BAM4_ARATH
ID BAM4_ARATH Reviewed; 531 AA.
AC Q9FM68; B9DHR3; Q94AS2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Inactive beta-amylase 4, chloroplastic;
DE AltName: Full=Inactive beta-amylase 6;
DE Flags: Precursor;
GN Name=BAM4; Synonyms=BMY6; OrderedLocusNames=At5g55700; ORFNames=MDF20.14;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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] OF 34-531.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-531.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, GENE FAMILY, AND
RP 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 [6]
RP FUNCTION.
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 [7]
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: No alpha-1,4-glucan hydrolase activity, including beta-
CC amylase, alpha-amylase, a-glucosidase or alpha-amyloglucosidase.
CC However, facilitates or regulates starch breakdown, especially at
CC night, by a mechanism involving direct interaction with starch or other
CC alpha-1,4-glucan. {ECO:0000269|PubMed:18390594,
CC ECO:0000269|PubMed:19664588}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18390594}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FM68-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in vascular tissue of
CC cotyledons, leaves, petioles, stems, petals, siliques and roots,
CC particularly in phloem. Also present in root tip.
CC {ECO:0000269|PubMed:20153546}.
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 -!- CAUTION: In contrast to other members of the family, lacks the
CC conserved Glu active site in position 473, which is replaced by an Arg
CC residue, explaining why it is inactive. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK76508.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB009050; BAB09237.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96669.1; -; Genomic_DNA.
DR EMBL; AY045834; AAK76508.1; ALT_INIT; mRNA.
DR EMBL; BT001909; AAN71908.1; -; mRNA.
DR EMBL; AK317617; BAH20280.1; -; mRNA.
DR RefSeq; NP_568829.2; NM_124952.5. [Q9FM68-1]
DR AlphaFoldDB; Q9FM68; -.
DR SMR; Q9FM68; -.
DR BioGRID; 20908; 1.
DR STRING; 3702.AT5G55700.1; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR PaxDb; Q9FM68; -.
DR PRIDE; Q9FM68; -.
DR ProteomicsDB; 240772; -. [Q9FM68-1]
DR EnsemblPlants; AT5G55700.1; AT5G55700.1; AT5G55700. [Q9FM68-1]
DR GeneID; 835664; -.
DR Gramene; AT5G55700.1; AT5G55700.1; AT5G55700. [Q9FM68-1]
DR KEGG; ath:AT5G55700; -.
DR Araport; AT5G55700; -.
DR TAIR; locus:2162152; AT5G55700.
DR eggNOG; ENOG502QRDP; Eukaryota.
DR HOGENOM; CLU_016754_5_1_1; -.
DR InParanoid; Q9FM68; -.
DR OMA; YNWSLYE; -.
DR PhylomeDB; Q9FM68; -.
DR PRO; PR:Q9FM68; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM68; baseline and differential.
DR Genevisible; Q9FM68; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005983; P:starch catabolic process; IMP:TAIR.
DR InterPro; IPR001554; Glyco_hydro_14.
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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism; Chloroplast; Plastid;
KW Polysaccharide degradation; Reference proteome; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..531
FT /note="Inactive beta-amylase 4, chloroplastic"
FT /id="PRO_0000393419"
SQ SEQUENCE 531 AA; 60117 MW; 0DBAC46474252449 CRC64;
MTETGVIGCG CRGVTGGNFF HPGGFSLKSC FLEQSTKRNR NFFRSVSMIP PFKRGRFITK
LRSVAGNSRI FSMDAREKSR SFVLVSSRHK RVPVFVMMPI DTFGIDASGC PKIKRLKALT
VSLKALKLAG VHGIAVEVWW GIVERFSPLE FKWSLYEELF RLISEAGLKL HVALCFHSNM
HLFGGKGGIS LPLWIREIGD VNKDIYYRDK SGFSNNDYLT LGVDQLPLFG GRTAVQCYED
FMLSFSTKFE PYLGNVIEEI SIGLGPSGEL RYPAHPSGDG RWKFPGIGEF QCHDKYMMED
LMAVASQEGK PQWGSRDPPN TGCYNSFPSG VPFFEEGNDS FLSDYGRFFL EWYSGKLICH
ADAILAKAAD VLRRRQEEEK SSVMLVAKIG GIYWWYKTSS HPAELTAGYY NTSLRDGYDP
VASVLSRHGA ALNIPCLDMA DSEIPEKYLC SPEGLRRQIH DVSKKWTIHV TGRNTSERFD
EMGLRQIREN CVQPNGDTLR SFTFCRMNEK IFRVENWNNF VPFIRQMSAD M
