G3P_PYRHO
ID G3P_PYRHO Reviewed; 334 AA.
AC O59494;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
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; OrderedLocusNames=PH1830;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from
RT Pyrococcus horikoshii ot3.";
RL Submitted (JAN-2006) to the PDB data bank.
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 -!- 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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; BA000001; BAA30950.1; -; Genomic_DNA.
DR PIR; G71194; G71194.
DR RefSeq; WP_010885890.1; NC_000961.1.
DR PDB; 2CZC; X-ray; 2.00 A; A/B/C/D=1-334.
DR PDBsum; 2CZC; -.
DR AlphaFoldDB; O59494; -.
DR SMR; O59494; -.
DR STRING; 70601.3258267; -.
DR EnsemblBacteria; BAA30950; BAA30950; BAA30950.
DR GeneID; 1442672; -.
DR KEGG; pho:PH1830; -.
DR eggNOG; arCOG00493; Archaea.
DR OMA; NAIVPNP; -.
DR OrthoDB; 32079at2157; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; O59494; -.
DR Proteomes; UP000000752; Chromosome.
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 3D-structure; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
FT CHAIN 1..334
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145731"
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:0000269|Ref.2"
FT BINDING 111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
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:0000269|Ref.2"
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:0000269|Ref.2"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 157..169
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:2CZC"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 217..227
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2CZC"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:2CZC"
FT TURN 298..302
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:2CZC"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:2CZC"
SQ SEQUENCE 334 AA; 37264 MW; AEA615734718E39B CRC64;
MKVKVGVNGY GTIGKRVAYA VTKQDDMELI GITKTKPDFE AYRAKELGIP VYAASEEFIP
RFEKEGFEVA GTLNDLLEKV DIIVDATPGG IGAKNKPLYE KAGVKAIFQG GEKADVAEVS
FVAQANYEAA LGKNYVRVVS CNTTGLVRTL SAIREYADYV YAVMIRRAAD PNDTKRGPIN
AIKPTVEVPS HHGPDVQTVI PINIETMAFV VPTTLMHVHS VMVELKKPLT KDDVIDIFEN
TTRVLLFEKE KGFDSTAQII EFARDLHREW NNLYEIAVWK ESINIKGNRL FYIQAVHQES
DVIPENIDAI RAMFELADKW DSIKKTNKSL GILK
