ID C5X2B1_SORBI Unreviewed; 437 AA.
AC C5X2B1;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 95.
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=SORBI_3002G225600 {ECO:0000313|EMBL:EER96852.1},
GN SORBI_3002G225650 {ECO:0000313|EMBL:EER96853.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER96852.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER96852.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|EMBL:EER96852.1}
RP NUCLEOTIDE SEQUENCE.
RA Paterson A., Mullet J., Bowers J., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A., Chapman J., Feltus F.,
RA Gowik U., Grigoriev I., Lyons E., Maher C., Martis M., Narechania A.,
RA Otillar R., Penning B., Salamov A., Wang Y., Zhang L., Carpita N.,
RA Freeling M., Gingle A., Hash C., Keller B., Klein P., Kresovich S.,
RA Mccann M., Ming R., Peterson D., Rahman M., Ware D., Westhoff P., Mayer K.,
RA Messing J., Sims D., Jenkins J., Shu S., Rokhsar D.;
RT "WGS assembly of Sorghum bicolor.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR001028,
CC ECO:0000256|RuleBase:RU003615}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000761; EER96852.1; -; Genomic_DNA.
DR EMBL; CM000761; EER96853.1; -; Genomic_DNA.
DR RefSeq; XP_002460331.1; XM_002460286.1.
DR RefSeq; XP_002460332.1; XM_002460287.1.
DR AlphaFoldDB; C5X2B1; -.
DR SMR; C5X2B1; -.
DR STRING; 4558.C5X2B1; -.
DR EnsemblPlants; EER96852; EER96852; SORBI_3002G225600.
DR EnsemblPlants; EER96853; EER96853; SORBI_3002G225650.
DR GeneID; 8063704; -.
DR GeneID; 8083215; -.
DR Gramene; EER96852; EER96852; SORBI_3002G225600.
DR Gramene; EER96853; EER96853; SORBI_3002G225650.
DR KEGG; sbi:8063704; -.
DR KEGG; sbi:8083215; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_030069_1_0_1; -.
DR InParanoid; C5X2B1; -.
DR OrthoDB; 201664at2759; -.
DR Proteomes; UP000000768; Chromosome 2.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
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:SF48; ALPHA-AMYLASE ISOZYME 3C; 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 3: Inferred from homology;
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:UP000000768};
KW Signal {ECO:0000256|PIRNR:PIRNR001028}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT CHAIN 27..437
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT /id="PRO_5010897875"
FT DOMAIN 27..371
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 366..426
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ SEQUENCE 437 AA; 47932 MW; D5A25C9EF4A9C615 CRC64;
MAKHSAAMCS LLVLVLLCLG SQLVQSQVLF QGFNWESCKK QGGWYNYLRG QVDDIAATGA
THVWLPPPSH SVAPQGYMPG RLYDLDASKY GTHAELKSLI AAFHAKGVQC VADVVINHRC
ADYKDSRGIY CIFEGGTPDS RLDWGPDMIC SDDTQYSNGR GHRDTGADFG AAPDIDHLNP
RVQEELSGWL NWLKSDLGFD GWRLDFAKGY SAAVAKVYVD NTAPTFVVAE IWSSLHYDGN
GEPSNNQDAD RQELVNWAQA VGGPAAAFDF TTKGVLQAAV QGELWRMKDG NGKAPGMIGW
LPEKAVTFVD NHDTGSTQNS WPFPSDKVMQ GYAYILTHPG TPCIFYDHVF DWNLKQEISA
LSAVRSRNGI HPGSKLNILA ADGDLYVAKI DDKVIVKIGS RYDVGNLIPS DFHAVAHGNN
YCVWEKSGLR VPAGRHH
//
