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Database: UniProt
Entry: A0A151TJ74_CAJCA
LinkDB: A0A151TJ74_CAJCA
Original site: A0A151TJ74_CAJCA 
ID   A0A151TJ74_CAJCA        Unreviewed;       541 AA.
AC   A0A151TJ74;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=KK1_013421 {ECO:0000313|EMBL:KYP67101.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
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; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP67101.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP67101.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
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; CM003608; KYP67101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151TJ74; -.
DR   SMR; A0A151TJ74; -.
DR   STRING; 3821.A0A151TJ74; -.
DR   OrthoDB; 46229at2759; -.
DR   Proteomes; UP000075243; Chromosome 6.
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; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31352:SF1; BETA-AMYLASE 3, CHLOROPLASTIC; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 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:UP000075243}.
FT   ACT_SITE        254
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        451
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         452..453
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         482
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ   SEQUENCE   541 AA;  60769 MW;  1E0DF9476E9EDA1D CRC64;
     MALTLRSSIS IVNQKKSKLP KPKHDVPTKV HFVKTKPSLR LRTKCSMQHA HHVTRNHTNE
     KMEKVHSPSV AHGHKNDSMR VPVFVMLPLD TVTMGGTLNK ARAMNASLMA LKSAGVEGVM
     VDAWWGLVEK EGPFKYNWEA YAELVQMVQK HGLKLQVVMS FHQCGGNVGD SCSIPLPPWV
     LEEISKNPDL VYTDKSGRRN PEYISLGCDS MPVLRGRTPL QVYSDYMRSF RDRFRDYLGS
     VIIEIQVGMG PCGELRYPSY PENNGTWRFP GIGEFQCYDK YMRASLEASA EAIGKKEWGR
     SGPHDSGQYN QYPENTGFFK REGTWNTEYG KFFLDWYSTK LLEHGEKILV SAKGIFNSSG
     VTLSAKVAGI HWHYKARSHA AELTAGYYNT RFHDGYLPIA QMLAKHGVVL NFTCMEMRDR
     DQPEHANCSP EGLVHQVKMA ARTAGAEVAG ENALERYDAG AFSQVVSTSN SGSGLAAFTY
     LRMNKRLFEG DNWRHFVEFV KCMSEGGKRQ RLPESDSCGT HLYVGHIAGI QRKQVQEAAL
     V
//
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