BAM8_ARATH
ID BAM8_ARATH Reviewed; 689 AA.
AC Q9FH80; Q2V314;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Beta-amylase 8;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Full=Beta-amylase 2;
GN Name=BAM8; Synonyms=BMY2; OrderedLocusNames=At5g45300; ORFNames=K9E15.8;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 Q9FH80; O80831: BAM7; NbExp=5; IntAct=EBI-4427212, EBI-15212616;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FH80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FH80-2; Sequence=VSP_038980;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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DR EMBL; AB020744; BAB10251.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95229.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95230.1; -; Genomic_DNA.
DR EMBL; AK117140; BAC41818.1; -; mRNA.
DR EMBL; BT006482; AAP21290.1; -; mRNA.
DR RefSeq; NP_001032014.1; NM_001036937.1. [Q9FH80-2]
DR RefSeq; NP_199343.1; NM_123898.3. [Q9FH80-1]
DR AlphaFoldDB; Q9FH80; -.
DR SMR; Q9FH80; -.
DR BioGRID; 19815; 12.
DR IntAct; Q9FH80; 12.
DR STRING; 3702.AT5G45300.1; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR iPTMnet; Q9FH80; -.
DR PaxDb; Q9FH80; -.
DR PRIDE; Q9FH80; -.
DR ProteomicsDB; 240740; -. [Q9FH80-1]
DR EnsemblPlants; AT5G45300.1; AT5G45300.1; AT5G45300. [Q9FH80-1]
DR EnsemblPlants; AT5G45300.2; AT5G45300.2; AT5G45300. [Q9FH80-2]
DR GeneID; 834566; -.
DR Gramene; AT5G45300.1; AT5G45300.1; AT5G45300. [Q9FH80-1]
DR Gramene; AT5G45300.2; AT5G45300.2; AT5G45300. [Q9FH80-2]
DR KEGG; ath:AT5G45300; -.
DR Araport; AT5G45300; -.
DR TAIR; locus:2158455; AT5G45300.
DR eggNOG; ENOG502QW2E; Eukaryota.
DR InParanoid; Q9FH80; -.
DR OMA; ELKYPSC; -.
DR PhylomeDB; Q9FH80; -.
DR PRO; PR:Q9FH80; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH80; baseline and differential.
DR Genevisible; Q9FH80; 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; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism; Cytoplasm; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome.
FT CHAIN 1..689
FT /note="Beta-amylase 8"
FT /id="PRO_0000393422"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 429
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 623
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 537
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 624..625
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 160..161
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038980"
SQ SEQUENCE 689 AA; 77160 MW; D591C143B130EC7B CRC64;
MHTLNNTITT TTGSQDPNLD PIPDPDQFPN RNRNQPQSRR PRGFAAAAAA ASIAPTENDV
NNGNIAGIGG GEGSSGGGGG GGGKGKRERE KEKERTKLRE RHRRAITSRM LAGLRQYGNF
PLPARADMND VIAALAREAG WSVEADGTTY RQSQQPNHVV QFPTRSIESP LSSSTLKNCA
KAAIESQQHS VLRNDEKLAP VSLDSIGIAE SDHPGNGRYT SVSPITSVGC LEANQLIQDV
HSAEQCNDFT ESFYVPVYAM LPVGIIDNFG QLVDPEGVRQ ELSYMKSLNV DGVVIDCWWG
IVEGWNPQKY VWSGYRELFN LIRDFKLKLQ VVMAFHEYGG NASGNVMISL PQWVLKIGKD
NPDIFFTDRE GRRSFECLNW SIDKERVLHG RTGIEVYFDF MRSFRSEFDD LFVEGLITAV
EIGLGASGEL KYPSFPERMG WIYPGIGEFQ CYDKYSQLSL QKEAKSRGFT FWGKGPENAG
QYSSHPHETV FFQERGEYDS YYGRFFLNWY SQLLIGHAEN VLSLANLAFE ETKIIVKIPA
IYWSYKTASH AAELTAGYYN PSNRDGYSLV FETLKKYSVT VKFVCPGPQM SPNAHEEALA
DPEGLSWQVI NAAWDKGLQI GGENAITCFD RDGCMRLIDI AKPRNHPDGY HFSFFTYRQP
SPLVQGSTCF PDLDYFIKRM HGDIRDKQF
