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Database: UniProt
Entry: O83816
LinkDB: O83816
Original site: O83816 
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   09-DEC-2015, entry version 110.
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; Spirochaetaceae; 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.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
CC   -!- FUNCTION: Catalyzes the oxidative phosphorylation of
CC       glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG)
CC       using the cofactor NAD. The first reaction step involves the
CC       formation of a hemiacetal intermediate between G3P and a cysteine
CC       residue, and this hemiacetal intermediate is then oxidized to a
CC       thioester, with concomitant reduction of NAD to NADH. The reduced
CC       NADH is then exchanged with the second NAD, and the thioester is
CC       attacked by a nucleophilic inorganic phosphate to produce BPG.
CC       {ECO:0000250|UniProtKB:P00362}.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC       {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
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AE000520; AAC65812.1; -; Genomic_DNA.
DR   PIR; D71273; D71273.
DR   RefSeq; WP_010882288.1; NC_021490.2.
DR   ProteinModelPortal; O83816; -.
DR   SMR; O83816; 1-349.
DR   IntAct; O83816; 2.
DR   STRING; 243276.TP0844; -.
DR   PRIDE; O83816; -.
DR   EnsemblBacteria; AAC65812; AAC65812; TP_0844.
DR   GeneID; 2611009; -.
DR   KEGG; tpa:TP_0844; -.
DR   PATRIC; 20531795; VBITrePal57110_0895.
DR   eggNOG; ENOG4105C17; Bacteria.
DR   eggNOG; COG0057; LUCA.
DR   OMA; MKAASSE; -.
DR   OrthoDB; EOG66TG3S; -.
DR   BioCyc; TPAL243276:GC1H-892-MONOMER; -.
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   Gene3D; 3.40.50.720; -; 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; IPR016040; NAD(P)-bd_dom.
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   Complete proteome; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    350       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000145712.
FT   NP_BIND      10     11       NAD. {ECO:0000250|UniProtKB:P00362}.
FT   REGION      161    163       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250|UniProtKB:P00362}.
FT   REGION      222    223       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250|UniProtKB:P00362}.
FT   ACT_SITE    162    162       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P00362}.
FT   BINDING      36     36       NAD. {ECO:0000250|UniProtKB:P00362}.
FT   BINDING      82     82       NAD; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00362}.
FT   BINDING     125    125       NAD. {ECO:0000250|UniProtKB:P00362}.
FT   BINDING     193    193       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250|UniProtKB:P00362}.
FT   BINDING     245    245       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250|UniProtKB:P00362}.
FT   BINDING     331    331       NAD. {ECO:0000250|UniProtKB:P00362}.
FT   SITE        190    190       Activates thiol group during catalysis.
FT                                {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
//
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