ID   G3P2_STRAE              Reviewed;         334 AA.
AC   E3VWI2;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000303|PubMed:6822480};
DE            Short=GAPDH 2 {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-sensitive glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:6822480};
GN   Name=gap2; Synonyms=gapR;
OS   Streptomyces arenae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=29301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tu469;
RX   PubMed=21284395; DOI=10.1021/ja111279h;
RA   Zhu D., Seo M.J., Ikeda H., Cane D.E.;
RT   "Genome mining in streptomyces. Discovery of an unprecedented P450-
RT   catalyzed oxidative rearrangement that is the final step in the
RT   biosynthesis of pentalenolactone.";
RL   J. Am. Chem. Soc. 133:2128-2131(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, INDUCTION, AND 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   -!- 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: Inhibited by pentalenolactone (PL).
CC       {ECO:0000269|PubMed:6822480}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=110 uM for NAD (at pH 8 and 26 degrees Celsius)
CC         {ECO:0000269|PubMed:6822480};
CC         KM=250 uM for G3P (at pH 8 and 26 degrees Celsius)
CC         {ECO:0000269|PubMed:6822480};
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 absence of pentalenolactone (PL).
CC       {ECO:0000269|PubMed:6822480}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ292065; ADO85570.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VWI2; -.
DR   SMR; E3VWI2; -.
DR   PRIDE; E3VWI2; -.
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..334
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT                   /id="PRO_0000433909"
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         315
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   334 AA;  35019 MW;  0AC5DE6C9D0BF354 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 ASCVFDAGLT
     RVSGPQVKVV GWYDNEWGYS NRLIDLATLI GSSL