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
//