ID D7FBY3_HELP3 Unreviewed; 330 AA.
AC D7FBY3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Glyceraldehyde 3-phosphate dehydrogenase {ECO:0000313|EMBL:CBI65690.1};
DE EC=1.2.1.12 {ECO:0000313|EMBL:CBI65690.1};
GN Name=gapA {ECO:0000313|EMBL:CBI65690.1};
GN OrderedLocusNames=HPB8_133 {ECO:0000313|EMBL:CBI65690.1};
OS Helicobacter pylori (strain B8).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=693745 {ECO:0000313|EMBL:CBI65690.1, ECO:0000313|Proteomes:UP000007091};
RN [1] {ECO:0000313|EMBL:CBI65690.1, ECO:0000313|Proteomes:UP000007091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8 {ECO:0000313|EMBL:CBI65690.1,
RC ECO:0000313|Proteomes:UP000007091};
RX PubMed=20507619; DOI=10.1186/1471-2164-11-335;
RA Farnbacher M., Jahns T., Willrodt D., Daniel R., Haas R., Goesmann A.,
RA Kurtz S., Rieder G.;
RT "Sequencing, annotation, and comparative genome analysis of the gerbil-
RT adapted Helicobacter pylori strain B8.";
RL BMC Genomics 11:335-335(2010).
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; FN598874; CBI65690.1; -; Genomic_DNA.
DR RefSeq; WP_001122606.1; NC_014256.1.
DR AlphaFoldDB; D7FBY3; -.
DR KEGG; hpl:HPB8_133; -.
DR HOGENOM; CLU_030140_0_2_7; -.
DR Proteomes; UP000007091; Chromosome.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
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; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CBI65690.1}.
FT DOMAIN 3..149
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 148..150
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 179
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 207..208
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 230
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 176
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 330 AA; 36035 MW; C744740874143991 CRC64;
MPIRIAINGT GRIGLCAIRV ASQRKDIEIV AINSTAELET LLHLIRHDSV HGHFEAQLNA
DRTLNIGHSK NILVLSERDI NKLDFSAANA EIIIECTGKF NSLEASSAHL KNSVKKVIIS
APAQNTPTFV YGVNHKNYHN ESVISNASCT TNATAPLLKI LDEAFKVENA LLTTIHSYTN
DQNLLDTKHK DIRRARAASL NLIPTSTGVS KAISLVLPHL GPKVTGLAIR VPTPNVSLVD
LSLNFKKSVS KASVQHALKD ACKHAFKGVV GIDEERLVSS DFISSPFSAI VIDDQIMTIG
EKNAKVLAWY DNEMGYSERL IDMAQYIAQN
//
