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Database: UniProt
Entry: B6ZLK7_STRDY
LinkDB: B6ZLK7_STRDY
Original site: B6ZLK7_STRDY 
ID   B6ZLK7_STRDY            Unreviewed;       307 AA.
AC   B6ZLK7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00021022, ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
DE   Flags: Fragment;
GN   Name=GAPDH {ECO:0000313|EMBL:BAG85377.1};
OS   Streptococcus dysgalactiae subsp. dysgalactiae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=99822 {ECO:0000313|EMBL:BAG85377.1};
RN   [1] {ECO:0000313|EMBL:BAG85377.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T11358 {ECO:0000313|EMBL:BAG85377.1};
RA   Abdelsalam M., Yoshida T.;
RT   "genetic characterization of Streptococcus dysgalactiae.";
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; AB470099; BAG85377.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6ZLK7; -.
DR   SMR; B6ZLK7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR43148:SF6; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160}.
FT   DOMAIN          1..143
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        143
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         3..4
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         25
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         69
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         142..144
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         173
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         203..204
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         226
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         307
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            170
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAG85377.1"
FT   NON_TER         307
FT                   /evidence="ECO:0000313|EMBL:BAG85377.1"
SQ   SEQUENCE   307 AA;  32686 MW;  1478AD2CA958CCF4 CRC64;
     FGRIGRLAFR RIQNVEGVEV TRINDLTDPN MLAHLLKYDT TQGRFDGTVE VKEGGFEVNG
     NFIKVSAERD PENIDWATDG VEIVLEATGF FAKKEAAEKH LHANGAKKVV ITAPGGNDVK
     TVVFNTNHDI LDGTETVISG ASCTTNCLAP MAKALHDAFG IQKGLMTTIH AYTGDQMILD
     GPHRGGDLRR ARAGAANIVP NSTGAAKAIG LVIPELNGKL DGAAQRVPVP TGSVTELVVT
     LDKNVSVDEI NAAMKAASND SFGYTEDPIV SSDIVGVSYG SLFDATQTKV MEVDGSQLVK
     VVSWYDN
//
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