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Q9FM68 (BAM4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inactive beta-amylase 4, chloroplastic
Alternative name(s):
Inactive beta-amylase 6
Gene names
Name:BAM4
Synonyms:BMY6
Ordered Locus Names:At5g55700
ORF Names:MDF20.14
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

No alpha-1,4-glucan hydrolase activity, including beta-amylase, alpha-amylase, a-glucosidase or alpha-amyloglucosidase. However, facilitates or regulates starch breakdown, especially at night, by a mechanism involving direct interaction with starch or other alpha-1,4-glucan. Ref.5 Ref.6

Subcellular location

Plastidchloroplast Ref.5.

Tissue specificity

Preferentially expressed in vascular tissue of cotyledons, leaves, petioles, stems, petals, siliques and roots, particularly in phloem. Also present in root tip. Ref.7

Disruption phenotype

Slightly retarded growth rate and reduced starch breakdown in leaves during the night. Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Caution

In contrast to other members of the family, lacks the conserved Glu active site in position 473, which is replaced by an Arg residue, explaining why it is inactive.

Sequence caution

The sequence AAK76508.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentChloroplast
Plastid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processstarch catabolic process

Inferred from mutant phenotype Ref.5. Source: TAIR

   Cellular componentchloroplast

Inferred from direct assay Ref.5. Source: TAIR

   Molecular functionbeta-amylase activity

Inferred from electronic annotation. Source: InterPro

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9FM68-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Chloroplast Potential
Chain63 – 531469Inactive beta-amylase 4, chloroplastic
PRO_0000393419

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 0DBAC46474252449

FASTA53160,117
        10         20         30         40         50         60 
MTETGVIGCG CRGVTGGNFF HPGGFSLKSC FLEQSTKRNR NFFRSVSMIP PFKRGRFITK 

        70         80         90        100        110        120 
LRSVAGNSRI FSMDAREKSR SFVLVSSRHK RVPVFVMMPI DTFGIDASGC PKIKRLKALT 

       130        140        150        160        170        180 
VSLKALKLAG VHGIAVEVWW GIVERFSPLE FKWSLYEELF RLISEAGLKL HVALCFHSNM 

       190        200        210        220        230        240 
HLFGGKGGIS LPLWIREIGD VNKDIYYRDK SGFSNNDYLT LGVDQLPLFG GRTAVQCYED 

       250        260        270        280        290        300 
FMLSFSTKFE PYLGNVIEEI SIGLGPSGEL RYPAHPSGDG RWKFPGIGEF QCHDKYMMED 

       310        320        330        340        350        360 
LMAVASQEGK PQWGSRDPPN TGCYNSFPSG VPFFEEGNDS FLSDYGRFFL EWYSGKLICH 

       370        380        390        400        410        420 
ADAILAKAAD VLRRRQEEEK SSVMLVAKIG GIYWWYKTSS HPAELTAGYY NTSLRDGYDP 

       430        440        450        460        470        480 
VASVLSRHGA ALNIPCLDMA DSEIPEKYLC SPEGLRRQIH DVSKKWTIHV TGRNTSERFD 

       490        500        510        520        530 
EMGLRQIREN CVQPNGDTLR SFTFCRMNEK IFRVENWNNF VPFIRQMSAD M 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:41-54(1998) [PubMed: 9628582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-531.
Strain: cv. Columbia.
[4]"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
DNA Res. 16:155-164(2009) [PubMed: 19423640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-531.
Strain: cv. Columbia.
[5]"Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts upstream of three active beta-amylases in Arabidopsis chloroplasts."
Fulton D.C., Stettler M., Mettler T., Vaughan C.K., Li J., Francisco P., Gil M., Reinhold H., Eicke S., Messerli G., Dorken G., Halliday K., Smith A.M., Smith S.M., Zeeman S.C.
Plant Cell 20:1040-1058(2008) [PubMed: 18390594] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, GENE FAMILY, NOMENCLATURE.
[6]"Catalytically-inactive beta-amylase BAM4 required for starch breakdown in Arabidopsis leaves is a starch-binding-protein."
Li J., Francisco P., Zhou W., Edner C., Steup M., Ritte G., Bond C.S., Smith S.M.
Arch. Biochem. Biophys. 489:92-98(2009) [PubMed: 19664588] [Abstract]
Cited for: FUNCTION.
[7]"The gene encoding the catalytically inactive beta-amylase BAM4 involved in starch breakdown in Arabidopsis leaves is expressed preferentially in vascular tissues in source and sink organs."
Francisco P., Li J., Smith S.M.
J. Plant Physiol. 167:890-895(2010) [PubMed: 20153546] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB009050 Genomic DNA. Translation: BAB09237.1.
CP002688 Genomic DNA. Translation: AED96669.1.
AY045834 mRNA. Translation: AAK76508.1. Different initiation.
BT001909 mRNA. Translation: AAN71908.1.
AK317617 mRNA. Translation: BAH20280.1.
IPIIPI00546276.
RefSeqNP_568829.2. NM_124952.4.
UniGeneAt.49179.
At.71092.

3D structure databases

HSSPHSSP built from PDB template 1B1Y based on UniProtKB P16098.
ProteinModelPortalQ9FM68.
SMRQ9FM68. Positions 89-531.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9FM68.

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G55700.1; AT5G55700.1; AT5G55700.
GeneID835664.
GenomeReviewsGene locus AT5G55700 in contig BA000015_GR.
KEGGath:AT5G55700.
NMPDRfig|3702.1.peg.27499.

Organism-specific databases

TAIRAt5g55700.

Phylogenomic databases

GeneTreeEPGT00070000028196.
InParanoidQ9FM68.
OMADAREKSR.
PhylomeDBQ9FM68.
ProtClustDBPLN02161.

Gene expression databases

GenevestigatorQ9FM68.

Family and domain databases

InterProIPR001554. Glyco_hydro_14.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00506. BETA_AMYLASE_1. False negative.
PS00679. BETA_AMYLASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBAM4_ARATH
AccessionPrimary (citable) accession number: Q9FM68
Secondary accession number(s): B9DHR3, Q94AS2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families