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Protein

Alpha-amylase

Gene

LOC101163630

Organism
Oryzias latipes (Japanese rice fish) (Japanese killifish)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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 annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151CalciumCombined sources
Metal bindingi173 – 1731Calcium; via carbonyl oxygenCombined sources
Metal bindingi182 – 1821CalciumCombined sources
Metal bindingi216 – 2161Calcium; via carbonyl oxygenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotationSAAS annotation (EC:3.2.1.1UniRule annotationSAAS annotation)
Gene namesi
Name:LOC101163630Imported
OrganismiOryzias latipes (Japanese rice fish) (Japanese killifish)Imported
Taxonomic identifieri8090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataOvalentariaAtherinomorphaeBeloniformesAdrianichthyidaeOryziinaeOryzias
ProteomesiUP000001038 Componenti: Unplaced

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 101Combined sources
Disulfide bondi85 ↔ 130Combined sources
Disulfide bondi156 ↔ 175Combined sources
Disulfide bondi394 ↔ 400Combined sources
Disulfide bondi466 ↔ 478Combined sources

Interactioni

Protein-protein interaction databases

STRINGi8090.ENSORLP00000024837.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VM5X-ray2.85A16-512[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000002882.
InParanoidiH2N0D4.
OMAiRNGMVHL.
OrthoDBiEOG7RJPR2.
TreeFamiTF312850.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

H2N0D4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLFVLIALF GLGFAQHNPN TRDGRTAIVH LFEWRWADIA AECERFLGPK
60 70 80 90 100
GFAGVQISPP NEHILVSSPW RPWWQRYQPI SYNLCSRSGG ENELRDMITR
110 120 130 140 150
CNNVGVNVYV DAVINHMCGA GGGEGTHSSC GSWFNANNKD FPSVPYSNLD
160 170 180 190 200
FNDGKCKTGS GNIENYGDPY QVRDCRLVGL LDLALEKDYV RGKVADFMNK
210 220 230 240 250
LIDMGVAGFR VDACKHMWPG DLDNVYRRLN NLNTKWFPGG SRPFIFQEVI
260 270 280 290 300
DLGGEPITTG EYVGLGRVTE FKYGARLGEL FRKWNGQKLS YTKNWGEGWG
310 320 330 340 350
FMADGNAVVF TDNHDNQRGH GAGGASILTF WDPRLYKMAV GYMLAHPYGF
360 370 380 390 400
TRVMSSYSWD RNFVNGKDEN DWIGPPSNGD GSTKPVPINP DQTCGDGWVC
410 420 430 440 450
EHRWRQIMNM VQFRNVVNGQ PHANWWDNGN NQVAFGRGNR GFIVFNNDDW
460 470 480 490 500
ALDVTLNTGL PGGTYCDVIS GNKDGGSCTG KQITVGGDGR AHFYINNSEE
510
DPFIAIHADS KL
Length:512
Mass (Da):57,167
Last modified:March 21, 2012 - v1
Checksum:iFFDA8EFC8F527D02
GO

Sequence databases

RefSeqiXP_004085115.1. XM_004085067.2.

Genome annotation databases

EnsembliENSORLT00000024838; ENSORLP00000024837; ENSORLG00000020006.
GeneIDi101163630.

Cross-referencesi

Sequence databases

RefSeqiXP_004085115.1. XM_004085067.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VM5X-ray2.85A16-512[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi8090.ENSORLP00000024837.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSORLT00000024838; ENSORLP00000024837; ENSORLG00000020006.
GeneIDi101163630.

Phylogenomic databases

GeneTreeiENSGT00390000002882.
InParanoidiH2N0D4.
OMAiRNGMVHL.
OrthoDBiEOG7RJPR2.
TreeFamiTF312850.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hd-rRImported.
  2. "Structural and functional characterization of recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris."
    Mizutani K., Toyoda M., Otake Y., Yoshioka S., Takahashi N., Mikami B.
    Biochim. Biophys. Acta 1824:954-962(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 16-512 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.
  3. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Hd-rRImported.

Entry informationi

Entry nameiH2N0D4_ORYLA
AccessioniPrimary (citable) accession number: H2N0D4
Entry historyi
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: June 24, 2015
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

3D-structureCombined sources, 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.