ID A0A061EY39_THECC Unreviewed; 500 AA.
AC A0A061EY39;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Beta-amylase {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
GN ORFNames=TCM_025391 {ECO:0000313|EMBL:EOY10020.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY10020.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY10020.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides so as to remove successive maltose units from the
CC non-reducing ends of the chains.; EC=3.2.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000546,
CC ECO:0000256|RuleBase:RU000509};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family.
CC {ECO:0000256|ARBA:ARBA00005652, ECO:0000256|RuleBase:RU000509}.
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DR EMBL; CM001883; EOY10020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061EY39; -.
DR STRING; 3641.A0A061EY39; -.
DR EnsemblPlants; EOY10020; EOY10020; TCM_025391.
DR Gramene; EOY10020; EOY10020; TCM_025391.
DR eggNOG; ENOG502QUU5; Eukaryota.
DR HOGENOM; CLU_016754_5_1_1; -.
DR InParanoid; A0A061EY39; -.
DR OMA; KQINFHG; -.
DR Proteomes; UP000026915; Chromosome 5.
DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001554; Glyco_hydro_14.
DR InterPro; IPR018238; Glyco_hydro_14_CS.
DR InterPro; IPR001371; Glyco_hydro_14B_pln.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31352:SF40; BETA-AMYLASE 5; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000509};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000509};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000509};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU000509};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 388..389
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 500 AA; 56580 MW; B9D87D31E26B5A23 CRC64;
MEAQSAVTDK KKMLANYVPI YVMLPLGIVS NDNVLLDKDG LKKQLLKLKE AGIDGVMSDV
WWGIVESPGP KQYDWSAYRS LVELVKECGL KLQAIMSFHQ CGGNVGDEVY IPIPQWVLDI
GETDPDIFYT NRAGNRNKEY LTLGVDHQAI FNGRTAIQIY SDYMKSFREV MSDLIEAGVI
IDIEVGLGAA GELRYPSYPQ SQGWVFPGIG EFQCYDKYLK AAFKEAATKA GHPEWELPDN
AGEYNDTPES TEFFGINGTY LTVKGKFFLT WYSNMLLCHG DDTLDEANKA FLGCELKLAA
KVSGIHWWYK SDSHAAELTA GYYNLNDRDG YRPIARMLSR HDRAILNFTC LEMRDSEQDA
AAKSGPQELV QQVLSGGWRE HIEVAGENAL SRYDSDAYNQ MLLNARPNGV TEEGRPQMHT
VTYLRSSDDL FEEENFELFK IFVKKMHADQ EYCSDPKMYG QELGPLQRSK PKIPIDDLLD
ATERLEPFPW DEETDMKVDG
//
