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Q9UUZ3

- MANBA_ASPNG

UniProt

Q9UUZ3 - MANBA_ASPNG

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Protein
Beta-mannosidase A
Gene
mndA
Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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).By similarity3 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.2 Publications

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.

Temperature dependencei

Optimum temperature is 70 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei479 – 4791Proton donor By similarityBy similarity

GO - Molecular functioni

  1. beta-mannosidase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17577.
UniPathwayiUPA00280.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.
mycoCLAPiMND2A_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-mannosidase A (EC:3.2.1.25)
Alternative name(s):
Mannanase A
Short name:
Mannase A
Gene namesi
Name:mndA
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 931910Beta-mannosidase A
PRO_0000012168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi79 – 791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi247 – 2471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi282 – 2821N-linked (GlcNAc...) Reviewed prediction
Glycosylationi347 – 3471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi550 – 5501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi608 – 6081N-linked (GlcNAc...) Reviewed prediction
Glycosylationi658 – 6581N-linked (GlcNAc...) Reviewed prediction
Glycosylationi738 – 7381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi790 – 7901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi798 – 7981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi830 – 8301N-linked (GlcNAc...) Reviewed prediction
Glycosylationi918 – 9181N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9UUZ3.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family. Beta-mannosidase A subfamily.By similarity

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR008979. Galactose-bd-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9UUZ3-1 [UniParc]FASTAAdd to Basket

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MRHSIGLAAA LLAPTLPVAL GQHIRDLSSE KWTLSSRALN RTVPAQFPSQ    50
VHLDLLRAGV IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYGSTWLV 100
FDGLDTFATI SILWTANRIH GQSVSPVSGS MYLPALEACQ RRILIRKVSF 150
RGGVTAEVNT CYLHIEWPDD VQLTYEYPNR WFMRKEQSDF GWDWGPAFAP 200
AGPWKPAYIV QLDKKESVYV LNTDLDIYRK NQINYLPPDQ SQPWVVNASI 250
DILGPLPAKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLN 300
PKLWWPQSSV IRTSTMFLSL SKVEGTRPWP VWTNGRASAP FFLNQRNITE 350
VQRAQGIAPG ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EERISRLFDA 400
VVVGNQNMLR VWSSGAYLHD YIYDLADEKG ILLWSEFEFS DALYPSDDAF 450
LENVAAEIVY NVRRVNHHPS LALWAGGNEI ESLMLPRVKD AAPSSYSYYV 500
GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA PVPMAERYDN 550
TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV 600
DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVISYYPIP 650
SKSDHISNFS AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE 700
DIWQAPSWAG IEYGGRWKVL HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS 750
DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK SVPFTVGGLN STRIYGTNVS 800
SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS WPKDLKIVDP 850
GLKLGYSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK 900
EIGFTVLDDT TNGAWVRNIT VQSLWDQKVR G 931
Length:931
Mass (Da):104,390
Last modified:May 1, 2000 - v1
Checksum:iD296E185EA3BF430
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ251874 Genomic DNA. Translation: CAB63902.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ251874 Genomic DNA. Translation: CAB63902.1 .

3D structure databases

ProteinModelPortali Q9UUZ3.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL5417.

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.
mycoCLAPi MND2A_ASPNG.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00280 .
BioCyci MetaCyc:MONOMER-17577.

Family and domain databases

Gene3Di 3.20.20.80. 2 hits.
InterProi IPR008979. Galactose-bd-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of Aspergillus niger genes encoding an alpha-galactosidase and a beta-mannosidase involved in galactomannan degradation."
    Ademark P., de Vries R.P., Haegglund P., Staalbrand H., Visser J.
    Eur. J. Biochem. 268:2982-2990(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
  2. "Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger."
    Ademark P., Lundqvist J., Haegglund P., Tenkanen M., Torto N., Tjerneld F., Staalbrand H.
    J. Biotechnol. 75:281-289(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 490-504, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION.
    Strain: ATCC 46890.
  3. "Phylogenetic analysis and substrate specificity of GH2 beta-mannosidases from Aspergillus species."
    Reddy S.K., Rosengren A., Klaubauf S., Kulkarni T., Karlsson E.N., de Vries R.P., Stalbrand H.
    FEBS Lett. 587:3444-3449(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Entry informationi

Entry nameiMANBA_ASPNG
AccessioniPrimary (citable) accession number: Q9UUZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 66 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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