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Q5BCI8 (MANBA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-mannosidase A

EC=3.2.1.25
Alternative name(s):
Mannanase A
Short name=Mannase A
Gene names
Name:mndA
ORF Names:AN1742
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length940 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Pathway

Glycan metabolism; N-glycan degradation.

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmannan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 940919Beta-mannosidase A
PRO_0000394649

Sites

Active site4761Proton donor By similarity

Amino acid modifications

Glycosylation151N-linked (GlcNAc...) Potential
Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation3141N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation3441N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential
Glycosylation6051N-linked (GlcNAc...) Potential
Glycosylation6261N-linked (GlcNAc...) Potential
Glycosylation6531N-linked (GlcNAc...) Potential
Glycosylation7331N-linked (GlcNAc...) Potential
Glycosylation7611N-linked (GlcNAc...) Potential
Glycosylation7851N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5BCI8 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 45E1CBB33D2AFAF0

FASTA940105,765
        10         20         30         40         50         60 
MHFHGIATQA VLASNITTGS GRHVSLSDVK WTLSSSALNS TVPASLPSQA HLDLLNAGVI 

        70         80         90        100        110        120 
DDPYYGLNEI DLQWIAQANW TYTSDPIPDL LEEYESTWLV FEGLDTFATV TFCGHNIAST 

       130        140        150        160        170        180 
NNQFRQYAFD VSSALKECTG GPVVRIDFAS APNTVDAIAA DPKTPVWPVQ LTAQLPNRWL 

       190        200        210        220        230        240 
MRKQQSDFGW DWGPAFAPCG PWKPAYVVQL EKTAPIHVLN TDLDIYRQGN INHLPPDQKQ 

       250        260        270        280        290        300 
PWVVNASIDF IGRLPAEPRL LIEIKELETG DVLASQISDS VTLIGTSITG VTTLKDASPK 

       310        320        330        340        350        360 
LWWPSSLGAQ NLYNVTITVF NKTEEVARIT KRTGFRTIFL NQRNITATQL SQGIAPGANW 

       370        380        390        400        410        420 
HFEVNGKEFY AKGSNFIPPD TFWPRVTKQK MTRLLDAVVA GNQNMLRIWS SGAYLPDFIY 

       430        440        450        460        470        480 
DLADERGILL WSEFQFSDSM YPVDEDFLDN VAQEVVYNVR RVNHHPSLAL WAGGNEIESL 

       490        500        510        520        530        540 
MLPLTREADP DNYPKYLAEY EKLYISLILP LVYENTRSIS YSPSSTTEGY LSVNLSAPVP 

       550        560        570        580        590        600 
MTERYENDEP GAYYGDTDYY NYDTTVSFDY SIYPVGRFAN EFGFHSMPSL QTWQQVADPE 

       610        620        630        640        650        660 
DLYFNSTTVV IHNRHYTSEG YGRIENSSRG MAEMTLGVER YYPIPDNPDS VANFSAWCLA 

       670        680        690        700        710        720 
TQLFQADFYK SQIQFYRRGS GMPERQLGSL YWQLEDIWQG PTWAGIEYDG RWKVLHYVAR 

       730        740        750        760        770        780 
DVYQPIIVSP FWNYTTGDLE IYVTADLWES AAGTVNLKWL NLSGEQIIDN AGTPTEIPFT 

       790        800        810        820        830        840 
VGAINTTKVY STNIHDLNLP DTRASILTLS LSSQANLPNA AVKTSLTHEN HFTPSFPKDL 

       850        860        870        880        890        900 
ELVNPGLELS YDAHSGIFTV EAKSGVSLYT WLDYPAGLVG YFTENAFLLV PGQKKKVQFV 

       910        920        930        940 
VQDGPKDQDW EWQSEVTVRS LWDQKSSTFL YALRVATGRP 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000027 Genomic DNA. Translation: EAA64028.1.
BN001307 Genomic DNA. Translation: CBF85479.1.
RefSeqXP_659346.1. XM_654254.1.

3D structure databases

ProteinModelPortalQ5BCI8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00008389.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008389; CADANIAP00008389; CADANIAG00008389.
GeneID2874889.
KEGGani:AN1742.2.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000216059.
KOK01192.
OMACHATQLF.
OrthoDBEOG78D7TH.

Enzyme and pathway databases

UniPathwayUPA00280.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProIPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR028369. Mannanase.
[Graphical view]
PANTHERPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANBA_EMENI
AccessionPrimary (citable) accession number: Q5BCI8
Secondary accession number(s): C8VP45
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: March 19, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries