ID A0A0K9P4K1_ZOSMR Unreviewed; 425 AA.
AC A0A0K9P4K1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
GN ORFNames=ZOSMA_425G00110 {ECO:0000313|EMBL:KMZ63137.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ63137.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ63137.1}.
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DR EMBL; LFYR01001270; KMZ63137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9P4K1; -.
DR STRING; 29655.A0A0K9P4K1; -.
DR OMA; TEVQIGM; -.
DR OrthoDB; 46229at2759; -.
DR Proteomes; UP000036987; 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:UP000036987}.
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
SQ SEQUENCE 425 AA; 48864 MW; E75820369E9114F6 CRC64;
MYDWDGYFDL VRLAATFRMK VRIVLGFHQR GTGPTDPCWL PLPIWVLEEM DRCPDLAYSD
RFGRRNKEYV SLGCDVLPVL KGRSPVQVYS DLMRSFRNKF EHVLGDIITE VQIGMGPCGE
LRYPSCPCER FTRPTDEPEL GEFQCYDKYM LASLNAAAHK IDIKQWGKGG PFGAGSLFQN
SEETIFFKND GSWNTQYGRF FLEWYSEMLL LHGERLCMAA DTIFFGTGVN LLGKVAGIHW
HYYTDSHPSE LTAGYYNTLT RDGYLSIARM FARYRMTMCC ACFDLKDAEE EDINPKSSPE
GFLRQLVHAA RICNLSLSGE NSRNRLDDAS LRQIIKSSKL YLGQSGGVHS NTTSLSFNFV
RMGKNMFDSH NWSRFTRFVR QMSDARTFQA SLGHRTSRSS FFCASEELMK LAERLYIFNS
FIPRF
//
