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Q8L762 (BAM6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 59. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-amylase 6

EC=3.2.1.2
Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Beta-amylase 5
Gene names
Name:BAM6
Synonyms:BMY5
Ordered Locus Names:At2g32290
ORF Names:T32F6.19
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Sequence caution

The sequence AAC69949.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from direct assay. Source: TAIR

   Molecular functionbeta-amylase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Beta-amylase 6
PRO_0000393420

Regions

Region448 – 4492Substrate binding By similarity

Sites

Active site2521Proton donor By similarity
Active site4471Proton acceptor By similarity
Binding site1191Substrate By similarity
Binding site1591Substrate By similarity
Binding site1671Substrate By similarity
Binding site3621Substrate By similarity
Binding site3671Substrate By similarity
Binding site4091Substrate By similarity
Binding site4851Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8L762 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 3538C82F34A27554

FASTA57766,568
        10         20         30         40         50         60 
MTSVLGMMNP NLINGRNLHK GSSIFVQDKE TKKRVQWRLS IKEGSLRTHQ ATASSATEPK 

        70         80         90        100        110        120 
ATEFNTTTYE DKMLTNYVPV YVMLQLGVIT NDNVLENEES LKKQLKKLKQ SQVDGVMVDV 

       130        140        150        160        170        180 
WWGIVESKGP KQYQWSAYRN LFAIVQSFGL KLQAIMSFHR CGGNIGDDVN IPIPKWVLEI 

       190        200        210        220        230        240 
GDSNPDIFYT NKSGNRNKEC LSLSVDNLSL FRGRTAVEMY RDYMKSFREN MEDFISSGVI 

       250        260        270        280        290        300 
IDIEVGLGPA GELRYPSYSE TQGWVFPGIG EFQCYDKYLR SDYEEEVRRI GHPEWKLPEN 

       310        320        330        340        350        360 
AGEYNSVPGE TEFFEYSNGT YLKEEGNFFL SWYSKKLLLH GDQILDEANK VFLGCKLKIA 

       370        380        390        400        410        420 
AKVSGIHWWY KTESHAAELT AGYYNLKNRD GYRAIAKIMR RHHAILNFTC LEMKNTEQPA 

       430        440        450        460        470        480 
KAKSGPQELV QQVLSSGWRE GIEVAGENAL PRFDRNGYNQ IILNARPNGV NQDGKPRMFG 

       490        500        510        520        530        540 
FTYLRLSDKL LNEPNFSTFK MFLKRMHANQ EYCSEPERYN HELLPLERSR NDESLEMFME 

       550        560        570 
ETEPFDPFPW LDETDMSIRP FESVLSLLRS TFLRKKS 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [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].
Strain: cv. Columbia.
[4]"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: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC005700 Genomic DNA. Translation: AAC69949.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC08663.1.
AY136463 mRNA. Translation: AAM97128.1.
IPIIPI00524134.
PIRC84731.
RefSeqNP_180788.2. NM_128788.2.
UniGeneAt.38097.
At.38099.

3D structure databases

HSSPHSSP built from PDB template 1UKO based on UniProtKB P10538.
ProteinModelPortalQ8L762.
SMRQ8L762. Positions 73-558.
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Proteomic databases

PRIDEQ8L762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G32290.1; AT2G32290.1; AT2G32290.
GeneID817789.
GenomeReviewsGene locus AT2G32290 in contig CT485783_GR.
KEGGath:AT2G32290.

Organism-specific databases

TAIRAt2g32290.

Phylogenomic databases

eggNOGNOG77898.
GeneTreeEPGT00070000030150.
HOGENOMHBG747772.
InParanoidQ8L762.
OMARENMEDF.
PhylomeDBQ8L762.
ProtClustDBPLN02801.

Gene expression databases

GenevestigatorQ8L762.

Family and domain databases

InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBAM6_ARATH
AccessionPrimary (citable) accession number: Q8L762
Secondary accession number(s): Q9ZV58
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: October 1, 2002
Last modified: December 14, 2011
This is version 59 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