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 29-MAY-2013, entry version 95.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
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 -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC dehydrogenase family.
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DR EMBL; AE000520; AAC65812.1; -; Genomic_DNA.
DR PIR; D71273; D71273.
DR RefSeq; NP_219280.1; NC_000919.1.
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:TP0844; -.
DR PATRIC; 20531795; VBITrePal57110_0895.
DR eggNOG; COG0057; -.
DR OMA; QDFIGEV; -.
DR ProtClustDB; CLSK793410; -.
DR BioCyc; TPAL243276:GC1H-892-MONOMER; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolysis; 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 TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT CHAIN 1 350 Glyceraldehyde-3-phosphate dehydrogenase.
FT /FTId=PRO_0000145712.
FT NP_BIND 10 11 NAD (By similarity).
FT REGION 161 163 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT REGION 222 223 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT ACT_SITE 162 162 Nucleophile (By similarity).
FT BINDING 36 36 NAD (By similarity).
FT BINDING 193 193 Glyceraldehyde 3-phosphate (By
FT similarity).
FT BINDING 245 245 Glyceraldehyde 3-phosphate (By
FT similarity).
FT BINDING 331 331 NAD (By similarity).
FT SITE 190 190 Activates thiol group during catalysis
FT (By similarity).
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
//
