ID B9MTV8_POPTR Unreviewed; 547 AA.
AC B9MTV8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=POPTR_001G148900 {ECO:0000313|EMBL:PNT54600.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT54600.1, ECO:0000313|Proteomes:UP000006729};
RN [1] {ECO:0000313|EMBL:PNT54600.1, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}, and
RC Nisqually-1 {ECO:0000313|EMBL:PNT54600.1};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2] {ECO:0000313|EMBL:PNT54600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nisqually-1 {ECO:0000313|EMBL:PNT54600.1};
RA Tuskan G., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U.,
RA Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L.,
RA Aerts A., Bhalerao R., Bhalerao R., Blaudez D., Boerjan W., Brun A.,
RA Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J.,
RA Chen G., Cooper D., Coutinho P., Couturier J., Covert S., Cronk Q.,
RA Cunningham R., Davis J., Degroeve S., Dejardin A., Depamphilis C.,
RA Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B.,
RA Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L.,
RA Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R.,
RA Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R.,
RA Joshi C., Kangasjarvi J., Karlsson J., Kelleher C., Kirkpatrick R.,
RA Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.,
RA Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C.,
RA Nelson D., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G.,
RA Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P.,
RA Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J.,
RA Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.,
RA Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G.,
RA Yin T., Douglas C., Marra M., Sandberg G., Van De Peer Y., Rokhsar D.;
RT "WGS assembly of Populus trichocarpa.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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; CM009290; PNT54600.1; -; Genomic_DNA.
DR EMBL; CM009290; PNT54601.1; -; Genomic_DNA.
DR EMBL; CM009290; PNT54602.1; -; Genomic_DNA.
DR RefSeq; XP_006385389.1; XM_006385327.1.
DR AlphaFoldDB; B9MTV8; -.
DR STRING; 3694.B9MTV8; -.
DR EnsemblPlants; Potri.001G148900.2.v4.1; Potri.001G148900.2.v4.1; Potri.001G148900.v4.1.
DR GeneID; 18096774; -.
DR Gramene; Potri.001G148900.2.v4.1; Potri.001G148900.2.v4.1; Potri.001G148900.v4.1.
DR KEGG; pop:18096774; -.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_1_1_1; -.
DR InParanoid; B9MTV8; -.
DR OMA; TADNMKF; -.
DR OrthoDB; 46229at2759; -.
DR Proteomes; UP000006729; Chromosome 1.
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:SF1; BETA-AMYLASE 3, CHLOROPLASTIC; 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.
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:UP000006729}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 258
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 455
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 456..457
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 547 AA; 61093 MW; 7F535DD8B155DC48 CRC64;
MTSALQSSTS FISLKDTRSP KTPDDFSGTI CFAHIKPSCR LQAKNSMQEA QLSHDEILMT
EGRKSKKGGE LHAISGPRSS NDSKVPVFVM LPLDTITIGG NLNKPRAMNA SLMALRSAGV
EGVMVDAWWG LVEKDGPLKY NWEGYAELVQ MVQKHGLKLQ VVMSFHQCGG NVGDSCSIPL
PPWVLEEMSK NPDLVYTDRS GRRNPEYISL GCDSLPILRG RTPIQVYSDY MRSFRERFKD
YLGDVIMEIQ VGMGPCGELR YPAYPETNGT WRFPGIGEFQ CYDKYMRASL EASAEALGKK
DWGRGGPHDS GQYNHFPEET GFFRRDGTWN TEYGQFFLEW YSGKLLEHGE KILAAAEGIF
QGTGAQLSGK VAGIHWHYRT RSHAAELTAG YYNTRHHDGY LPIARMFSKH GVVFNFTCME
MRDGEQPEHA NCSPQGLVRQ VKMATRTAGT ELAGENALER YDAGAYTQVL ATSRSESGNG
LTAFTYLRMN KKLFEGDNWR QLVEFVKSMS EGGRNEKLSE CDSHGTNLYI GFIKDKSVQK
TKEAALA
//
