ID GAPN_ARATH Reviewed; 496 AA. AC Q1WIQ6; Q9ZUG8; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 2. DT 16-JUN-2009, entry version 26. DE RecName: Full=NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; DE EC=1.2.1.9; DE AltName: Full=Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase [NADP+]; DE AltName: Full=Triosephosphate dehydrogenase; DE AltName: Full=Aldehyde dehydrogenase family 11 member A3; GN Name=ALDH11A3; Synonyms=GAPN; OrderedLocusNames=At2g24270; GN ORFNames=F27D4.18; 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 [MRNA]. RC STRAIN=cv. Columbia; RA Rius S.P., Iglesias A.A., Gomez-Casati D.F.; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [3] 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 [4] RP NOMENCLATURE. RX PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004; RA Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.; RT "The ALDH gene superfamily of Arabidopsis."; RL Trends Plant Sci. 9:371-377(2004). CC -!- FUNCTION: Important as a means of generating NADPH for CC biosynthetic reactions. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O CC = 3-phospho-D-glycerate + NADPH. CC -!- INTERACTION: CC Q42403:TRX3; NbExp=1; IntAct=EBI-449197, EBI-449157; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ268762; ABB83822.1; -; mRNA. DR EMBL; AC005967; AAD03388.1; -; Genomic_DNA. DR EMBL; AY037205; AAK59790.1; -; mRNA. DR EMBL; AY136409; AAM97075.1; -; mRNA. DR EMBL; BT004551; AAO42797.1; -; mRNA. DR IPI; IPI00530233; -. DR PIR; F84634; F84634. DR RefSeq; NP_180004.1; -. DR RefSeq; NP_973526.1; -. DR UniGene; At.22354; -. DR HSSP; Q59931; 1EUH. DR IntAct; Q1WIQ6; 1. DR PRIDE; Q1WIQ6; -. DR GeneID; 816962; -. DR GenomeReviews; CT485783_GR; AT2G24270. DR KEGG; ath:AT2G24270; -. DR NMPDR; fig|3702.1.peg.9449; -. DR TAIR; At2g24270; -. DR OMA; Q1WIQ6; SRPKATV. DR BioCyc; MetaCyc:AT2G24270-MON; -. DR BRENDA; 1.2.1.9; 302. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (N...; IDA:TAIR. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase. FT CHAIN 1 496 NADP-dependent glyceraldehyde-3-phosphate FT dehydrogenase. FT /FTId=PRO_0000256066. FT NP_BIND 245 249 NAD (By similarity). FT REGION 169 170 Substrate binding (By similarity). FT REGION 297 299 Substrate binding (By similarity). FT ACT_SITE 264 264 Proton acceptor (By similarity). FT ACT_SITE 298 298 Nucleophile (By similarity). FT BINDING 116 116 Substrate (By similarity). FT BINDING 192 192 NADP (By similarity). FT BINDING 195 195 NADP (By similarity). FT BINDING 230 230 NADP (By similarity). FT BINDING 391 391 NADP (By similarity). FT BINDING 451 451 Substrate (By similarity). FT SITE 169 169 Transition state stabilizer (By FT similarity). FT CONFLICT 47 47 V -> A (in Ref. 1; ABB83822). FT CONFLICT 56 56 N -> Y (in Ref. 1; ABB83822). SQ SEQUENCE 496 AA; 53060 MW; 9231656A951175D5 CRC64; MAGTGLFAEI LDGEVYKYYA DGEWKTSSSG KSVAIMNPAT RKTQYKVQAC TQEEVNAVME LAKSAQKSWA KTPLWKRAEL LHKAAAILKD NKAPMAESLV KEIAKPAKDS VTEVVRSGDL ISYCAEEGVR ILGEGKFLLS DSFPGNDRTK YCLTSKIPLG VVLAIPPFNY PVNLAVSKIA PALIAGNSLV LKPPTQGAVS CLHMVHCFHL AGFPKGLISC ITGKGSEIGD FLTMHPAVNC ISFTGGDTGI SISKKAGMIP LQMELGGKDA CIVLDDADLD LVASNIIKGG FSYSGQRCTA VKVVLVMESV ADELVEKVKA KVAKLTVGPP EENSDITAVV SESSANFIEG LVMDAKEKGA TFCQEYKREG NLIWPLLLDN VRPDMRIAWE EPFGPVVPVL RINSVEEGIN HCNASNFGLQ GCVFTKDINK AILISDAMET GTVQINSAPA RGPDHFPFQG LKDSGIGSQG VTNSINLMTK VKTTVINLPT PSYSMG //