G3P_THEMA
ID G3P_THEMA Reviewed; 333 AA.
AC P17721;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:2271518, ECO:0000303|PubMed:7877172};
DE Short=GAPDH {ECO:0000303|PubMed:2271518, ECO:0000303|PubMed:7877172};
DE EC=1.2.1.12 {ECO:0000269|PubMed:2271518, ECO:0000269|PubMed:8508805};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:7877172};
GN Name=gap; OrderedLocusNames=TM_0688;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=8508805; DOI=10.1111/j.1432-1033.1993.tb17894.x;
RA Tomschy A., Glockhuber R., Jaenicke R.;
RT "Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase from
RT the hyperthermophilic eubacterium Thermotoga maritima in Escherichia coli.
RT Authenticity and kinetic properties of the recombinant enzyme.";
RL Eur. J. Biochem. 214:43-50(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP PROTEIN SEQUENCE OF 2-333.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=2401296; DOI=10.1111/j.1432-1033.1990.tb19190.x;
RA Schultes V., Deutzmann R., Jaenicke R.;
RT "Complete amino-acid sequence of glyceraldehyde-3-phosphate dehydrogenase
RT from the hyperthermophilic eubacterium Thermotoga maritima.";
RL Eur. J. Biochem. 192:25-31(1990).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=2271518; DOI=10.1021/bi00485a007;
RA Wrba A., Schweiger A., Schultes V., Jaenicke R., Zavodszky P.;
RT "Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the
RT eubacterium Thermotoga maritima.";
RL Biochemistry 29:7584-7592(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOG, AND SUBUNIT.
RX PubMed=7877172; DOI=10.1006/jmbi.1994.0103;
RA Korndoerfer I., Steipe B., Huber R., Tomschy A., Jaenicke R.;
RT "The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase
RT from the hyperthermophilic bacterium Thermotoga maritima at 2.5-A
RT resolution.";
RL J. Mol. Biol. 246:511-521(1995).
CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD
CC (PubMed:2271518). The first reaction step involves the formation of a
CC hemiacetal intermediate between G3P and a cysteine residue, and this
CC hemiacetal intermediate is then oxidized to a thioester, with
CC concomitant reduction of NAD to NADH. The reduced NADH is then
CC exchanged with the second NAD, and the thioester is attacked by a
CC nucleophilic inorganic phosphate to produce BPG (By similarity).
CC {ECO:0000250|UniProtKB:P00362, ECO:0000269|PubMed:2271518}.
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:0000269|PubMed:2271518, ECO:0000269|PubMed:8508805};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=440 uM for glyceraldehyde-3-phosphate (at pH 8.0 and 40 degrees
CC Celsius) {ECO:0000269|PubMed:2271518};
CC KM=360 uM for glyceraldehyde-3-phosphate (at pH 8.0 and 50 degrees
CC Celsius) {ECO:0000269|PubMed:2271518};
CC KM=400 uM for glyceraldehyde-3-phosphate (at pH 8.0 and 60 degrees
CC Celsius) {ECO:0000269|PubMed:2271518};
CC KM=18.6 uM for NAD(+) (at pH 8.0 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:2271518};
CC KM=37.0 uM for NAD(+) (at pH 8.0 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:2271518};
CC KM=78.8 uM for NAD(+) (at pH 8.0 and 60 degrees Celsius)
CC {ECO:0000269|PubMed:2271518};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:2271518,
CC ECO:0000269|PubMed:7877172}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8508805}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X72629; CAA51205.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35770.1; -; Genomic_DNA.
DR PIR; S33325; DEHGGT.
DR RefSeq; NP_228497.1; NC_000853.1.
DR RefSeq; WP_004081074.1; NZ_CP011107.1.
DR PDB; 1HDG; X-ray; 2.50 A; O/Q=2-333.
DR PDBsum; 1HDG; -.
DR AlphaFoldDB; P17721; -.
DR SMR; P17721; -.
DR STRING; 243274.THEMA_01225; -.
DR PRIDE; P17721; -.
DR EnsemblBacteria; AAD35770; AAD35770; TM_0688.
DR KEGG; tma:TM0688; -.
DR eggNOG; COG0057; Bacteria.
DR InParanoid; P17721; -.
DR OMA; NCVAPMA; -.
DR OrthoDB; 944149at2; -.
DR BioCyc; MetaCyc:MON-401; -.
DR SABIO-RK; P17721; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P17721; -.
DR Proteomes; UP000008183; 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; IDA: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; Direct protein sequencing; Glycolysis; NAD;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2401296"
FT CHAIN 2..333
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145711"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 151..153
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 182
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 197
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 210..211
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 233
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|PubMed:7877172"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7877172"
FT SITE 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q6GIL8"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:1HDG"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1HDG"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1HDG"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1HDG"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:1HDG"
FT TURN 266..272
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:1HDG"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1HDG"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:1HDG"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:1HDG"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1HDG"
SQ SEQUENCE 333 AA; 36425 MW; 12B77104AB5E1CD0 CRC64;
MARVAINGFG RIGRLVYRII YERKNPDIEV VAINDLTDTK TLAHLLKYDS VHKKFPGKVE
YTENSLIVDG KEIKVFAEPD PSKLPWKDLG VDFVIESTGV FRNREKAELH LQAGAKKVII
TAPAKGEDIT VVIGCNEDQL KPEHTIISCA SCTTNSIAPI VKVLHEKFGI VSGMLTTVHS
YTNDQRVLDL PHKDLRRARA AAVNIIPTTT GAAKAVALVV PEVKGKLDGM AIRVPTPDGS
ITDLTVLVEK ETTVEEVNAV MKEATEGRLK GIIGYNDEPI VSSDIIGTTF SGIFDATITN
VIGGKLVKVA SWYDNEYGYS NRVVDTLELL LKM
