FAPHMLYVQN KDKPGFIGNL GKLLSSKDIN
     IATFNLGRAA PGGTAYALLA VDQPLDDDTL KALSDLPQID EARMLSF
//
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