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Protein

Beta-amylase

Gene

PHYPADRAFT_222395

Organism
Physcomitrella patens subsp. patens (Moss)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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.UniRule annotation

GO - Molecular functioni

  1. beta-amylase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradationUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-amylaseUniRule annotation (EC:3.2.1.2UniRule annotation)
Gene namesi
ORF Names:PHYPADRAFT_222395Imported
OrganismiPhyscomitrella patens subsp. patens (Moss)Imported
Taxonomic identifieri3218 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella
ProteomesiUP000006727 Componenti: Partially assembled WGS sequence

Interactioni

Protein-protein interaction databases

STRINGi3218.JGI222395.

Structurei

3D structure databases

ProteinModelPortaliA9THN6.
SMRiA9THN6. Positions 37-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.UniRule annotation

Phylogenomic databases

InParanoidiA9THN6.
KOiK01177.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9THN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTMFPEHKS LLDWDNTADE WKEHAFHETP TSRGVHGGVP VFVMLPLDSV
60 70 80 90 100
NINNTLKRRR ALNASLLALK SAGVEGVMMD VWWGIVEKEG PRNYNWSAYR
110 120 130 140 150
ELIDMVRKHG LKVQAVMSFH QCGGNVGDSC NIPLPPWVLE EVQKNPDLAY
160 170 180 190 200
TDKAGKRNAE YISLGADNVP ALKGRTPVQC YADFMRSFRD NFKDLLGDVI
210 220 230 240 250
IEIQCGMGPA GELRYPSYPE SEGRWRFPGI GEFQCYDKYM LASLKANAQA
260 270 280 290 300
LGKPAWGHGG PCDAGNYNQW PDETGFFHRD GSWCSEYGQF FMEWYSEMIL
310 320 330 340 350
AHGERLLASA SGIFKGTGAV ISGKVAGIHW HYGTRSHAAE LTAGYYNTRT
360 370 380 390 400
RDGYATIAQM FAKYGVTLNF TCIEMRDYEQ PSQASCSPEG LVRQVALATR
410 420 430 440 450
RAGIPMAGEN ALPRFDSSAH EQIVRKSRLR MNEHGDCHEE YEPMAAFTFL
460 470 480 490 500
RMCESLFHSE NWKLFVPFVR HMEEGRTFQP WEEEHHRTET HVHATRPLVQ

EAASLMY
Length:507
Mass (Da):57,417
Last modified:February 4, 2008 - v1
Checksum:i8ECB1B76D811EC85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS545122 Genomic DNA. Translation: EDQ57039.1.
RefSeqiXP_001778149.1. XM_001778097.1.
UniGeneiPpa.11850.

Genome annotation databases

GeneIDi5941359.
KEGGippp:PHYPADRAFT_222395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS545122 Genomic DNA. Translation: EDQ57039.1.
RefSeqiXP_001778149.1. XM_001778097.1.
UniGeneiPpa.11850.

3D structure databases

ProteinModelPortaliA9THN6.
SMRiA9THN6. Positions 37-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3218.JGI222395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5941359.
KEGGippp:PHYPADRAFT_222395.

Phylogenomic databases

InParanoidiA9THN6.
KOiK01177.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants."
    Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., Suzuki Y.
    , Hashimoto S.-I., Yamaguchi K., Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L.
    Science 319:64-69(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Gransden 2004Imported.

Entry informationi

Entry nameiA9THN6_PHYPA
AccessioniPrimary (citable) accession number: A9THN6
Entry historyi
Integrated into UniProtKB/TrEMBL: February 4, 2008
Last sequence update: February 4, 2008
Last modified: January 6, 2015
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.