ID   G3P1_GLORO              Reviewed;         324 AA.
AC   O16027;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE            Short=GAPDH-1;
DE            EC=1.2.1.12;
DE   Flags: Fragment;
GN   Name=GPD-1;
OS   Globodera rostochiensis (Golden nematode worm).
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Tylenchida; Tylenchina;
OC   Tylenchoidea; Heteroderidae; Heteroderinae; Globodera.
OX   NCBI_TaxID=31243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Ro1 / Mierenbos;
RX   MEDLINE=99066932; PubMed=9851607; DOI=10.1016/S0166-6851(98)00108-X;
RA   Qin L., Smant G., Stokkermans J.P.W.G., Bakker J., Schots A.,
RA   Helder J.;
RT   "Cloning of a trans-spliced glyceraldehyde-3-phosphate-dehydrogenase
RT   gene from the potato cyst nematode Globodera rostochiensis and
RT   expression of its putative promoter region in Caenorhabditis
RT   elegans.";
RL   Mol. Biochem. Parasitol. 96:59-67(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 (By similarity).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; AF004522; AAC79129.1; -; mRNA.
DR   HSSP; P00354; 3GPD.
DR   SMR; O16027; 3-324.
DR   BRENDA; 1.2.1.12; 288734.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000173; GlycerAld_3-P_DH.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   PANTHER; PTHR10836; GAP_DH; 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   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN         1   >324       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000145516.
FT   NP_BIND      13     14       NAD (By similarity).
FT   REGION      157    159       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      217    218       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    158    158       Nucleophile (By similarity).
FT   BINDING      35     35       NAD (By similarity).
FT   BINDING      85     85       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     188    188       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     240    240       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     322    322       NAD (By similarity).
FT   NON_TER     324    324
SQ   SEQUENCE   324 AA;  34580 MW;  1815C606CBBE1039 CRC64;
     MVKPKVGING FGRIGRLALR AAVEKDTVQV VAINDPFIEL DYMVYMFNYD STHGRFNGKI
     STSAGNLVVE KEGKATHTIK VFNLKDPAEI KWAEVGAEYV IESTGVFTTI EKASAHLKGG
     AKKVVISAPS ADAPMYVMGV NEDKYDPAKD NVISNASCTT NCLAPLAKVI NDEFGIIEGL
     MTTVHAVTAT QKTVDGPNGK QWRDGRGAAQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR
     VPTPNVSVVD LTARLEKPAS LDAIKAAVKK AAEGNLKGIL GYTEDQVVST DFLGDSRSSI
     FDAGACISLN PHFVKLVSWY DNEF
//