BAM6_ARATH
ID BAM6_ARATH Reviewed; 577 AA.
AC Q8L762; Q9ZV58;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Beta-amylase 6;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Full=Beta-amylase 5;
GN Name=BAM6; Synonyms=BMY5; OrderedLocusNames=At2g32290; ORFNames=T32F6.19;
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;
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 [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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC69949.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005700; AAC69949.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08663.1; -; Genomic_DNA.
DR EMBL; AY136463; AAM97128.1; -; mRNA.
DR PIR; C84731; C84731.
DR RefSeq; NP_180788.2; NM_128788.3.
DR AlphaFoldDB; Q8L762; -.
DR SMR; Q8L762; -.
DR STRING; 3702.AT2G32290.1; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR PaxDb; Q8L762; -.
DR PRIDE; Q8L762; -.
DR ProteomicsDB; 240775; -.
DR EnsemblPlants; AT2G32290.1; AT2G32290.1; AT2G32290.
DR GeneID; 817789; -.
DR Gramene; AT2G32290.1; AT2G32290.1; AT2G32290.
DR KEGG; ath:AT2G32290; -.
DR Araport; AT2G32290; -.
DR TAIR; locus:2062535; AT2G32290.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_5_1_1; -.
DR InParanoid; Q8L762; -.
DR OMA; PIPPFPW; -.
DR OrthoDB; 533202at2759; -.
DR PhylomeDB; Q8L762; -.
DR BioCyc; ARA:AT2G32290-MON; -.
DR PRO; PR:Q8L762; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L762; baseline and differential.
DR Genevisible; Q8L762; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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 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; PTHR31352; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome.
FT CHAIN 1..577
FT /note="Beta-amylase 6"
FT /id="PRO_0000393420"
FT ACT_SITE 252
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 447
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 448..449
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 577 AA; 66568 MW; 3538C82F34A27554 CRC64;
MTSVLGMMNP NLINGRNLHK GSSIFVQDKE TKKRVQWRLS IKEGSLRTHQ ATASSATEPK
ATEFNTTTYE DKMLTNYVPV YVMLQLGVIT NDNVLENEES LKKQLKKLKQ SQVDGVMVDV
WWGIVESKGP KQYQWSAYRN LFAIVQSFGL KLQAIMSFHR CGGNIGDDVN IPIPKWVLEI
GDSNPDIFYT NKSGNRNKEC LSLSVDNLSL FRGRTAVEMY RDYMKSFREN MEDFISSGVI
IDIEVGLGPA GELRYPSYSE TQGWVFPGIG EFQCYDKYLR SDYEEEVRRI GHPEWKLPEN
AGEYNSVPGE TEFFEYSNGT YLKEEGNFFL SWYSKKLLLH GDQILDEANK VFLGCKLKIA
AKVSGIHWWY KTESHAAELT AGYYNLKNRD GYRAIAKIMR RHHAILNFTC LEMKNTEQPA
KAKSGPQELV QQVLSSGWRE GIEVAGENAL PRFDRNGYNQ IILNARPNGV NQDGKPRMFG
FTYLRLSDKL LNEPNFSTFK MFLKRMHANQ EYCSEPERYN HELLPLERSR NDESLEMFME
ETEPFDPFPW LDETDMSIRP FESVLSLLRS TFLRKKS
