LOCUS AEC06945.2 389 aa PRT PLN 23-MAR-2023 DEFINITION Arabidopsis thaliana Putative N-acetyl-gamma-glutamyl- phosphate reductase protein. ACCESSION CP002685-2109 PROTEIN_ID AEC06945.2 SOURCE Arabidopsis thaliana (thale cress) ORGANISM Arabidopsis thaliana Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. REFERENCE 1 (bases 1 to 19698289) AUTHORS Lin,X., Kaul,S., Rounsley,S., Shea,T.P., Benito,M.I., Town,C.D., Fujii,C.Y., Mason,T., Bowman,C.L., Barnstead,M., Feldblyum,T.V., Buell,C.R., Ketchum,K.A., Lee,J., Ronning,C.M., Koo,H.L., Moffat,K.S., Cronin,L.A., Shen,M., Pai,G., Van Aken,S., Umayam,L., Tallon,L.J., Gill,J.E., Adams,M.D., Carrera,A.J., Creasy,T.H., Goodman,H.M., Somerville,C.R., Copenhaver,G.P., Preuss,D., Nierman,W.C., White,O., Eisen,J.A., Salzberg,S.L., Fraser,C.M. and Venter,J.C. TITLE Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana JOURNAL Nature 402 (6763), 761-768 (1999) PUBMED 10617197 REFERENCE 2 (bases 1 to 19698289) AUTHORS Swarbreck,D., Lamesch,P., Wilks,C. and Huala,E. CONSRTM TAIR TITLE Direct Submission JOURNAL Submitted (18-FEB-2011) Department of Plant Biology, Carnegie Institution, 260 Panama Street, Stanford, CA, USA REFERENCE 3 (bases 1 to 19698289) AUTHORS Krishnakumar,V., Cheng,C.-Y., Chan,A.P., Schobel,S., Kim,M., Ferlanti,E.S., Belyaeva,I., Rosen,B.D., Micklem,G., Miller,J.R., Vaughn,M. and Town,C.D. TITLE Direct Submission JOURNAL Submitted (17-MAY-2016) Plant Genomics, J. Craig Venter Institute, 9704 Medical Center Dr, Rockville, MD 20850, USA REMARK Protein update by submitter FEATURES Qualifiers source /organism="Arabidopsis thaliana" /mol_type="genomic DNA" /db_xref="taxon:3702" /chromosome="2" /ecotype="Columbia" protein /locus_tag="AT2G19940" /gene_synonym="F6F22.3" /gene_synonym="F6F22_3" /inference="similar to RNA sequence, EST:INSD:DR348610.1,INSD:DR348609.1,INSD:AA721836.1, INSD:AV558790.1,INSD:EL125815.1,INSD:EH913251.1, INSD:AV533125.1,INSD:EH947644.1,INSD:AV565770.1, INSD:AV541134.1,INSD:AV524449.1,INSD:AV540497.1, INSD:EL201570.1,INSD:BP664004.1,INSD:EH953478.1, INSD:DR381227.1,INSD:BP849990.1,INSD:EL184043.1, INSD:AV551931.1,INSD:BX837930.1,INSD:EH807007.1, INSD:AV816353.1,INSD:EH911852.1,INSD:ES035377.1, INSD:EL201027.1,INSD:DR348608.1,INSD:BP798909.1, INSD:ES007320.1,INSD:BP597966.1,INSD:EL330459.1, INSD:AV828652.1,INSD:DR348611.1,INSD:EL157278.1, INSD:AV558125.1,INSD:AV802293.1,INSD:BP807670.1, INSD:EL989198.1,INSD:AV518727.1,INSD:BP810902.1, INSD:AV439907.1" /inference="similar to RNA sequence, mRNA:INSD:AY058082.1,INSD:AY090309.1,INSD:BX820669.1, INSD:BX820214.1,INSD:BX819415.1" /note="oxidoreductases, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor;copper ion binding; FUNCTIONS IN: oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor, copper ion binding; INVOLVED IN: response to cadmium ion, cellular amino acid metabolic process; LOCATED IN: nucleolus, chloroplast stroma, chloroplast, membrane; EXPRESSED IN: 25 plant structures; EXPRESSED DURING: 14 growth stages; CONTAINS InterPro DOMAIN/s: Semialdehyde dehydrogenase, dimerisation domain (InterPro:IPR012280), Semialdehyde dehydrogenase, NAD-binding (InterPro:IPR000534), N-acetyl-gamma-glutamyl-phosphate reductase (InterPro:IPR000706); Has 8034 Blast hits to 8033 proteins in 2187 species: Archae - 385; Bacteria - 4804; Metazoa - 0; Fungi - 163; Plants - 77; Viruses - 0; Other Eukaryotes - 2605 (source: NCBI BLink)." /db_xref="Araport:AT2G19940" /db_xref="TAIR:AT2G19940" intron_pos 5:1 (1/12) intron_pos 62:0 (2/12) intron_pos 98:0 (3/12) intron_pos 127:0 (4/12) intron_pos 144:0 (5/12) intron_pos 168:0 (6/12) intron_pos 208:0 (7/12) intron_pos 228:1 (8/12) intron_pos 255:1 (9/12) intron_pos 282:0 (10/12) intron_pos 312:0 (11/12) intron_pos 355:0 (12/12) BEGIN 1 MLVQGRKENC VADKRAKRLT LGSHVASPSS MSFRVSASSS VKPEKDIRIG LLGASGYTGA 61 EIVRLLANHP HFQVTLMTAD RKAGQSMESV FPHLRAQKLP TLVSVKDADF STVDAVFCCL 121 PHGTTQEIIK ELPTALKIVD LSADFRLRNI AEYEEWYGQP HKAVELQKEV VYGLTEILRE 181 DIKKARLVAN PGCYPTTIQL PLVPLLKANL IKHENIIIDA KSGVSGAGRG AKEANLYSEI 241 AEGISSYGVT RHRHVPEIEQ GLSDVAQSKV TVSFTPHLMP MIRGMQSTIY VEMAPGVRTE 301 DLHQQLKTSY EDEEFVKVLD EGVVPRTHNV RGSNYCHMSV FPDRIPGRAI IISVIDNLVK 361 GASGQALQNL NIMLGYPETT GLLHQPLFP //