ID A5X611_SALET Unreviewed; 308 AA.
AC A5X611;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
DE Flags: Fragment;
GN Name=gapA {ECO:0000313|EMBL:ABG33973.1};
OS Salmonella enterica I.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=59201 {ECO:0000313|EMBL:ABG33973.1};
RN [1] {ECO:0000313|EMBL:ABG33973.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=02-0061 {ECO:0000313|EMBL:ABG33976.1}, 02-0062
RC {ECO:0000313|EMBL:ABG34014.1}, 02-0105 {ECO:0000313|EMBL:ABG34015.1},
RC 02-0115 {ECO:0000313|EMBL:ABG34018.1}, 2433
RC {ECO:0000313|EMBL:ABG34017.1}, CNM-1029 02
RC {ECO:0000313|EMBL:ABG33973.1}, CNM-1374/99
RC {ECO:0000313|EMBL:ABG34019.1}, CNM-3556/03
RC {ECO:0000313|EMBL:ABG34016.1}, CNM-3578 03
RC {ECO:0000313|EMBL:ABG33975.1}, and CNM-3663 03
RC {ECO:0000313|EMBL:ABG33977.1};
RA McQuiston J.R., Basi H.K., Herrera-Leon S., Bryant L.T., Steigerwalt A.G.,
RA Fields P.I.;
RT "A Multiplex PCR for identifying Salmonellae and differentiating them from
RT other species of Enterobacteriaceae.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003501}.
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:0000256|ARBA:ARBA00001810};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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; DQ644638; ABG33973.1; -; Genomic_DNA.
DR EMBL; DQ644640; ABG33975.1; -; Genomic_DNA.
DR EMBL; DQ644641; ABG33976.1; -; Genomic_DNA.
DR EMBL; DQ644642; ABG33977.1; -; Genomic_DNA.
DR EMBL; DQ644679; ABG34014.1; -; Genomic_DNA.
DR EMBL; DQ644680; ABG34015.1; -; Genomic_DNA.
DR EMBL; DQ644681; ABG34016.1; -; Genomic_DNA.
DR EMBL; DQ644682; ABG34017.1; -; Genomic_DNA.
DR EMBL; DQ644683; ABG34018.1; -; Genomic_DNA.
DR EMBL; DQ644684; ABG34019.1; -; Genomic_DNA.
DR AlphaFoldDB; A5X611; -.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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-KW.
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; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160}.
FT DOMAIN 1..144
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 6..7
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 114
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 143..145
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 174
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 308
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 171
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABG33973.1"
FT NON_TER 308
FT /evidence="ECO:0000313|EMBL:ABG33973.1"
SQ SEQUENCE 308 AA; 33087 MW; 217FA12AB35497C5 CRC64;
INGFGRIGRI VFRAAQKRSD IEIVAINDLL DAEYMAYMLK YDSTHGRFDG TVEVKDGHLI
VNGKKIRVTA ERDPANLKWD EVGVDVVAEA TGIFLTDETA RKHITAGAKK VVLTGPSKDN
TPMFVKGANF DKYEGQDIVS NASCTTNCLA PLAKVINDNF GIIEGLMTTV HATTATQKTV
DGPSHKDWRG GRGASQNIIP SSTGAAKAVG KVLPELNGKL TGMAFRVPTP NVSVVDLTVR
LEKAATYEQI KAAVKAAAEG EMKGVLGYTE DDVVSTDFNG EVCTSVFDAK AGIALNDNFV
KLVSWYDN
//
