G3P_AQUAE
ID G3P_AQUAE Reviewed; 342 AA.
AC O67161;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
DE Short=GAPDH {ECO:0000250|UniProtKB:P00362};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
GN Name=gap; OrderedLocusNames=aq_1065;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Structural study of Project ID aq_1065 from Aquifex aeolicus VF5.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC NAD. The first reaction step involves the formation of a hemiacetal
CC intermediate between G3P and a cysteine residue, and this hemiacetal
CC intermediate is then oxidized to a thioester, with concomitant
CC reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC second NAD, and the thioester is attacked by a nucleophilic inorganic
CC phosphate to produce BPG. {ECO:0000250|UniProtKB:P00362}.
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=1.2.1.12;
CC Evidence={ECO:0000250|UniProtKB:P09124};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07122.1; -; Genomic_DNA.
DR PIR; F70391; F70391.
DR RefSeq; NP_213724.1; NC_000918.1.
DR RefSeq; WP_010880662.1; NC_000918.1.
DR PDB; 2EP7; X-ray; 2.30 A; A/B=1-342.
DR PDBsum; 2EP7; -.
DR AlphaFoldDB; O67161; -.
DR SMR; O67161; -.
DR STRING; 224324.aq_1065; -.
DR PRIDE; O67161; -.
DR EnsemblBacteria; AAC07122; AAC07122; aq_1065.
DR KEGG; aae:aq_1065; -.
DR PATRIC; fig|224324.8.peg.825; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_0; -.
DR InParanoid; O67161; -.
DR OMA; NCVAPMA; -.
DR OrthoDB; 944149at2; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; O67161; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43148; PTHR43148; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..342
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145629"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 151..153
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 182
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 197
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 210..211
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 233
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT SITE 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:2EP7"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:2EP7"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2EP7"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2EP7"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2EP7"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2EP7"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 255..270
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2EP7"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:2EP7"
FT HELIX 324..339
FT /evidence="ECO:0007829|PDB:2EP7"
SQ SEQUENCE 342 AA; 37613 MW; 4A6E070088985DAA CRC64;
MAIKVGINGF GRIGRSFFRA SWGREEIEIV AINDLTDAKH LAHLLKYDSV HGIFKGSVEA
KDDSIVVDGK EIKVFAQKDP SQIPWGDLGV DVVIEATGVF RDRENASKHL QGGAKKVIIT
APAKNPDITV VLGVNEEKYN PKEHNIISNA SCTTNCLAPC VKVLNEAFGV EKGYMVTVHA
YTNDQRLLDL PHKDFRRARA AAINIVPTTT GAAKAIGEVI PELKGKLDGT ARRVPVPDGS
LIDLTVVVNK APSSVEEVNE KFREAAQKYR ESGKVYLKEI LQYCEDPIVS TDIVGNPHSA
IFDAPLTQVI DNLVHIAAWY DNEWGYSCRL RDLVIYLAER GL
