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Entry version 82 (23 Feb 2022)
Sequence version 1 (01 May 2000)
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Protein

Beta-mannosidase A

Gene

mndA

Organism
Aspergillus niger
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan. Releases the terminal mannose residue from mannobiose and mannotriose, as well as from galactosyl-mannobiose (GM2), galactosyl-mannotriose (GM3) and di-galactosyl-mannopentaose (G2M5).

2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 4048 min(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.
  1. KM=0.3 mM for p-nitrophenyl-beta-mannopyranoside1 Publication

pH dependencei

Optimum pH is 2.5-5.1 Publication

Temperature dependencei

Optimum temperature is 70 degrees Celsius.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: N-glycan degradation

This protein is involved in the pathway N-glycan degradation, which is part of Glycan metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway N-glycan degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei479Proton donorBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q9UUZ3

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00280

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH2, Glycoside Hydrolase Family 2

CLAE, a database of fungal genes encoding lignocellulose-active proteins

More...
CLAEi
MND2A_ASPNG

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Beta-mannosidase A (EC:3.2.1.25)
Alternative name(s):
Mannanase A
Short name:
Mannase A
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:mndA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAspergillus niger
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri5061 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillusAspergillus subgen. Circumdati

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:An11g06540
FungiDB:ASPNIDRAFT2_1160135
FungiDB:ATCC64974_92080
FungiDB:M747DRAFT_299830

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5417

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001216822 – 931Beta-mannosidase AAdd BLAST910

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi40N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi79N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi247N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi282N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi347N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi550N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi608N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi658N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi738N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi790N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi798N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi830N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi918N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9UUZ3

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
FWNYTTG

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR041625, Beta-mannosidase_Ig
IPR008979, Galactose-bd-like_sf
IPR017853, Glycoside_hydrolase_SF
IPR013783, Ig-like_fold
IPR041447, Mannosidase_ig

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17753, Ig_mannosidase, 1 hit
PF17786, Mannosidase_ig, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49785, SSF49785, 1 hit
SSF51445, SSF51445, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UUZ3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRHSIGLAAA LLAPTLPVAL GQHIRDLSSE KWTLSSRALN RTVPAQFPSQ
60 70 80 90 100
VHLDLLRAGV IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYGSTWLV
110 120 130 140 150
FDGLDTFATI SILWTANRIH GQSVSPVSGS MYLPALEACQ RRILIRKVSF
160 170 180 190 200
RGGVTAEVNT CYLHIEWPDD VQLTYEYPNR WFMRKEQSDF GWDWGPAFAP
210 220 230 240 250
AGPWKPAYIV QLDKKESVYV LNTDLDIYRK NQINYLPPDQ SQPWVVNASI
260 270 280 290 300
DILGPLPAKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLN
310 320 330 340 350
PKLWWPQSSV IRTSTMFLSL SKVEGTRPWP VWTNGRASAP FFLNQRNITE
360 370 380 390 400
VQRAQGIAPG ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EERISRLFDA
410 420 430 440 450
VVVGNQNMLR VWSSGAYLHD YIYDLADEKG ILLWSEFEFS DALYPSDDAF
460 470 480 490 500
LENVAAEIVY NVRRVNHHPS LALWAGGNEI ESLMLPRVKD AAPSSYSYYV
510 520 530 540 550
GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA PVPMAERYDN
560 570 580 590 600
TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV
610 620 630 640 650
DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVISYYPIP
660 670 680 690 700
SKSDHISNFS AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE
710 720 730 740 750
DIWQAPSWAG IEYGGRWKVL HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS
760 770 780 790 800
DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK SVPFTVGGLN STRIYGTNVS
810 820 830 840 850
SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS WPKDLKIVDP
860 870 880 890 900
GLKLGYSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK
910 920 930
EIGFTVLDDT TNGAWVRNIT VQSLWDQKVR G
Length:931
Mass (Da):104,390
Last modified:May 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD296E185EA3BF430
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ251874 Genomic DNA Translation: CAB63902.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ251874 Genomic DNA Translation: CAB63902.1

3D structure databases

SMRiQ9UUZ3
ModBaseiSearch...

Chemistry databases

ChEMBLiCHEMBL5417

Protein family/group databases

CAZyiGH2, Glycoside Hydrolase Family 2
CLAEiMND2A_ASPNG

Organism-specific databases

VEuPathDBiFungiDB:An11g06540
FungiDB:ASPNIDRAFT2_1160135
FungiDB:ATCC64974_92080
FungiDB:M747DRAFT_299830

Phylogenomic databases

OMAiFWNYTTG

Enzyme and pathway databases

UniPathwayiUPA00280
SABIO-RKiQ9UUZ3

Family and domain databases

Gene3Di2.60.40.10, 3 hits
InterProiView protein in InterPro
IPR041625, Beta-mannosidase_Ig
IPR008979, Galactose-bd-like_sf
IPR017853, Glycoside_hydrolase_SF
IPR013783, Ig-like_fold
IPR041447, Mannosidase_ig
PfamiView protein in Pfam
PF17753, Ig_mannosidase, 1 hit
PF17786, Mannosidase_ig, 1 hit
SUPFAMiSSF49785, SSF49785, 1 hit
SSF51445, SSF51445, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMANBA_ASPNG
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UUZ3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: February 23, 2022
This is version 82 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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