ID Q7X9T1_PHAAN Unreviewed; 421 AA.
AC Q7X9T1;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 115.
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|PIRNR:PIRNR001028};
GN ORFNames=HKW66_Vig0202320 {ECO:0000313|EMBL:KAG2380859.1},
GN LR48_Vigan11g120700 {ECO:0000313|EMBL:KOM58173.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:BAC76729.1};
RN [1] {ECO:0000313|EMBL:BAC76729.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cotyledon {ECO:0000313|EMBL:BAC76729.1};
RX PubMed=12834286; DOI=10.1271/bbb.67.1080;
RA Mar S.S., Mori H., Lee J.H., Fukuda K., Saburi W., Fukuhara A., Okuyama M.,
RA Chiba S., Kimura A.;
RT "Purification, characterization, and sequence analysis of two alpha-amylase
RT isoforms from azuki bean, Vigna angularis, showing different affinity
RT towards beta-cyclodextrin sepharose.";
RL Biosci. Biotechnol. Biochem. 67:1080-1093(2003).
RN [2] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [3] {ECO:0000313|EMBL:KOM58173.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM58173.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAG2380859.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2380859.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|PIRNR:PIRNR001028, ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR001028};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR001028,
CC ECO:0000256|RuleBase:RU003615}.
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DR EMBL; AB096198; BAC76729.1; -; mRNA.
DR EMBL; JABFOF010000009; KAG2380859.1; -; Genomic_DNA.
DR EMBL; CM003381; KOM58173.1; -; Genomic_DNA.
DR RefSeq; NP_001316768.1; NM_001329839.1.
DR AlphaFoldDB; Q7X9T1; -.
DR SMR; Q7X9T1; -.
DR STRING; 3914.Q7X9T1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblPlants; KOM58173; KOM58173; LR48_Vigan11g120700.
DR GeneID; 108346293; -.
DR Gramene; KOM58173; KOM58173; LR48_Vigan11g120700.
DR KEGG; var:108346293; -.
DR OMA; CVVIMSN; -.
DR OrthoDB; 201664at2759; -.
DR SABIO-RK; Q7X9T1; -.
DR Proteomes; UP000053144; Chromosome 11.
DR Proteomes; UP000743370; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; 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:SF37; ALPHA-AMYLASE 1; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001028; Alph-amls_plant; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
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 Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Signal {ECO:0000256|PIRNR:PIRNR001028}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT CHAIN 27..421
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT /id="PRO_5015024080"
FT DOMAIN 24..361
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 362..421
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT ACT_SITE 226
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ SEQUENCE 421 AA; 46882 MW; 53B253B70BDB8779 CRC64;
MDSFSRLSIF CLFISLLPLF SSPALLFQGF NWESSKKGGW YNSLKNSIPD LANAGITHVW
LPPPSQSVSP EGYLPGRLYD LDASRYGSKN ELKSLIAAFY EKGIKCLADI VINHRTAERK
DGRGIYCIFE GGTPDSRLDW GPSFICRDDT AYSDGTGNND SGEGYDAAPD IDHLNPQVQR
ELSEWMNWLK TEIGFDGWRF DFVKGYAPSI SKIYMEQTRP DFAVGEKWDS LSSGQDGKPN
YNQDSHRGAL VNWVESAGGA ITAFDFTTKG ILQAAVQGEL WRLIDPNGKP PGMIGVKPEN
AVTFIDNHDT GSTQRLWPFP SDKVMQGYAY ILTHPGTPSI FYDHFFDWGL KEQIAKLSSI
RVRNGINEKS TVKILASEGD LYVAKIDNKI MVKIGPKMDL GNLIPSNFHV ATSGQDYAVW
E
//
