LOCUS AEC10601.1 246 aa PRT PLN 23-MAR-2023
DEFINITION Arabidopsis thaliana phosphomannomutase protein.
ACCESSION CP002685-7110
PROTEIN_ID AEC10601.1
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 /gene="PMM"
/locus_tag="AT2G45790"
/gene_synonym="ATPMM"
/gene_synonym="F4I18.23"
/gene_synonym="phosphomannomutase"
/gene_synonym="PHOSPHOMANNOMUTASE"
/inference="Similar to RNA sequence,
EST:INSD:DR370107.1,INSD:ES055566.1,INSD:DR213269.1,
INSD:AV794469.1,INSD:BP657698.1,INSD:DR213268.1,
INSD:EL299693.1,INSD:AI996290.1,INSD:EL203849.1,
INSD:ES085814.1,INSD:EL982283.1,INSD:BP631848.1,
INSD:BP787812.1,INSD:DR213266.1,INSD:AU230146.1,
INSD:EL297604.1,INSD:EL162732.1,INSD:ES083664.1,
INSD:ES149576.1,INSD:BP867302.2,INSD:DR213265.1,
INSD:DR213263.1,INSD:H37387.1,INSD:EH920324.1,
INSD:ES197829.1,INSD:BP564494.1,INSD:ES073817.1,
INSD:AI099998.1,INSD:EL054931.1,INSD:ES059734.1,
INSD:EH862230.1,INSD:EL129510.1,INSD:ES031038.1,
INSD:EH971439.1,INSD:T75806.1,INSD:ES022412.1,
INSD:EH822990.1,INSD:ES166489.1,INSD:ES168728.1,
INSD:EL005957.1,INSD:BP853066.1,INSD:BP843452.1,
INSD:ES032381.1,INSD:BP842429.1,INSD:BP844303.1,
INSD:EL141471.1,INSD:EL983074.1,INSD:ES051954.1,
INSD:BP665736.1,INSD:DR213264.1,INSD:AV826344.1,
INSD:ES128728.1,INSD:ES061258.1,INSD:DR213267.1,
INSD:ES018655.1,INSD:BP624648.1,INSD:CD530405.1,
INSD:AV557122.1,INSD:EH853900.1"
/inference="similar to RNA sequence,
mRNA:INSD:BX819611.1,INSD:DQ442991.1,INSD:AY113964.1,
INSD:AY088930.1,INSD:AY050806.1"
/note="phosphomannomutase (PMM); FUNCTIONS IN: protein
binding, phosphomannomutase activity; INVOLVED IN:
L-ascorbic acid biosynthetic process, response to salt
stress, mannose biosynthetic process; LOCATED IN:
cytoplasm; EXPRESSED IN: 24 plant structures; EXPRESSED
DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s:
Eukaryotic phosphomannomutase (InterPro:IPR005002),
HAD-superfamily hydrolase, subfamily IIB
(InterPro:IPR006379); Has 1083 Blast hits to 1081 proteins
in 282 species: Archae - 1; Bacteria - 92; Metazoa - 201;
Fungi - 171; Plants - 223; Viruses - 0; Other Eukaryotes -
395 (source: NCBI BLink)."
/db_xref="Araport:AT2G45790"
/db_xref="TAIR:AT2G45790"
intron_pos 39:0 (1/9)
intron_pos 61:1 (2/9)
intron_pos 87:0 (3/9)
intron_pos 99:0 (4/9)
intron_pos 117:2 (5/9)
intron_pos 151:0 (6/9)
intron_pos 183:0 (7/9)
intron_pos 213:0 (8/9)
intron_pos 230:1 (9/9)
BEGIN
1 MAAKIPGVIA LFDVDGTLTA PRKEATPELL DFIRELRKVV TIGVVGGSDL SKISEQLGKT
61 VTNDYDYCFS ENGLVAHKDG KSIGIQSLKL HLGDDKLKEL INFTLHYIAD LDIPIKRGTF
121 IEFRNGMLNV SPIGRNCSQE ERDEFERYDK VQNIRPKMVA ELRERFAHLN LTFSIGGQIS
181 FDVFPKGWDK TYCLQYLEDF SEIHFFGDKT YEGGNDYEIY ESPKTIGHSV TSPDDTVAKC
241 KALFMS
//