ID G3P_KLEPN Reviewed; 303 AA.
AC P24164;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-APR-2013, entry version 85.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
DE Flags: Fragment;
GN Name=gap;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 /
RC NCTC 9633;
RX PubMed=1862091; DOI=10.1073/pnas.88.15.6667;
RA Nelson K., Whittam T.S., Selander R.K.;
RT "Nucleotide polymorphism and evolution in the glyceraldehyde-3-
RT phosphate dehydrogenase gene (gapA) in natural populations of
RT Salmonella and Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6667-6671(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-303.
RC STRAIN=LD119;
RX PubMed=1955870;
RA Lawrence J.G., Ochman H., Hartl D.L.;
RT "Molecular and evolutionary relationships among enteric bacteria.";
RL J. Gen. Microbiol. 137:1911-1921(1991).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC dehydrogenase family.
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DR EMBL; M66869; AAA25069.1; ALT_TERM; Genomic_DNA.
DR EMBL; M63371; AAA25068.1; -; Genomic_DNA.
DR ProteinModelPortal; P24164; -.
DR SMR; P24164; 1-303.
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 Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT CHAIN <1 >303 Glyceraldehyde-3-phosphate dehydrogenase.
FT /FTId=PRO_0000145664.
FT NP_BIND 6 7 NAD (By similarity).
FT REGION 143 145 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT REGION 203 204 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT ACT_SITE 144 144 Nucleophile (By similarity).
FT BINDING 28 28 NAD (By similarity).
FT BINDING 72 72 NAD; via carbonyl oxygen (By similarity).
FT BINDING 174 174 Glyceraldehyde 3-phosphate (By
FT similarity).
FT BINDING 226 226 Glyceraldehyde 3-phosphate (By
FT similarity).
FT SITE 171 171 Activates thiol group during catalysis
FT (By similarity).
FT NON_TER 1 1
FT NON_TER 303 303
SQ SEQUENCE 303 AA; 32306 MW; 327B18AC56E39B2B CRC64;
INGFGRIGRI VFRAAQKRSD IEIVAINDLL DAEYMAYMLK YDSTHGRFDG TVEVKDGHLV
VNGKKIRVTA ERDPANLKWD EVGVDVVAEA TGIFLTDETA RKHITAGAKK VVLTGPSKDN
TPMFVRGANF DAYAGQDIVS NASCTTNCLA PLAKVINDNF GIVEGLMTTV HATTATQKTV
DGPSHKDWRG GRGAAQNIIP SSTGAAKAVG KVLPELNGKL TGMAFRVPTP NVSVVDLTVR
LEKAASYEEI KKAIKAASEG AMKGVLGYTE DDVVSTDFNG EVCTSVFDAK AGIALNDNFV
KLV
//
