G3P_PYRWO
ID G3P_PYRWO Reviewed; 334 AA.
AC P61880; P20286;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:2165475};
DE Short=GAPDH;
DE EC=1.2.1.59 {ECO:0000269|PubMed:2165475};
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase;
GN Name=gap; Synonyms=gapDH;
OS Pyrococcus woesei.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=2262;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 49860 / DSM 3773 / JCM 8421 / Vul4;
RX PubMed=2165475; DOI=10.1128/jb.172.8.4329-4338.1990;
RA Zwickl P., Fabry S., Bogedain C., Haas A., Hensel R.;
RT "Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic
RT archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning
RT and sequencing of the gene, and expression in Escherichia coli.";
RL J. Bacteriol. 172:4329-4338(1990).
RN [2]
RP PUTATIVE SUBCELLULAR LOCATION, AND CLASSIFICATION.
RX PubMed=34362927; DOI=10.1038/s41467-021-25071-y;
RA Andreas M.P., Giessen T.W.;
RT "Large-scale computational discovery and analysis of virus-derived
RT microbial nanocompartments.";
RL Nat. Commun. 12:4748-4748(2021).
CC -!- FUNCTION: Possible cargo protein of a type 4B encapsulin
CC nanocompartment (Probable). Active in the presence of NAD and NADP,
CC prefers NADP (PubMed:2165475). {ECO:0000269|PubMed:2165475,
CC ECO:0000305|PubMed:34362927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC Evidence={ECO:0000269|PubMed:2165475};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC Evidence={ECO:0000269|PubMed:2165475};
CC -!- ACTIVITY REGULATION: Insensitive to pentalenolactone, an inhibitor of
CC bacterial and eukaryotic GAPDH. Activity in vitro is significantly
CC stabilized by potassium citrate. {ECO:0000269|PubMed:2165475}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 mM for phosphate {ECO:0000269|PubMed:2165475};
CC KM=1.0 mM for NAD(+) {ECO:0000269|PubMed:2165475};
CC KM=0.01 mM for NADP(+) {ECO:0000269|PubMed:2165475};
CC Temperature dependence:
CC Thermostable. Has a 44-minute half-life at 100 degrees Celsius.
CC {ECO:0000269|PubMed:2165475};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Encapsulin nanocompartment
CC {ECO:0000305|PubMed:34362927}. Note=Its location in a locus with a type
CC 4B encapsulin shell protein suggests it might be located in an
CC encapsulin nanocompartment. {ECO:0000305|PubMed:34362927}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC 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; M83988; AAA73180.1; -; Genomic_DNA.
DR PIR; S10653; DEQYG.
DR AlphaFoldDB; P61880; -.
DR SMR; P61880; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR InterPro; IPR000846; DapB_N.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01113; DapB_N; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01546; GAPDH-II_archae; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Encapsulin nanocompartment;
KW Glycolysis; NAD; NADP; Oxidoreductase.
FT CHAIN 1..334
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145733"
FT ACT_SITE 141
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 140..142
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 192..193
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 37436 MW; 224E0626923AFC66 CRC64;
MKIKVGINGY GTIGKRVAYA VTKQDDMELI GVTKTKPDFE AYRAKELGIP VYAASEEFLP
RFEKAGFEVE GTLNDLLEKV DIIVDATPGG MGEKNKQLYE KAGVKAIFQG GEKAEVAQVS
FVAQANYEAA LGKDYVRVVS CNTTGLVRTL NAIKDYVDYV YAVMIRRAAD PNDIKRGPIN
AIKPSVTIPS HHGPDVQTVI PINIETSAFV VPTTIMHVHS IMVELKKPLT REDVIDIFEN
TTRVLLFEKE KGFESTAQLI EFARDLHREW NNLYEIAVWK ESINVKGNRL FYIQAVHQES
DVIPENIDAI RAMFEIAEKW ESIKKTNKSL GILK
