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A9T0X2

- A9T0X2_PHYPA

UniProt

A9T0X2 - A9T0X2_PHYPA

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Protein
Alpha-amylase
Gene
PHYPADRAFT_138602
Organism
Physcomitrella patens subsp. patens (Moss)
Status
Unreviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.UniRule annotation

GO - Molecular functioni

  1. alpha-amylase activity Source: InterPro
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotation (EC:3.2.1.1UniRule annotation)
Gene namesi
ORF Names:PHYPADRAFT_138602Imported
OrganismiPhyscomitrella patens subsp. patens (Moss)
Taxonomic identifieri3218 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella
ProteomesiUP000006727: Partially assembled WGS sequence

Interactioni

Protein-protein interaction databases

STRINGi3218.JGI138602.

Structurei

3D structure databases

ProteinModelPortaliA9T0X2.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotation

Phylogenomic databases

KOiK01176.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR012850. A-amylase_bs_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Fragment.

A9T0X2-1 [UniParc]FASTAAdd to Basket

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VFSQGFDWES HNHNPSWWIH FQSKIEDLFE LGITDVWLPP ASQSVDKHGY    50
LPGQLYNLDS SRYGKGIELR NLLDVLHMHG MCGIADIVIN HRTAGTQDKQ 100
GHWNIFDGGV PDKRLAWGAW AVVDNDVYNS GGKGKHDTGE SYGAAPDLDH 150
TSKRVQDELT DWMNWLRAEV GFDGWRFDFA KGYGPQYCGL YCERTCPSFA 200
VGEIWTSMSY KDSSLLADQD AHRQKLCDWI DGTGGRVCAF DFTTKGILQT 250
AVEGQLWRLQ DSFGKPPGLI GWWPQKAVTF VDNHDTGSTQ RHWSFPDDKI 300
AMGYAYILTH PGIPCIFYDH YFNTHLKFQI KELVQVRLRN HINTESKVSI 350
KIAEADIYVA SIADRVLVKL GPRQVPISLS 380
Length:380
Mass (Da):43,067
Last modified:February 5, 2008 - v1
Checksum:iC3BBFCDD032993EF
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS545037 Genomic DNA. Translation: EDQ62933.1.
RefSeqiXP_001772280.1. XM_001772228.1.

Genome annotation databases

GeneIDi5935498.
KEGGippp:PHYPADRAFT_138602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS545037 Genomic DNA. Translation: EDQ62933.1 .
RefSeqi XP_001772280.1. XM_001772228.1.

3D structure databases

ProteinModelPortali A9T0X2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3218.JGI138602.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5935498.
KEGGi ppp:PHYPADRAFT_138602.

Phylogenomic databases

KOi K01176.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR012850. A-amylase_bs_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Gransden 2004.

Entry informationi

Entry nameiA9T0X2_PHYPA
AccessioniPrimary (citable) accession number: A9T0X2
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

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