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O04893

- AGLU_SPIOL

UniProt

O04893 - AGLU_SPIOL

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Protein

Alpha-glucosidase

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Alpha-glucosidase I and II have high activity towards malto-oligosaccharides and starch, while form III and IV have high activity towards malto-oligosaccharides but low activity toward starch.

Catalytic activityi

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei465 – 4651By similarity
Active sitei468 – 4681By similarity
Active sitei564 – 5641Proton donorBy similarity

GO - Molecular functioni

  1. alpha-1,4-glucosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. maltose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-glucosidase (EC:3.2.1.20)
Alternative name(s):
Maltase
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 903879Alpha-glucosidasePRO_0000018584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi600 – 6001N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Four different forms (I-IV) may be produced by post-translational modification.

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliO04893.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O04893-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKKIPSLAL GILLVFLLQY LVAGISTSEN DPEGVIGYGY KVKSVKVDSG
60 70 80 90 100
TRRSLTALPQ LVKNSSVYGP DIQLLSITAS LESNDRLRVR ITDAKHRRWE
110 120 130 140 150
IPDNILHRHQ PPPPPPHSLS SLYRTLLSSP TTNRRKILLS HPNSDLTFSL
160 170 180 190 200
INTTPFGFTI SRKSTHDVLF DATPDPTNPN TFLIFIDQYL HLTSSLPGTR
210 220 230 240 250
AHIYGLGEHS KPTFQLAHNQ TLTMRAADIP SSNPDVNLYG SHPFYMDVRS
260 270 280 290 300
SPVAGSTHGV LLLNSNGMDV EYTGNRITYK VIGGIIDLYF FAGPSPGQVV
310 320 330 340 350
EQFTRVIGRP APMPYWAFGF QQCRYGYHDV YELQSVVAGY AKAKIPLEVM
360 370 380 390 400
WTDIDYMDAY KDFTLDPVNF PLDKMKKFVN NLHKNGQKYV VILDPGISTN
410 420 430 440 450
KTYETYIRGM KHDVFLKRNG KPYLGSVWPG PVYFPDFLKP SALTFWTDEI
460 470 480 490 500
KRFLNLLPVD GLWIDMNEIS NFISSPPIPG STLDNPPYKI NNSGVMLPII
510 520 530 540 550
NKTIPPTAMH YGDIPEYNVH NLFGYLEARV TRAALIKLTE KRPFVLSRST
560 570 580 590 600
FSGSGKYTAH WTGDNAATWN DLVYSIPSML DFGLFGIPMV GADICGFLGN
610 620 630 640 650
TTEELCRRWI QLGAFYPFSR DHSSLGTTYQ ELYRWESVAA SARKVLGLRY
660 670 680 690 700
TLLPYFYTLM YEAQLNGIPI ARPLFFSFPD DIKTYGISSQ FLLGKGVMVS
710 720 730 740 750
PVLKPGVVSV TAYFPRGNWF DLFDYTRSVT ASTGRYVTLS APPDHINVHI
760 770 780 790 800
QEGNILAMQG KAMTTQAARK TPFHLLVVMS DCGASFGELF LDDGVEVTMG
810 820 830 840 850
VNRGKWTFVK FIAASAKQTC IITSDVVSGE FAVSQKWVID KVTILGLRKG
860 870 880 890 900
TKINGYTVRT GAVTRKGDKS KLKSTPDRKG EFIVAEISGL NLLLGREFKL

VLH
Length:903
Mass (Da):100,881
Last modified:July 1, 1997 - v1
Checksum:i5B054E27C20EC33A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D86624 mRNA. Translation: BAA19924.1.
PIRiT09143.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D86624 mRNA. Translation: BAA19924.1 .
PIRi T09143.

3D structure databases

ProteinModelPortali O04893.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.70. 2 hits.
InterProi IPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and characterization of a cDNA encoding alpha-glucosidase from spinach."
    Sugimoto M., Furui S., Suzuki Y.
    Plant Mol. Biol. 33:765-768(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Dash.

Entry informationi

Entry nameiAGLU_SPIOL
AccessioniPrimary (citable) accession number: O04893
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3