ID A0A0D9WZY9_9ORYZ Unreviewed; 1112 AA.
AC A0A0D9WZY9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR07G15070.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR07G15070.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR07G15070.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR07G15070.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0D9WZY9; -.
DR STRING; 77586.A0A0D9WZY9; -.
DR EnsemblPlants; LPERR07G15070.1; LPERR07G15070.1; LPERR07G15070.
DR Gramene; LPERR07G15070.1; LPERR07G15070.1; LPERR07G15070.
DR eggNOG; ENOG502QUU5; Eukaryota.
DR HOGENOM; CLU_008352_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 7.
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; 2.
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:SF57; BETA-AMYLASE; 1.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF01373; Glyco_hydro_14; 2.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR PROSITE; PS00506; BETA_AMYLASE_1; 2.
DR PROSITE; PS00679; BETA_AMYLASE_2; 2.
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:UP000032180}.
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 808
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 1002
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 675
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 715
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 723
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 917
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 922
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 964
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 1003..1004
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 1042
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 1112 AA; 124465 MW; DF79F8147E35638E CRC64;
MTTTSLPSGQ PVRLQQRWTC RSRAVSPAPL LSPPTTRRLV ADFRRKTVAS LRVRGVAAER
EQDDSPLPEP PPALTDEEKM LANYVPVYVM LPLGVVTAEN ELEDAGSLRE QLRRLREEAR
VDGVMADVWW GIVEGAGPGM YEWRAYRELF GMAREEGLKV QAIMSFHACG GNVGDDAVCI
PLPRWVRDVG DVDPDVYYTS PRGVRNQEYL TIGVDDRPLF HGRTAIQLYA DFMKSFRENM
ADFLDSGLIV DIEVGLGPAG ELRYPSYPEN QGWEFPGIGQ FQCYDKYLNE DFKAAATAAG
HPEWDLPDAN DTGDYNDTPD DTRFFAAGTG TYLTDAGRFF LTWYSTKLLS HGDRILDEAN
IAFLGCTLKL AAKVSGIHWW YLHPSHAAEL AAGYYNVAGR RDGYAPVARV LARHDGAVMN
FTCAEMRDSE QPEEAMSSPE ALVRQALSAA WREGVDAACE NALSRYDRRG YNQMLLNARP
NGVVVGGDAT PRRVAAVTYL RLSEELLTGS NFRAFRSFVR KMHADQDYCP DPARYGRPMR
PLERSGPEVP VERLREATAP VPPYPFDGET DMSVGGGLAE FIDWVFDKVE WIFSPERPAT
FIKPSSVSNN KVKLVFSEHT QAATMAGSLL ANYVQVNVML PLDAVTVDNK FEKGDEIRAQ
LKKLTEAGVD GVMVDVWWGL VEGKSPGVYD WDAYRQLFKL VQEAGLKLQA IMSFHQCGGN
VGDVVNIPIP QWVRDVSKSD PDIFYTNRGG ARNIEYLTLG VDDQPLFHGR TAIQMYADYM
KSFRENMAEF LDAGVIVDIE VGLGPAGEMR YPSYPQSQGW AFPGIGEFIC YDKYLEADFK
AEAAKAGHPE WGLPDDAGEY NDTPEKTRFF TGNGTYVTEK GKFFLTWYSN KLIEHGDKIL
DEANKAFLGC RVHLAIKISG IHWWYRVPNH AAELTAGYYN LDDRDGYRTI ARMLTRHRAC
VNFTCAEMRD SEQSSEAKSA PEELVQQVLS AGWREGLNVA CENALGRYDA TAYNTILRNA
RPTGINKNGP PEHKLSGFTY LRLSDELLEG QNYNTFRSFV KRMHANQDHN SNVDPIKPLQ
RSTPKMPIGE ILQAAQPKLE PFPFDENTDL PV
//
