G3P1_STRAE
ID G3P1_STRAE Reviewed; 333 AA.
AC P54226;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1 {ECO:0000303|PubMed:6822480};
DE Short=GAPDH 1 {ECO:0000303|PubMed:6822480};
DE EC=1.2.1.12 {ECO:0000269|PubMed:6822480};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:6822480};
DE AltName: Full=PL-insensitive glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:6822480};
GN Name=gap1; Synonyms=gapR;
OS Streptomyces arenae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=29301;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Tu469;
RX PubMed=8599535; DOI=10.1007/bf01692859;
RA Froehlich K.-U., Kannwischer R., Ruediger M., Mecke D.;
RT "Pentalenolactone-insensitive glyceraldehyde-3-phosphate dehydrogenase from
RT Streptomyces arenae is closely related to GAPDH from thermostable
RT eubacteria and plant chloroplasts.";
RL Arch. Microbiol. 165:179-186(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP SUBUNIT.
RC STRAIN=Tu469;
RX PubMed=6822480; DOI=10.1128/jb.153.2.930-936.1983;
RA Maurer K.H., Pfeiffer F., Zehender H., Mecke D.;
RT "Characterization of two glyceraldehyde-3-phosphate dehydrogenase
RT isoenzymes from the pentalenolactone producer Streptomyces arenae.";
RL J. Bacteriol. 153:930-936(1983).
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:0000269|PubMed:6822480,
CC ECO:0000269|PubMed:8599535}.
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:6822480};
CC -!- ACTIVITY REGULATION: Resistant to pentalenolactone (PL).
CC {ECO:0000269|PubMed:8599535}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for NAD (at pH 8 and 26 degrees Celsius)
CC {ECO:0000269|PubMed:6822480};
CC KM=100 uM for G3P (at pH 8 and 26 degrees Celsius)
CC {ECO:0000269|PubMed:6822480};
CC Temperature dependence:
CC Moderately thermotolerant. {ECO:0000269|PubMed:8599535};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:6822480}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: In the presence of pentalenolactone (PL).
CC {ECO:0000269|PubMed:6822480}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U44856; AAB00916.1; -; Genomic_DNA.
DR AlphaFoldDB; P54226; -.
DR SMR; P54226; -.
DR PRIDE; P54226; -.
DR SABIO-RK; P54226; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA: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; 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 Cytoplasm; Glycolysis; NAD; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..333
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1"
FT /id="PRO_0000145699"
FT ACT_SITE 153
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:0000250|UniProtKB:P00362"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 152..154
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 183
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 198
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 180
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P00362"
SQ SEQUENCE 333 AA; 34946 MW; ED8998E77BA5BA25 CRC64;
MTVRIGINGF GRIGRNVFRA AAARSSELEI VAVNDLGDVP TMAHLLAYDS ILGRFPEEVT
AEPGAIRVGD RTIKVLAERD PGALPWGDLG VDIVIESTGI FTDAAKARSH VDGGAKKVII
AAPASGEDFT VVLGVNDGDY DPERHTIISN ASCTTNCLGV LAKVLHDAVG IDSGMMTTVH
AYTQDQNLQD APHKDLRRAR AAALNIVPTS SGAAKAIGLV LPELAGRLDA FALRVPVPTG
SVTDLTVTTR RGTSVEEVKE AYAAAASGPY KGLLSYVDAP LVSTDIVGDP ASLFDAGLTR
VCGPQVKVVG WYDNEWGYSN RLIDLATLIG SSL
