LOCUS AEC10364.1 347 aa PRT PLN 23-MAR-2023
DEFINITION Arabidopsis thaliana Dihydrodipicolinate reductase, bacterial/
plant protein.
ACCESSION CP002685-6802
PROTEIN_ID AEC10364.1
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="AT2G44040"
/gene_synonym="F6E13.17"
/inference="Similar to RNA sequence,
EST:INSD:DR222706.1,INSD:CB262930.1,INSD:BX840842.1,
INSD:EH917822.1,INSD:DR222708.1,INSD:EH922765.1,
INSD:DR222710.1,INSD:AV796612.1,INSD:DR222711.1,
INSD:EL033855.1,INSD:EL288865.1,INSD:EL041936.1,
INSD:EL329316.1,INSD:DR222709.1,INSD:EH831164.1,
INSD:EH811428.1,INSD:AU231064.1,INSD:EL231603.1,
INSD:EL310998.1,INSD:AV802464.1,INSD:DR222707.1,
INSD:EL209061.1,INSD:ES198669.1,INSD:EH913383.1,
INSD:EH886116.1,INSD:AV820286.1,INSD:BP798182.1,
INSD:EL110542.1,INSD:ES173050.1,INSD:EH961229.1,
INSD:EL071052.1,INSD:DR222712.1,INSD:EH966724.1,
INSD:DR371649.1,INSD:ES164731.1,INSD:ES141351.1,
INSD:EL309154.1"
/inference="similar to RNA sequence,
mRNA:INSD:AK118845.1,INSD:AY084299.1"
/note="Dihydrodipicolinate reductase, bacterial/plant;
FUNCTIONS IN: dihydrodipicolinate reductase activity;
INVOLVED IN: oxidation reduction, lysine biosynthetic
process via diaminopimelate, metabolic process,
diaminopimelate biosynthetic process; LOCATED IN:
chloroplast; EXPRESSED IN: cotyledon; CONTAINS InterPro
DOMAIN/s: Dihydrodipicolinate reductase, C-terminal
(InterPro:IPR022663), NAD(P)-binding domain
(InterPro:IPR016040), Dihydrodipicolinate reductase, plant
(InterPro:IPR011859), Dihydrodipicolinate reductase,
bacterial/plant (InterPro:IPR011770), Dihydrodipicolinate
reductase, N-terminal (InterPro:IPR000846); BEST
Arabidopsis thaliana protein match is: Dihydrodipicolinate
reductase, bacterial/plant (TAIR:AT3G59890.1); Has 3366
Blast hits to 3365 proteins in 1356 species: Archae - 124;
Bacteria - 2714; Metazoa - 2; Fungi - 0; Plants - 79;
Viruses - 0; Other Eukaryotes - 447 (source: NCBI BLink)."
/db_xref="Araport:AT2G44040"
/db_xref="TAIR:AT2G44040"
intron_pos 5:2 (1/8)
intron_pos 77:0 (2/8)
intron_pos 156:1 (3/8)
intron_pos 201:0 (4/8)
intron_pos 226:0 (5/8)
intron_pos 260:0 (6/8)
intron_pos 296:2 (7/8)
intron_pos 326:0 (8/8)
BEGIN
1 MATNGLMASS SVFLHRPRIA FASRTNQTVG KYGKGRVSFM GIGTRRLPVV LSMTAMADSG
61 EEAVKSVLPG NGISIMVNGC SGKMGKAVIK AADSAGVNIV PISFGSAGED GQRVEVCGKE
121 ITVHGPTERE KVLSSVFEKH PELIVVDYTI PSAVNDNAEL YSKVGVPFVM GTTGGDRNKL
181 YETVEEAKIY AVISPQMGKQ VVAFLAAMEI MAEQFPGAFS GYSLDVMESH QASKLDASGT
241 AKAVISCFQE LGVSYDMDQI QLIRDPKQQV EMVGVPEEHI SGHAFHLYHL TSPDETVSFE
301 FQHNVCGRSI YAEGTVDAVL FLAKKIRLKA DQRIYNMIDV LREGNMR
//