G3P_TREPA
ID G3P_TREPA Reviewed; 350 AA.
AC O83816;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
DE Short=GAPDH {ECO:0000250|UniProtKB:P00362};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
GN Name=gap; OrderedLocusNames=TP_0844;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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:0000250|UniProtKB:P00362}.
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:0000250|UniProtKB:P09124};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00362}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AE000520; AAC65812.1; -; Genomic_DNA.
DR PIR; D71273; D71273.
DR RefSeq; WP_010882288.1; NC_021490.2.
DR AlphaFoldDB; O83816; -.
DR SMR; O83816; -.
DR IntAct; O83816; 2.
DR STRING; 243276.TPANIC_0844; -.
DR PRIDE; O83816; -.
DR EnsemblBacteria; AAC65812; AAC65812; TP_0844.
DR GeneID; 57879361; -.
DR KEGG; tpa:TP_0844; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_3_12; -.
DR OMA; NCVAPMA; -.
DR OrthoDB; 944149at2; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS: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; PTHR10836; PTHR10836; 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 3: Inferred from homology;
KW Cytoplasm; Glycolysis; NAD; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..350
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145712"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 82
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 161..163
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 193
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 222..223
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 245
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 331
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 190
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P0A9B2"
SQ SEQUENCE 350 AA; 38083 MW; E305A8F535913CAA CRC64;
MRVAINGFGR IGRLVLQAMA EQKLLGKEFD VAAVVDLSTD ARYFAYQLKY DSVQGKMGSS
LSAPAEDILE VGGHRIKCVC GRGLKPSQLP WKDLGIEVVI EATGIYANES SYGHLEAGAK
RVIISAPAKS SDASKPVKTI VMGVNEHEFD PAEHKVVSNA SCTTNCLAPV VHVFLKEGVG
IETGLMTTIH SYTATQKTVD GVSLKDWRGG RAAAVNIIPS TTGAAKAVGE VLPSTRGKLT
GMAFRVPTPT GSVVDLTFRT EKETSVADLN AMLKKASESY LRGVLQYCDE DIVSADVIHN
QYSSIYDSRA TLQNNLPNEK RFFKVVSWYD NEWGYSNRVV DLLKFISQKR
