Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q02751

- MALT_CANAX

UniProt

Q02751 - MALT_CANAX

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Alpha-glucosidase

Gene

MAL2

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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 sitei206 – 2061NucleophileBy similarity
Active sitei263 – 2631Proton donorBy similarity
Sitei338 – 3381Transition state stabilizerBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. maltose metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Maltose metabolism

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.
mycoCLAPiAGL13B_CANAL.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-glucosidase (EC:3.2.1.20)
Alternative name(s):
Maltase
Gene namesi
Name:MAL2
Synonyms:MAL1
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 570569Alpha-glucosidasePRO_0000054327Add
BLAST

Expressioni

Inductioni

By maltose and sucrose. Repressed by glucose.

Structurei

3D structure databases

ProteinModelPortaliQ02751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiCOG0366.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. 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.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q02751-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEHKWWKEA VVYQIWPASY KDSNGDGVGD IPGIISTLDY IASLGVTTVW
60 70 80 90 100
LSPMYDSPQD DMGYDVSDYE NVYSKYGTLQ DMDRLIAGCH DRGLKLILDL
110 120 130 140 150
VINHTSVEHK WFKESRSSKD NPKRDWYIWK PPRIDSNGNK HPPNNWGSYF
160 170 180 190 200
SGSAWKYDEL TGEYYLHLFA ESQPDLNWEN KECREAIYNS AIKFWLDKGV
210 220 230 240 250
DGFRIDTAGM YSKYQHFKDA PVAFPDTEFQ PCEIYHKNGP RIHEFHKEMA
260 270 280 290 300
KVMEPYDTMT VGEVGHSTRE QALKYVSAAE KEMNMMFLFD VVELGSDPRD
310 320 330 340 350
RFRYNGFDLV DLKKAIKSQG EFAEGTDAWS TVFIENHDQA RAISRFGNDS
360 370 380 390 400
PEFRVLSGKA IAMLQCCLTG TLFIYQGQEI GMTNVPRSWP IEEYKDINTI
410 420 430 440 450
NYYRAFKEKY GKDADYKQKE EKLVDVINRL ARDNARTPVQ WSHQQYAGFS
460 470 480 490 500
EVEPWMRVND NYKEINVEDQ DGDDHSLLNF YRKLLKLRGE YKDLFVYGEM
510 520 530 540 550
KFLDFDDKKL FTFAKEAPGS PVAYIVINFS GEDVKFEPLI KGNYKLVLTN
560 570
VDKDSKDALS PYEARMYVVD
Length:570
Mass (Da):66,210
Last modified:January 23, 2007 - v4
Checksum:iF688281082968887
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M94674 mRNA. Translation: AAA34350.2.
PIRiA45249.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M94674 mRNA. Translation: AAA34350.2 .
PIRi A45249.

3D structure databases

ProteinModelPortali Q02751.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.
mycoCLAPi AGL13B_CANAL.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0366.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProi 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
[Graphical view ]
SMARTi SM00642. Aamy. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of a Candida albicans maltase gene involved in sucrose utilization."
    Geber A., Williamson P.R., Rex J.H., Sweeney E.C., Bennett J.E.
    J. Bacteriol. 174:6992-6996(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-27.
    Strain: ATCC 32354 / B311.

Entry informationi

Entry nameiMALT_CANAX
AccessioniPrimary (citable) accession number: Q02751
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 80 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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