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BAM3_ARATH
ID   BAM3_ARATH              Reviewed;         548 AA.
AC   O23553; Q941A5; Q9SMW0;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 3.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Beta-amylase 3, chloroplastic;
DE            EC=3.2.1.2;
DE   AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE   AltName: Full=Beta-amylase 8;
DE   AltName: Full=Chloroplast beta-amylase;
DE            Short=CT-BMY;
DE   Flags: Precursor;
GN   Name=BAM3; Synonyms=BMY8, CTBMY; OrderedLocusNames=At4g17090;
GN   ORFNames=dl4575c, FCAALL.5;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10652124; DOI=10.1046/j.1365-313x.1999.00625.x;
RA   Lao N.T., Schoneveld O., Mould R.M., Hibberd J.M., Gray J.C.,
RA   Kavanagh T.A.;
RT   "An Arabidopsis gene encoding a chloroplast-targeted beta-amylase.";
RL   Plant J. 20:519-527(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, AND INDUCTION BY COLD.
RX   PubMed=16297066; DOI=10.1111/j.1365-313x.2005.02565.x;
RA   Kaplan F., Guy C.L.;
RT   "RNA interference of Arabidopsis beta-amylase8 prevents maltose
RT   accumulation upon cold shock and increases sensitivity of PSII
RT   photochemical efficiency to freezing stress.";
RL   Plant J. 44:730-743(2005).
RN   [8]
RP   FUNCTION, AND INDUCTION BY CIRCADIAN DAYLENGTH.
RX   PubMed=16055686; DOI=10.1104/pp.105.061903;
RA   Lu Y., Gehan J.P., Sharkey T.D.;
RT   "Daylength and circadian effects on starch degradation and maltose
RT   metabolism.";
RL   Plant Physiol. 138:2280-2291(2005).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16698902; DOI=10.1104/pp.106.079186;
RA   Sparla F., Costa A., Lo Schiavo F., Pupillo P., Trost P.;
RT   "Redox regulation of a novel plastid-targeted beta-amylase of
RT   Arabidopsis.";
RL   Plant Physiol. 141:840-850(2006).
RN   [10]
RP   INDUCTION BY TREHALOSE.
RX   PubMed=17031512; DOI=10.1007/s11103-006-9082-2;
RA   Ramon M., Rolland F., Thevelein J.M., van Dijck P., Leyman B.;
RT   "ABI4 mediates the effects of exogenous trehalose on Arabidopsis growth and
RT   starch breakdown.";
RL   Plant Mol. Biol. 63:195-206(2007).
RN   [11]
RP   FUNCTION.
RX   PubMed=17631522; DOI=10.1104/pp.107.104224;
RA   Edner C., Li J., Albrecht T., Mahlow S., Hejazi M., Hussain H., Kaplan F.,
RA   Guy C., Smith S.M., Steup M., Ritte G.;
RT   "Glucan, water dikinase activity stimulates breakdown of starch granules by
RT   plastidial beta-amylases.";
RL   Plant Physiol. 145:17-28(2007).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP   PHENOTYPE, 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).
RN   [13]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19664588; DOI=10.1016/j.abb.2009.07.024;
RA   Li J., Francisco P., Zhou W., Edner C., Steup M., Ritte G., Bond C.S.,
RA   Smith S.M.;
RT   "Catalytically-inactive beta-amylase BAM4 required for starch breakdown in
RT   Arabidopsis leaves is a starch-binding-protein.";
RL   Arch. Biochem. Biophys. 489:92-98(2009).
RN   [14]
RP   TISSUE SPECIFICITY.
RX   PubMed=20153546; DOI=10.1016/j.jplph.2010.01.006;
RA   Francisco P., Li J., Smith S.M.;
RT   "The gene encoding the catalytically inactive beta-amylase BAM4 involved in
RT   starch breakdown in Arabidopsis leaves is expressed preferentially in
RT   vascular tissues in source and sink organs.";
RL   J. Plant Physiol. 167:890-895(2010).
CC   -!- FUNCTION: Beta-amylase activity. No alpha-amylase activity. Involved in
CC       cold resistance. Mediates the accumulation of maltose upon freezing
CC       stress, thus contributing to the protection of the photosynthetic
CC       electron transport chain. Plays a role in the circadian-regulated
CC       starch degradation and maltose metabolism in chloroplasts, especially
CC       at night. More active on phosphorylated glucan. Interacts directly with
CC       starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:10652124,
CC       ECO:0000269|PubMed:16055686, ECO:0000269|PubMed:16297066,
CC       ECO:0000269|PubMed:17631522, ECO:0000269|PubMed:18390594,
CC       ECO:0000269|PubMed:19664588}.
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   -!- ACTIVITY REGULATION: Redox regulation; active in reducing conditions,
CC       inactive in oxidizing conditions. {ECO:0000250}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6-7. {ECO:0000269|PubMed:18390594,
CC         ECO:0000269|PubMed:19664588};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:10652124, ECO:0000269|PubMed:16698902,
CC       ECO:0000269|PubMed:18390594}.
CC   -!- TISSUE SPECIFICITY: Expressed in vascular tissue of cotyledons, leaves,
CC       petioles, stems, petals, siliques and roots, particularly in phloem, as
CC       well as in photosynthetic tissues. {ECO:0000269|PubMed:20153546}.
CC   -!- INDUCTION: By cold stress. Light-mediated circadian regulation; highest
CC       levels at dawn and at dusk in long days (LD) but only at dusk in short
CC       days (SD). Repressed by trehalose in a ABI4-dependent manner, this
CC       effect is reversed in the presence of sucrose.
CC       {ECO:0000269|PubMed:16055686, ECO:0000269|PubMed:16297066,
CC       ECO:0000269|PubMed:17031512}.
CC   -!- DISRUPTION PHENOTYPE: Slightly retarded growth rate and reduced starch
CC       breakdown in leaves during the night. {ECO:0000269|PubMed:18390594}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK96508.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAL31225.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB46051.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB80980.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ250341; CAB58423.1; -; mRNA.
DR   EMBL; Z97342; CAB46051.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL161545; CAB80980.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002687; AEE83848.1; -; Genomic_DNA.
DR   EMBL; AY052315; AAK96508.1; ALT_SEQ; mRNA.
DR   EMBL; AY061898; AAL31225.1; ALT_SEQ; mRNA.
DR   EMBL; AY087592; AAM65134.1; -; mRNA.
DR   PIR; D71439; D71439.
DR   PIR; H85190; H85190.
DR   PIR; T52556; T52556.
DR   RefSeq; NP_567523.1; NM_117813.3.
DR   AlphaFoldDB; O23553; -.
DR   SMR; O23553; -.
DR   STRING; 3702.AT4G17090.1; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   iPTMnet; O23553; -.
DR   PaxDb; O23553; -.
DR   PRIDE; O23553; -.
DR   ProteomicsDB; 241123; -.
DR   EnsemblPlants; AT4G17090.1; AT4G17090.1; AT4G17090.
DR   GeneID; 827419; -.
DR   Gramene; AT4G17090.1; AT4G17090.1; AT4G17090.
DR   KEGG; ath:AT4G17090; -.
DR   Araport; AT4G17090; -.
DR   TAIR; locus:2130504; AT4G17090.
DR   eggNOG; ENOG502QTBX; Eukaryota.
DR   HOGENOM; CLU_016754_1_1_1; -.
DR   OMA; HEKTFTP; -.
DR   OrthoDB; 533202at2759; -.
DR   PhylomeDB; O23553; -.
DR   BioCyc; ARA:AT4G17090-MON; -.
DR   BioCyc; MetaCyc:AT4G17090-MON; -.
DR   BRENDA; 3.2.1.2; 399.
DR   PRO; PR:O23553; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O23553; baseline and differential.
DR   Genevisible; O23553; AT.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016161; F:beta-amylase activity; IDA:TAIR.
DR   GO; GO:0000024; P:maltose biosynthetic process; IMP:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0005983; P:starch catabolic process; IDA:TAIR.
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; PS00506; BETA_AMYLASE_1; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chloroplast; Glycosidase; Hydrolase; Plastid;
KW   Polysaccharide degradation; Reference proteome; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..548
FT                   /note="Beta-amylase 3, chloroplastic"
FT                   /id="PRO_0000393418"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        259
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        456
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         457..458
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         489
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  61353 MW;  A5794EDC8427FE30 CRC64;
     MELTLNSSSS LIKRKDAKSS RNQESSSNNM TFAKMKPPTY QFQAKNSVKE MKFTHEKTFT
     PEGETLEKWE KLHVLSYPHS KNDASVPVFV MLPLDTVTMS GHLNKPRAMN ASLMALKGAG
     VEGVMVDAWW GLVEKDGPMN YNWEGYAELI QMVQKHGLKL QVVMSFHQCG GNVGDSCSIP
     LPPWVLEEIS KNPDLVYTDK SGRRNPEYIS LGCDSVPVLR GRTPIQVYSD FMRSFRERFE
     GYIGGVIAEI QVGMGPCGEL RYPSYPESNG TWRFPGIGEF QCYDKYMKSS LQAYAESIGK
     TNWGTSGPHD AGEYKNLPED TEFFRRDGTW NSEYGKFFME WYSGKLLEHG DQLLSSAKGI
     FQGSGAKLSG KVAGIHWHYN TRSHAAELTA GYYNTRNHDG YLPIAKMFNK HGVVLNFTCM
     EMKDGEQPEH ANCSPEGLVK QVQNATRQAG TELAGENALE RYDSSAFGQV VATNRSDSGN
     GLTAFTYLRM NKRLFEGQNW QQLVEFVKNM KEGGHGRRLS KEDTTGSDLY VGFVKGKIAE
     NVEEAALV
 
 
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