ID   G3PC_CHOCR              Reviewed;         335 AA.
AC   P34920;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-NOV-2008, entry version 54.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE            EC=1.2.1.12;
GN   Name=GAPC;
OS   Chondrus crispus (Carragheen).
OC   Eukaryota; Rhodophyta; Florideophyceae; Gigartinales; Gigartinaceae;
OC   Chondrus.
OX   NCBI_TaxID=2769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Stackhouse;
RX   MEDLINE=94275876; PubMed=8007000; DOI=10.1007/BF00163149;
RA   Liaud M.-F., Valentin C., Martin W., Bouget F.Y., Kloareg B.,
RA   Cerff R.;
RT   "The evolutionary origin of red algae as deduced from the nuclear
RT   genes encoding cytosolic and chloroplast glyceraldehyde-3-phosphate
RT   dehydrogenases from Chondrus crispus.";
RL   J. Mol. Evol. 38:319-327(1994).
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; X73034; CAA51515.1; -; mRNA.
DR   EMBL; X73036; CAA51517.1; -; Genomic_DNA.
DR   PIR; S43339; S43339.
DR   HSSP; P56649; 1CRW.
DR   SMR; P34920; 5-334.
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    335       Glyceraldehyde-3-phosphate dehydrogenase,
FT                                cytosolic.
FT                                /FTId=PRO_0000145597.
FT   NP_BIND      13     14       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      35     35       NAD (By similarity).
FT   BINDING      80     80       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   CONFLICT    250    250       A -> T (in Ref. 1; CAA51517).
SQ   SEQUENCE   335 AA;  36054 MW;  B09241EF399D397C CRC64;
     MTAPKVGING FGRIGRLVLR AAIEKGTCQV VAINDPFIDL DYMAYMLKYD STHGRYAGDV
     SIKDGKLQVD GNSITVFAHR DPAEIPWATA AADYIVEATG VFTLKDKAAA HFKGGAKKVV
     ISAPSKDAPM FVCGVNEAKY TPDLDIISNA SCTTNCLAPL VKVIHEKYGI EEGLMTTVHA
     TTATQKTVDG PSNKDWRGGR GRGRNIIPSS TGAAKAVGKV MPELNGKLTG MAFRVPTPDV
     SVVDLTVRLA SETTYEDIKA TMKAAADDSM KGIMKYTEDA VVSTDFIHDD ASCIFDASAG
     IMLNSKFCKL VAWYDNEWGY SNRVVDLIAH ISKVQ
//