ID D7KXK5_ARALL Unreviewed; 882 AA.
AC D7KXK5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
GN ORFNames=ARALYDRAFT_339218 {ECO:0000313|EMBL:EFH65000.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; GL348714; EFH65000.1; -; Genomic_DNA.
DR RefSeq; XP_002888741.1; XM_002888695.1.
DR AlphaFoldDB; D7KXK5; -.
DR STRING; 81972.D7KXK5; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_2001317; fgenesh1_pg.C_scaffold_2001317; fgenesh1_pg.C_scaffold_2001317.
DR Gramene; fgenesh1_pg.C_scaffold_2001317; fgenesh1_pg.C_scaffold_2001317; fgenesh1_pg.C_scaffold_2001317.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_018421_0_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR012850; A-amylase_bs_C.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF33; ALPHA-AMYLASE 3, CHLOROPLASTIC; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00810; Alpha-amyl_C2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 491..820
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 821..881
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT REGION 244..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 99115 MW; A1A0CCDEE30C869B CRC64;
MSTVPIESLL HHSHLRDNSK IYRGTRSFFI PCSLNLPSHF TSNKLLHSIR TSVGASSKHR
RSVAIRASSS DTAVVETAQS DDVIFKENFP VQRIEKAQGK IYVRLKQVKE KNWELSVGSS
IPGKWILHWG VSYVGDTGSE WDQPPEDMRP PGSIAIKDYA IETPLKKLSE GDSFFEVAIN
LNLESSVAAL NFVLKDEETG AWYQHKGRDF KVPLVDDVPD NGNLIGAKKG FGAIGQLSNI
PLKQDESSAE VKKKSKSSSD STKERKGLQE FYEEMPISKR VADDNSVSVT ARKCSETSKN
IVSIETDLPG DVTVHWGVCK NGSKKWEIPS EPYPEDTSLF KNKALRTRLQ RKDDGNGSFG
LFSLDGNLEG GEDFYVPFLT SSSSLVGTEA TEAAQLSKHT PKTDKEVSAS GFTDEIITEI
RNLAIDIHSH KNQKTNVKEV QENILQEIEK LAAEAYSIFR STTPTFSEES ILAEAEKPDI
KISSGTGSGF EILCQGFNWE SHKSGRWYLE LQEKADELAS LGFTVLWLPP PTESVSPEGY
MPKDLYNLNS RYGTIDELKD TVRKFHKVGI KVLGDAVLNH RCAHFKNQNG VWNLFGGRLN
WDDRAVVADD PHFQGRGNKS SGDNFHAAPN IDHSQDFVRK DIKEWLCWMM EEVGYDGWRL
DFVRGFWGGY VKDYMDASKP YFAVGEYWDS LSYTYGEMDY NQDAHRQRIV DWINATSGAT
GAFDVTTKGI LHTALQKCEY WRLSDPKGKP PGVVGWWPSR AVTFIENHDT GSTQGHWRFP
EGKEMQGYAY ILTHPGTPAV FFDHIFSDYH PEIAALLSLR NRQKLHCRSE VNIDKSERDV
YAAIIDDKVA MKIGPGHYEP PNGSKNWSVA VEGRDYKVWE TS
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