ID C3W8N1_HORVV Unreviewed; 415 AA.
AC C3W8N1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238, ECO:0000256|PIRNR:PIRNR001028};
GN Name=AMY4 {ECO:0000313|EMBL:CAX51375.1};
OS Hordeum vulgare subsp. vulgare (Domesticated barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=112509 {ECO:0000313|EMBL:CAX51375.1};
RN [1] {ECO:0000313|EMBL:CAX51375.1}
RP NUCLEOTIDE SEQUENCE.
RA Radchuk V.V., Borisjuk L., Sreenivasulu N., Merx K., Mock H.P.,
RA Rolletschek H., Wobus U., Weschke W.;
RT "SPATIO-TEMPORAL PROFILING OF STARCH BIOSYNTHESIS AND DEGRADATION IN THE
RT DEVELOPING BARLEY GRAIN.";
RL Plant Physiol. 150:190-204(2009).
RN [2] {ECO:0000313|Proteomes:UP000011116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX PubMed=23075845; DOI=10.1038/nature11543;
RG The International Barley Genome Sequencing Consortium;
RA Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT "A physical, genetic and functional sequence assembly of the barley
RT genome.";
RL Nature 491:711-716(2012).
RN [3] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0164800.1}
RP IDENTIFICATION.
RC STRAIN=subsp. vulgare
RC {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0164800.1};
RG EnsemblPlants;
RL Submitted (JAN-2022) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|PIRNR:PIRNR001028};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR001028};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR001028}.
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DR EMBL; FN179392; CAX51375.1; -; mRNA.
DR AlphaFoldDB; C3W8N1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; 4513-MLOC_63781-2; -.
DR EnsemblPlants; HORVU.MOREX.r3.2HG0164800.1; HORVU.MOREX.r3.2HG0164800.1; HORVU.MOREX.r3.2HG0164800.
DR Gramene; HORVU.MOREX.r2.2HG0135830.1; HORVU.MOREX.r2.2HG0135830.1; HORVU.MOREX.r2.2HG0135830.
DR Gramene; HORVU.MOREX.r3.2HG0164800.1; HORVU.MOREX.r3.2HG0164800.1; HORVU.MOREX.r3.2HG0164800.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_030069_1_0_1; -.
DR OMA; MQYFEWN; -.
DR OrthoDB; 201664at2759; -.
DR Proteomes; UP000011116; Chromosome 2H.
DR ExpressionAtlas; C3W8N1; baseline and differential.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProt.
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; IPR013775; A-amylase_pln.
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:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001028; Alph-amls_plant; 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 2: Evidence at transcript level;
KW Germination {ECO:0000256|ARBA:ARBA00022544};
KW Glycosidase {ECO:0000313|EMBL:CAX51375.1};
KW Hydrolase {ECO:0000313|EMBL:CAX51375.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011116}.
FT DOMAIN 26..368
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 357..415
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ SEQUENCE 415 AA; 47215 MW; 5716179C5A673B3A CRC64;
MGQMVSDGVV QEQAARNVGI IKNGREILLQ AFNWESHKHN WWSNLEGRVA DIAKSGFTSA
WLPPPTQSLS PEGYLPQNLY SLDSCYGSLQ QLNSLIQNMN DHNIRAMADV VINHRVGTTK
GLNGMYNRYD GIPISWDEHA VTSCSGGKGN KSTGDNFDGV PNIDHTQPFV RKDIIEWLIW
LRETIGFQDF RFDFTKGYAS KFVKEYIEES KPLFAVGEYW DSCEYAPPDN HLSYNQDKHR
QRIINWIDST GGLCAAFDFT TKGILQEAVK GELWRLRDPE EKPPGVMGWW PSRSVTFIEN
HDTGSTQGHW PFPPDHVMEG YAYILTHPGI PTVFYDHFFD WGDSFHDEIA KLMEIRKSQD
IHSRSAVKIL EASSNLYSAI IDDKLCMKIG EGSWCPSGPE WKLAACGDRY AVWHK
//
