ID   G3PC_ARATH              Reviewed;         338 AA.
AC   P25858; Q42352; Q9M8W8;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   25-NOV-2008, entry version 76.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
DE            EC=1.2.1.12;
GN   Name=GAPC; OrderedLocusNames=At3g04120; ORFNames=T6K12.26;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=92009205; PubMed=1916285; DOI=10.1016/0378-1119(91)90242-4;
RA   Shih M.-C., Heinrich P., Goodman H.M.;
RT   "Cloning and chromosomal mapping of nuclear genes encoding chloroplast
RT   and cytosolic glyceraldehyde-3-phosphate-dehydrogenase from
RT   Arabidopsis thaliana.";
RL   Gene 104:133-138(1991).
RN   [2]
RP   ERRATUM.
RX   MEDLINE=93013005; PubMed=1398114; DOI=10.1016/0378-1119(92)90290-6;
RA   Shih M.-C., Heinrich P., Goodman H.M.;
RL   Gene 119:317-319(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-321.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=96158348; PubMed=8580968;
RX   DOI=10.1046/j.1365-313X.1996.09010101.x;
RA   Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA   Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA   Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y.,
RA   Marbach J., Fleck J., Clement B., Philipps G., Herve C., Bardet C.,
RA   Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F.,
RA   Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H.,
RA   Hoefte H.;
RT   "Further progress towards a catalogue of all Arabidopsis genes:
RT   analysis of a set of 5000 non-redundant ESTs.";
RL   Plant J. 9:101-124(1996).
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; M64116; AAA32794.1; -; mRNA.
DR   EMBL; M64119; AAA32796.1; -; Genomic_DNA.
DR   EMBL; AC016829; AAF26801.1; -; Genomic_DNA.
DR   EMBL; AY052267; AAK97737.1; -; mRNA.
DR   EMBL; AY060521; AAL31134.1; -; mRNA.
DR   EMBL; AY140084; AAM98225.1; -; mRNA.
DR   EMBL; F20074; CAA23391.1; -; mRNA.
DR   PIR; JQ1287; JQ1287.
DR   RefSeq; NP_187062.1; -.
DR   UniGene; At.22963; -.
DR   HSSP; P00357; 4GPD.
DR   GeneID; 819567; -.
DR   GenomeReviews; BA000014_GR; AT3G04120.
DR   KEGG; ath:AT3G04120; -.
DR   TAIR; At3g04120; -.
DR   ArrayExpress; P25858; -.
DR   GermOnline; AT3G04120; Arabidopsis thaliana.
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   Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN         1    338       Glyceraldehyde-3-phosphate dehydrogenase,
FT                                cytosolic.
FT                                /FTId=PRO_0000145594.
FT   NP_BIND      15     16       NAD (By similarity).
FT   REGION      155    157       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      215    216       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    156    156       Nucleophile (By similarity).
FT   BINDING      37     37       NAD (By similarity).
FT   BINDING      84     84       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     186    186       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     238    238       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     320    320       NAD (By similarity).
FT   SITE        183    183       Activates thiol group during catalysis
FT                                (By similarity).
FT   CONFLICT    127    127       A -> E (in Ref. 1; AAA32794/AAA32796).
FT   CONFLICT    260    260       D -> E (in Ref. 1; AAA32794/AAA32796).
SQ   SEQUENCE   338 AA;  36914 MW;  4186F65E1F1EE96F CRC64;
     MADKKIRIGI NGFGRIGRLV ARVVLQRDDV ELVAVNDPFI TTEYMTYMFK YDSVHGQWKH
     NELKIKDEKT LLFGEKPVTV FGIRNPEDIP WAEAGADYVV ESTGVFTDKD KAAAHLKGGA
     KKVVISAPSK DAPMFVVGVN EHEYKSDLDI VSNASCTTNC LAPLAKVIND RFGIVEGLMT
     TVHSITATQK TVDGPSMKDW RGGRAASFNI IPSSTGAAKA VGKVLPALNG KLTGMSFRVP
     TVDVSVVDLT VRLEKAATYD EIKKAIKEES EGKLKGILGY TEDDVVSTDF VGDNRSSIFD
     AKAGIALSDK FVKLVSWYDN EWGYSSRVVD LIVHMSKA
//