ID A0A0E0QK76_ORYRU Unreviewed; 984 AA.
AC A0A0E0QK76;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI08G20030.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI08G20030.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Important for breakdown of endosperm starch during
CC germination. {ECO:0000256|ARBA:ARBA00002195}.
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|ARBA:ARBA00000548};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR AlphaFoldDB; A0A0E0QK76; -.
DR STRING; 4529.A0A0E0QK76; -.
DR EnsemblPlants; ORUFI08G20030.1; ORUFI08G20030.1; ORUFI08G20030.
DR Gramene; ORUFI08G20030.1; ORUFI08G20030.1; ORUFI08G20030.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_004203_0_0_1; -.
DR OMA; MYIENCK; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProt.
DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR012850; A-amylase_bs_C.
DR InterPro; IPR006046; Alpha_amylase.
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:SF40; ALPHA-AMYLASE ISOZYME 3D; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 2.
DR Pfam; PF00128; Alpha-amylase; 2.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 2.
DR SMART; SM00810; Alpha-amyl_C2; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..984
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002371300"
FT DOMAIN 26..370
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 365..425
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT DOMAIN 574..912
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 913..973
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
SQ SEQUENCE 984 AA; 108665 MW; D938176D47FBCCBB CRC64;
MGKHHVTLCC VVFAVLCLAS SLAQAQVLFQ GFNWESWRKQ GGWYNFLHEK VEEIASTGAT
HVWLPPPSHS VSPQGYMPGR LYDLDASKYG TEAELKSLIE AFHDKNVECL ADIVINHRCA
DYKDSRGVYC VFEGGTPDGR LDWGPDMICS DDTQYSNGRG HRDTGAGFGA APDIDHLNPR
VQRELTDWLN WLRTDLGFDG WRLDFAKGYS APLARIYVDN TNPTFVVGEI WSSLIYNGDG
KPSTNQDADR QELVNWVEGV GKPATAFDFT TKGILQAAVQ GELWRLHDGN GKAPGLMGWM
PDQAVTFVDN HDTGSTQSLW PFPSDKVMQG YAYILTHPGI PCIFYDHVFD WNLQHEIATL
AEIRSRNGIH AESTLDILKA EGDIYVAMID SKVITKLGPR YDAGGIIPSD FHVVAHGNDY
CVWEKEGLRW MVAVERQSTT EGEDNGGGFR VRRLGQRGRR MCAPLQATRK RGDVDLGKGD
DSPHWLSTLS SSPARHAVAA AASSPPLSFP NADLVIRHEH IDQPSSTRDR SVVVSSNSLS
NTVSAYTDMK NTSSLCLLLL VVLCSLTCNS GQAQVLFQGF NWESWKQQGG WYNMLKGQVD
DIAKAGVTHV WLPPPSHSVA PQGYMPGRLY DLDASKYGTA AELKSLIAAF HGKGVQCVAD
VVINHRCAEK KDARGVYCVF EGGTPDDRLD WGPGMICSDD TQYSDGTGHR DTGEGFGAAP
DIDHLNPRVQ RELTDWLNWL KSDVGFDGWR LDFAKGYSTD IAKMYVESCK PGFVVAEIWN
SLSYNGDGKP AANQDQGRQE LVNWVNAVGG PAMTFDFTTK GLLQAGVQGE LWRLRDGNGK
AAGMIGWLPE KAVTFVDNHD TGSTQKLWPF PSDKVMQGYA YILTHPGVPC IFYDHMFDWN
LKQEITALAA IRERNGINAG SKLRIVVADA DAYVAVVDEK VMVKIGTRYD VGNAVPSDFH
QTVHGKDYCV WEKGSLRVPA GRHL
//
