BAM7_ARATH
ID BAM7_ARATH Reviewed; 691 AA.
AC O80831; Q0WU61;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Beta-amylase 7;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Full=Beta-amylase 4;
GN Name=BAM7; Synonyms=BMY4; OrderedLocusNames=At2g45880; ORFNames=F4I18.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18390594; DOI=10.1105/tpc.107.056507;
RA Fulton D.C., Stettler M., Mettler T., Vaughan C.K., Li J., Francisco P.,
RA Gil M., Reinhold H., Eicke S., Messerli G., Dorken G., Halliday K.,
RA Smith A.M., Smith S.M., Zeeman S.C.;
RT "Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts
RT upstream of three active beta-amylases in Arabidopsis chloroplasts.";
RL Plant Cell 20:1040-1058(2008).
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 -!- INTERACTION:
CC O80831; Q9FH80: BAM8; NbExp=5; IntAct=EBI-15212616, EBI-4427212;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28536.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004665; AAC28536.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10613.1; -; Genomic_DNA.
DR EMBL; AK227323; BAE99337.1; -; mRNA.
DR PIR; T02459; T02459.
DR RefSeq; NP_182112.2; NM_130151.7.
DR AlphaFoldDB; O80831; -.
DR SMR; O80831; -.
DR BioGRID; 4532; 2.
DR IntAct; O80831; 2.
DR STRING; 3702.AT2G45880.1; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR iPTMnet; O80831; -.
DR PaxDb; O80831; -.
DR PRIDE; O80831; -.
DR ProteomicsDB; 240636; -.
DR EnsemblPlants; AT2G45880.1; AT2G45880.1; AT2G45880.
DR GeneID; 819196; -.
DR Gramene; AT2G45880.1; AT2G45880.1; AT2G45880.
DR KEGG; ath:AT2G45880; -.
DR Araport; AT2G45880; -.
DR TAIR; locus:2050720; AT2G45880.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_4_1_1; -.
DR InParanoid; O80831; -.
DR OMA; NDEFMFH; -.
DR OrthoDB; 533202at2759; -.
DR PhylomeDB; O80831; -.
DR BioCyc; ARA:AT2G45880-MON; -.
DR PRO; PR:O80831; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80831; baseline and differential.
DR Genevisible; O80831; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048831; P:regulation of shoot system development; IMP:TAIR.
DR InterPro; IPR008540; BES1_N.
DR InterPro; IPR001554; Glyco_hydro_14.
DR InterPro; IPR018238; Glyco_hydro_14_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; PTHR31352; 1.
DR Pfam; PF05687; BES1_N; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase; Phosphoprotein;
KW Polysaccharide degradation; Reference proteome.
FT CHAIN 1..691
FT /note="Beta-amylase 7"
FT /id="PRO_0000393421"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 618
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 619..620
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 654
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LIR6"
FT CONFLICT 377
FT /note="K -> R (in Ref. 3; BAE99337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 77131 MW; FAB1130D333CACE4 CRC64;
MATDMHKLLG TSEEDDDEEM DMDVKEEDDG DRRNRDKHAA SGSSSNDEFM FQQSMQDQVG
TPGGGGSRRS RPLEEKERTK LRERHRRAIT ARILGGLRRH GNYNLRVRAD INDVIAALAR
EAGWVVLPDG TTFPSKSQGT KPTGGSSAVA AGSSASHIAS QQTSPPALRV VSSGLRSPVE
LSSCRMKGVF TPAPSPYDML PIQSPELVGS VNKAEGLVGC SVDVINSKQI LEIPPNLTEQ
DFSGTPYVPV YVMLPLGVIN MKCELADRDG LLKHLRILKS IHVDGVKVDC WWGIVEGHSP
QEYNWTGYRQ LFQMVRDLNL KIQVLMSFHE CGGNVGDDVC IPLPHWVAEI GRTNPDIYFT
DREGRRNPEC LSWGIDKERI LRGRTALEVY FDYMRSFRIE LAEFLEDGVI SMVEIGLGPC
GELRYPSCPI KHGWRYPGVG EFQCYDKYLS KSLRKAAESR GHLFWARGPD NTGSYNSQPQ
GTGFFCDGGD YDGLYGRFFL KWYSQVLIDH ADQILCLAKL VFDSSCIAAK LPDVHWWYRT
ASHAAELTAG FYNPSNRDGY SAIASTLKKH GATLSFVSGE VQVLNRPDDF SGALGEPEAV
AWQVLNAAWD SGTPVARENS LACHDRVGYN KMLESVKFRN DPDRKHLSSF AYSRLVPALM
EGHNIVEFER FVKKLHGEAV MNHHHHHHQQ V
