G3P_PYRFU
ID G3P_PYRFU Reviewed; 334 AA.
AC P61879; P20286;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.59;
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase;
GN Name=gap; Synonyms=gapDH; OrderedLocusNames=PF1874;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP PUTATIVE SUBCELLULAR LOCATION.
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 (By similarity). {ECO:0000250|UniProtKB:P61880,
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:0000250|UniProtKB:P61880};
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:0000250|UniProtKB:P61880};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: 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}.
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DR EMBL; AE009950; AAL81998.1; -; Genomic_DNA.
DR RefSeq; WP_011013013.1; NZ_CP023154.1.
DR AlphaFoldDB; P61879; -.
DR SMR; P61879; -.
DR STRING; 186497.PF1874; -.
DR EnsemblBacteria; AAL81998; AAL81998; PF1874.
DR GeneID; 41713694; -.
DR KEGG; pfu:PF1874; -.
DR PATRIC; fig|186497.12.peg.1945; -.
DR eggNOG; arCOG00493; Archaea.
DR HOGENOM; CLU_069533_0_0_2; -.
DR OMA; NAIVPNP; -.
DR OrthoDB; 32079at2157; -.
DR PhylomeDB; P61879; -.
DR BRENDA; 1.2.1.59; 5243.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Encapsulin nanocompartment; Glycolysis; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..334
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145730"
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
