ID   G3PC_PETCR              Reviewed;         336 AA.
AC   P26519;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE            EC=1.2.1.12;
GN   Name=GAPC; Synonyms=GAPDH;
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae;
OC   apioid superclade; Apium clade; Petroselinum.
OX   NCBI_TaxID=4043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Martin W., Gierl A., Saedler H.;
RT   "Molecular evidence for pre-Cretaceous angiosperm origins.";
RL   Nature 339:46-48(1989).
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   -!- MISCELLANEOUS: Plants contain three forms of GAPDH: a cytosolic
CC       form which participates in glycolysis and two chloroplast forms
CC       which participates in photosynthesis. These three forms are
CC       encoded by distinct genes.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; X60344; CAA42902.1; -; mRNA.
DR   PIR; S18484; DEPZG.
DR   HSSP; P56649; 1IHX.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD 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_DHase.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DHase_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    336       Glyceraldehyde-3-phosphate dehydrogenase,
FT                                cytosolic.
FT                                /FTId=PRO_0000145611.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      152    154       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      212    213       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    153    153       Nucleophile (By similarity).
FT   BINDING      34     34       NAD (By similarity).
FT   BINDING      81     81       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     183    183       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     235    235       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     317    317       NAD (By similarity).
FT   SITE        180    180       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   336 AA;  36372 MW;  9CD52A143AFA2494 CRC64;
     MKMKIGINGF GRIGRLVARV ALMSDDIELV AVNDPFITTE YMTYMFKYDS VHGQWKKDEL
     KVKDSKTLLF GDKPLTVFGV RNPEEDPWGE AGAEYVVEST GVFTDKDKAA AHLKGGAKKV
     VISAPSGNAP MFVVGVNEKE YKKDIDIVSN ASCTTNCLAP LAKVLNDKFG IVEGLMTTVH
     SITATRKTVD GPSMKDWRGG RAASFNIIPS STGAAKAVGK VLPALNGKLT GMAFRVPTVD
     VSVVDLTARL EKAATYDEIK AAIKHESETS LKGILGYTED DVVSTDFVGD SRSSIFDAKA
     GIALNGNFVK VVSWYDNEWG YSNRVIDLIR HMASVA
//