G3P_THEAQ
ID G3P_THEAQ Reviewed; 331 AA.
AC P00361;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:8611563};
DE Short=GAPDH {ECO:0000303|PubMed:8611563};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:8611563};
GN Name=gap;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=2602126; DOI=10.1093/nar/17.23.10123;
RA Hecht R.M., Garza A., Lee Y.H., Miller M.D., Pisegna M.A.;
RT "Nucleotide sequence of the glyceraldehyde-3-phosphate dehydrogenase gene
RT from Thermus aquaticus YT1.";
RL Nucleic Acids Res. 17:10123-10123(1989).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=6773768; DOI=10.1111/j.1432-1033.1980.tb04752.x;
RA Hocking J.D., Harris J.I.;
RT "D-glyceraldehyde-3-phosphate dehydrogenase. Amino-acid sequence of the
RT enzyme from the extreme thermophile Thermus aquaticus.";
RL Eur. J. Biochem. 108:567-579(1980).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=8611563; DOI=10.1021/bi951988q;
RA Tanner J.J., Hecht R.M., Krause K.L.;
RT "Determinants of enzyme thermostability observed in the molecular structure
RT of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5-A
RT resolution.";
RL Biochemistry 35:2597-2609(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RA Jenkins J.L., Buencamino R., Tanner J.J.;
RT "High resolution structures of Thermus aquaticus glyceraldehyde-3-phosphate
RT dehydrogenase: role of 220's loop motion in catalysis.";
RL Submitted (MAR-2006) 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. {ECO:0000269|PubMed:8611563};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8611563, ECO:0000269|Ref.4}.
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; X16595; CAA34605.1; -; Genomic_DNA.
DR PIR; S06930; DETWG3.
DR RefSeq; WP_053768084.1; NZ_LHCI01000106.1.
DR PDB; 1CER; X-ray; 2.50 A; A/B/C/D/O/P/Q/R=1-331.
DR PDB; 2G82; X-ray; 1.65 A; A/B/C/D/O/P/Q/R=1-331.
DR PDBsum; 1CER; -.
DR PDBsum; 2G82; -.
DR AlphaFoldDB; P00361; -.
DR SMR; P00361; -.
DR PRIDE; P00361; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P00361; -.
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; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
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; Direct protein sequencing; Glycolysis; NAD;
KW Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..331
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145710"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:8611563"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8611563, ECO:0000269|Ref.4"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8611563, ECO:0000269|Ref.4"
FT BINDING 75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 148..150
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 179
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 194
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 207..208
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 230
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 311
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8611563, ECO:0000269|Ref.4"
FT SITE 176
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000305|PubMed:8611563"
FT CONFLICT 34..35
FT /note="DN -> ND (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:2G82"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2G82"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2G82"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2G82"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 167..177
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2G82"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:2G82"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:2G82"
FT TURN 264..269
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2G82"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:2G82"
FT HELIX 313..329
FT /evidence="ECO:0007829|PDB:2G82"
SQ SEQUENCE 331 AA; 35892 MW; 01946C1AB2A84D3F CRC64;
MKVGINGFGR IGRQVFRILH SRGVEVALIN DLTDNKTLAH LLKYDSIYHR FPGEVAYDDQ
YLYVDGKAIR ATAVKDPKEI PWAEAGVGVV IESTGVFTDA DKAKAHLEGG AKKVIITAPA
KGEDITIVMG VNHEAYDPSR HHIISNASCT TNSLAPVMKV LEEAFGVEKA LMTTVHSYTN
DQRLLDLPHK DLRRARAAAI NIIPTTTGAA KATALVLPSL KGRFDGMALR VPTATGSISD
ITALLKREVT AEEVNAALKA AAEGPLKGIL AYTEDEIVLQ DIVMDPHSSI VDAKLTKALG
NMVKVFAWYD NEWGYANRVA DLVELVLRKG V
