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SERA_BOVIN
ID   SERA_BOVIN              Reviewed;         533 AA.
AC   Q5EAD2; Q2KJ79;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=3-PGDH;
DE            EC=1.1.1.95 {ECO:0000250|UniProtKB:O43175};
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000305};
DE            EC=1.1.1.399 {ECO:0000250|UniProtKB:O43175};
DE   AltName: Full=Malate dehydrogenase {ECO:0000305};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:O43175};
GN   Name=PHGDH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate
CC       to 3-phosphonooxypyruvate, the first step of the phosphorylated L-
CC       serine biosynthesis pathway. Also catalyzes the reversible oxidation of
CC       2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of
CC       (S)-malate to oxaloacetate. {ECO:0000250|UniProtKB:O43175}.
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         Evidence={ECO:0000250|UniProtKB:O43175};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.399; Evidence={ECO:0000250|UniProtKB:O43175};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000250|UniProtKB:O43175};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 1/3.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O08651}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; BT020637; AAX08654.1; -; mRNA.
DR   EMBL; BC105479; AAI05480.1; -; mRNA.
DR   RefSeq; NP_001030189.1; NM_001035017.1.
DR   AlphaFoldDB; Q5EAD2; -.
DR   SMR; Q5EAD2; -.
DR   STRING; 9913.ENSBTAP00000008907; -.
DR   PaxDb; Q5EAD2; -.
DR   PeptideAtlas; Q5EAD2; -.
DR   PRIDE; Q5EAD2; -.
DR   GeneID; 505103; -.
DR   KEGG; bta:505103; -.
DR   CTD; 26227; -.
DR   eggNOG; KOG0068; Eukaryota.
DR   HOGENOM; CLU_019796_8_1_1; -.
DR   InParanoid; Q5EAD2; -.
DR   OrthoDB; 911009at2759; -.
DR   TreeFam; TF314548; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central.
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; 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; PF19304; PGDH_inter; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 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   2: Evidence at transcript level;
KW   Acetylation; Amino-acid biosynthesis; Isopeptide bond; NAD; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Serine biosynthesis; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   CHAIN           2..533
FT                   /note="D-3-phosphoglycerate dehydrogenase"
FT                   /id="PRO_0000076011"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        283
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   BINDING         155..156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   BINDING         207
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   BINDING         234..236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   BINDING         260
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   BINDING         283..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q61753"
FT   MOD_RES         58
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61753"
FT   MOD_RES         78
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O43175"
FT   CONFLICT        414..415
FT                   /note="RE -> GK (in Ref. 2; AAI05480)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  56452 MW;  9351034A033A2750 CRC64;
     MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT
     SDIINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMIMCLARQ
     IPQAAASMKD GKWERKKFMG TELNGKVLGI LGLGRIGREV ATRMQSFGMK TIGYDPIISP
     EVSASFGVQQ LPLEQIWPLC DFITVHTPLL PSTTGLLNDS TFAQCKKGVC VVNCARGGIV
     DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVNHENVIS CPHLGASTKE AQSRCGEEIA
     LQFVDMVKGK ALAGVVNAQA LASIFCPHTK PWVSLAKALG ALMQAWAGSP KGAIQVVTQG
     SSLKNSGSCL APAVIIGLLK DASQQSNVNL VNAMLLVKEA GLDVTTSHNP ATPREQDFGE
     CLLTVALAGA PYQAVGLVQG TKPVLQALNG AVFRPEVPLH PGQPLLMFRA QASNPAMLPT
     MIGLLAEAGV QLLSYQSSVV SDGETWHVMS ISSLLPSLAP WKPHVTEAFQ FCF
 
 
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