ID W1PHK7_AMBTC Unreviewed; 559 AA.
AC W1PHK7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
GN ORFNames=AMTR_s00058p00155330 {ECO:0000313|EMBL:ERN06600.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN06600.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(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|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; KI393888; ERN06600.1; -; Genomic_DNA.
DR RefSeq; XP_006844925.1; XM_006844862.2.
DR AlphaFoldDB; W1PHK7; -.
DR STRING; 13333.W1PHK7; -.
DR EnsemblPlants; ERN06600; ERN06600; AMTR_s00058p00155330.
DR GeneID; 18434799; -.
DR Gramene; ERN06600; ERN06600; AMTR_s00058p00155330.
DR KEGG; atr:18434799; -.
DR eggNOG; ENOG502QSJZ; Eukaryota.
DR HOGENOM; CLU_016754_1_0_1; -.
DR OMA; TEVQIGM; -.
DR OrthoDB; 46229at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352:SF7; BETA-AMYLASE; 1.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000509};
KW Glycosidase {ECO:0000256|RuleBase:RU000509};
KW Hydrolase {ECO:0000256|RuleBase:RU000509};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU000509};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 476
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
SQ SEQUENCE 559 AA; 62390 MW; 63E8FAC2F25C7093 CRC64;
MAIYPTSISP SFCRTRHHPS EPSSFSSGGT PASIRCTHLS TTSNFRIRAH KTCRARAQRN
LGQGGLTAMA KLFSKPSGAD GSVSPEEPNE LHYLGPAQSR GGRGFPVFVA LPLDSVSSDG
KMMRRKAMEV SFRALKLAGV EGVAMDVWWG LVERDRPGVY DWRGYREVVE MALRHGLKVR
AVMAFHSCVG TEADPCHITL PHWVRQEMER ETDSAYTDRQ GRRNYDYISL GSDLLPVLRG
RSPIQAYSDF MRNFRGTFQQ FLGVIITGIQ VGMGPAGELR YPSHPSENLS WSSQGIGEFQ
CYDKHMLASL DACAREIGKE EWGKGGPIDA GSYYQNPEET GFFKSDGTWN TPYGHFFLEW
YSGMLLLHGE RLCIAAESIF SGTGVKLSAK VGGIHWQYDL KSHPAELTAG YFNTSFRDGY
IPIAHMFARH GVSLCCPCFD MSDENAKFFN IHSSPEGFLK QIVFAAKICN IHLTGENSLT
KLDESSSKQV LKSSKLYPDG GLDPACSFLF VRMNKNFFLP DNWNRFERLV WHMSDTGNFH
ARLGNKNTIE SRLCSNVAI
//
