ID   G3P1_GIALA              Reviewed;         337 AA.
AC   P53429;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE            Short=GAPDH;
DE            EC=1.2.1.12;
GN   Name=GAP1;
OS   Giardia lamblia (Giardia intestinalis).
OC   Eukaryota; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30957 / WB;
RA   Rozario C., Smith M.W., Muller M.;
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-312.
RC   STRAIN=ATCC 30957 / WB;
RA   Smith M.W., Doolittle R.F.;
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
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; M88062; AAB18421.1; -; Genomic_DNA.
DR   HSSP; P56649; 1CRW.
DR   BRENDA; 1.2.1.12; 322.
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   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
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   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN         1    337       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000145526.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      151    153       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      211    212       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    152    152       Nucleophile (By similarity).
FT   BINDING      34     34       NAD (By similarity).
FT   BINDING      79     79       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     182    182       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     234    234       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     316    316       NAD (By similarity).
FT   SITE        179    179       Activates thiol group during catalysis
FT                                (By similarity).
FT   VARIANT     214    214       A -> P (in strain: ATCC 30957 / WB).
FT   VARIANT     268    268       N -> K (in strain: ATCC 30957 / WB).
SQ   SEQUENCE   337 AA;  36450 MW;  762F1AE90143B462 CRC64;
     MPIRLGINGF GRIGRMALRA SLNIDGVQVV AINDPFTDCE YMEYMLKYDT VHGRFDGTIA
     HSEDSITVNG NKISVFKSMK PEEIPWGKTQ VDIVLECTGR FTTKKDAELH ITGGCKRVII
     SAPSADAPMF VCGCNLETYD PSTMKVISNA SCTTNCLAPL AMVVNKKFGI KEGLMTTVHA
     VTATQLPVDG PSKKDWRGGR SCGANVIPSS TGAAKAVGKV LPALNGKLTG MAFRVPVPDV
     SVVDLTCTLE KDATYDEICA EIKRGSENEL KGIMTYTNED VVSSDFLSTT STCNFDSKAG
     IMLNSRFVKL VAWYDNEFGY ANKLVELAKY VGSKGCQ
//