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Protein

Alpha-galactosidase D

Gene

aglD

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Active on paranitrophenyl-alpha-galactoside but not on raffinose, locust bean gum and gum guar.1 Publication

Catalytic activityi

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.

pH dependencei

Optimum pH is 5.0.1 Publication

Temperature dependencei

Optimum temperature is 52 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei156 – 1561NucleophileBy similarity
Active sitei223 – 2231Proton donorBy similarity

GO - Molecular functioni

  • alpha-galactosidase activity Source: UniProtKB
  • raffinose alpha-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

mycoCLAPiMEL27D_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-galactosidase D (EC:3.2.1.22)
Alternative name(s):
Melibiase D
Gene namesi
Name:aglD
ORF Names:AN7152
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome IV
  • UP000005890 Componenti: Partially assembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AN7152.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 659639Alpha-galactosidase DPRO_0000395075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence analysis
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi125 ↔ 158By similarity
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence analysis
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence analysis
Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence analysis
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence analysis
Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence analysis
Glycosylationi583 – 5831N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2055Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000217283.
InParanoidiQ5AX28.
KOiK07407.
OrthoDBiEOG7CNZQQ.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR013780. Glyco_hydro_b.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5AX28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALVPMVVA ATALASPAPA LKPRLDDGLA RTPQMGWNTY NQYNCFPNES
60 70 80 90 100
IVHENAQALV DTGLADLGYR YVTIDCGWGV EDRLPNGTIT WNPELFPQGF
110 120 130 140 150
PAMGQYLHDL GLLFGVYGDS GILLCGSPPN ITGSLYYEDI DARTFAEWGA
160 170 180 190 200
DSLKYDNCYS DAATNYPNVN YAPSTSPHPR FANMSRYIQA QDRDILFQVC
210 220 230 240 250
EWGIDFPALW APEIGHSWRI GNDIIPHWRS IFRTLNQAVP QTDFAGPGQW
260 270 280 290 300
PDLDMLLVGL DGVLTVPEEQ THFSLWSILK SPLTIGAAIP GMRAESLEIL
310 320 330 340 350
SNADVIAFNQ DALGVSAALR RRWSDEGYEV WSGPLEGGRT IAAVINWRDE
360 370 380 390 400
DREITLDLPD IGLQYAETLQ NVWADETVNG VKTSYSSVVE AHGVMLVQLA
410 420 430 440 450
ETVEEGVYPA DVFAATNRDV TTFSDVYAIT SSPNFVLNIT LTEVTAAATN
460 470 480 490 500
ITIITDSSRR PISTSIPAGS SSISTSVSLI AGSNNTITIR NAPPLSSITL
510 520 530 540 550
SPPEPTYYTG AQDFTLTSPA GAYTCPDAYC LPAGSKIVDL STESAATAHI
560 570 580 590 600
NSSTSGSKYL EIDYINNEVA FDSSWGWGAN SRNLTIKVND NNPVRLEVPL
610 620 630 640 650
SGRHSELFGP GLGWWDSGRL GVLTDGWIKG TNELVLSNEG GEGGFTKYAP

DVVGIAVYD
Length:659
Mass (Da):71,482
Last modified:June 15, 2010 - v2
Checksum:iF7D5BC5D10F6ECAB
GO

Sequence cautioni

The sequence CBF78972.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA61404.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490505 mRNA. Translation: ABF50881.1.
AACD01000122 Genomic DNA. Translation: EAA61404.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF78972.1. Sequence problems.
RefSeqiXP_664756.1. XM_659664.1.

Genome annotation databases

EnsemblFungiiCADANIAT00000305; CADANIAP00000305; CADANIAG00000305.
EAA61404; EAA61404; AN7152.2.
GeneIDi2870158.
KEGGiani:AN7152.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490505 mRNA. Translation: ABF50881.1.
AACD01000122 Genomic DNA. Translation: EAA61404.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF78972.1. Sequence problems.
RefSeqiXP_664756.1. XM_659664.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiMEL27D_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00000305; CADANIAP00000305; CADANIAG00000305.
EAA61404; EAA61404; AN7152.2.
GeneIDi2870158.
KEGGiani:AN7152.2.

Organism-specific databases

EuPathDBiFungiDB:AN7152.

Phylogenomic databases

HOGENOMiHOG000217283.
InParanoidiQ5AX28.
KOiK07407.
OrthoDBiEOG7CNZQQ.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR013780. Glyco_hydro_b.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiAGALD_EMENI
AccessioniPrimary (citable) accession number: Q5AX28
Secondary accession number(s): C8VD73, Q1HFR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: May 11, 2016
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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 one 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.