ID   MANBB_ASPNC             Reviewed;         844 AA.
AC   A2QYN2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   02-SEP-2026, entry version 89.
DE   RecName: Full=Beta-mannosidase B;
DE            EC=3.2.1.25;
DE   AltName: Full=Mannanase B;
DE            Short=Mannase B;
GN   Name=mndB; ORFNames=An12g01850;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose
CC       residue from the non-reducing end of beta-mannosidic oligosaccharides
CC       of various complexity and length. Prefers mannobiose over mannotriose
CC       and has no activity against polymeric mannan. Is also severely
CC       restricted by galactosyl substitutions at the +1 subsite (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC         in beta-D-mannosides.; EC=3.2.1.25;
CC   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC   -!- MISCELLANEOUS: In contrast to clade A beta-mannosidases, which are
CC       likely secreted, clade B proteins appear to be intracellular.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000305}.
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DR   EMBL; AM270263; CAK48467.1; -; Genomic_DNA.
DR   RefSeq; XP_001395271.1; XM_001395234.3.
DR   AlphaFoldDB; A2QYN2; -.
DR   SMR; A2QYN2; -.
DR   GlyCosmos; A2QYN2; 1 site, No reported glycans.
DR   EnsemblFungi; CAK48467; CAK48467; An12g01850.
DR   GeneID; 4985535; -.
DR   KEGG; ang:An12g01850; -.
DR   VEuPathDB; FungiDB:An12g01850; -.
DR   HOGENOM; CLU_005015_1_0_1; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000006706; Chromosome 3L.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IEA:TreeGrafter.
DR   FunFam; 2.60.120.260:FF:000118; Beta-mannosidase B; 1.
DR   FunFam; 3.20.20.80:FF:000050; Beta-mannosidase B; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR054593; Beta-mannosidase-like_N2.
DR   InterPro; IPR050887; Beta-mannosidase_GH2.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006102; Ig-like_GH2.
DR   InterPro; IPR041447; Mannosidase_ig.
DR   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF22666; Glyco_hydro_2_N2; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome.
FT   CHAIN           1..844
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000394655"
FT   ACT_SITE        432
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        723
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   844 AA;  97117 MW;  D24AE1CB82B9CEA0 CRC64;
     MAAFAQYTLS TGWYFKDRDE LASEAWMPVP VVPSVVHQDL QANGKLKNPY VGFNELDARW
     VNEKSWTYRK ILQKPTVLAG SRIVLAFDGL DTFAKVKLDN NIILESSNMF QAYRVDVTKA
     LDCGDEHVLE IEFDCAMLRA QELRKQDPNH NWASFNGDPA RMSVRKAQYH WGWDWGPVLM
     TAGIWRAVRL EVYSTRLADL WTEINLDPTH KTASISAFTE LESVDLDPSY KVKFTITLHG
     KQIAQAEATP QEGRAKVEFN IDQPCLWWPH GYGDSTLYEV SASLNADQLE LHRVTKKIGI
     RTAEVVQRPD KHGKSFFFRI NGVDIFCGGS CWIPADNLLP NISPQRYRKW IQLMVAGRQA
     MIRVWGGGCY EDDSFYEACD ELGVLVWQDF MFGCGNYPTW PELLKSIEQE AIYNVRRLRH
     HPSIVVYVGN NEDYQVQEQA GLEYNYEDKN PENWLKTNFP ARYIYEELLP SVVERCSPKT
     FYHPGSPWGD GKITSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHLSTI
     EYFVENEKDK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETYIYL TQVVQAETMM
     FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAYYAVA RVLNPVAVGV
     RREHHDWSIT HAQPPKTSKY ELWVVSSLQK PASGKVELRF LSVDTGREIR ERIVRENVDI
     VPNGTTNLIT DGLIDHTVDA EPHVLAARLW VDGEIVARDV DWPQPFKYLD FADRGLEVKR
     VSEASDQQVF QISTEKPVKC LVFEERDGVK FSDSAMDIVP GDVQTVKVTG LRADEKLKYK
     FLGQ
//