ID   MANBB_ASPFC             Reviewed;         845 AA.
AC   B0YBU9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=AFUB_087900;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499601; EDP48080.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YBU9; -.
DR   SMR; B0YBU9; -.
DR   EnsemblFungi; EDP48080; EDP48080; AFUB_087900.
DR   VEuPathDB; FungiDB:AFUB_087900; -.
DR   HOGENOM; CLU_005015_1_0_1; -.
DR   PhylomeDB; B0YBU9; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR041447; Mannosidase_ig.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..845
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000394652"
FT   ACT_SITE        432
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        717
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        723
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   845 AA;  97047 MW;  B7D783CF578985E3 CRC64;
     MSKLQQFPLS KGWSFRDNEA TSEDAWMPVP VVPSVVHQDL QANNKLKDPY IGFNELEARW
     VNEKSWTYKT VFQKPAAPAG SCIVLAFDGL DTFAKVKLDG NVILENDNMF LARRVDVTKA
     LEAEGDHVLE IDFDCAFLRA KELRKQDPRH NWASFNGDPS RLSVRKAQYH WGWDWGPVLM
     TAGIWREVRL EVYSARVADL WTEVQLASDH QSAQVTAFVE VESVHSGSHR ACFTLSLHGQ
     EITREEIGVT ENGTAKATFD VKEPSLWWPH GYGDATLYEV SVSLVKEQEE LHRVSKKFGI
     RTAEVIQRPD KHGKSFFFRV NGVDIFCGGS CWIPADNLLP SITAERYRKW IELMVHGRQV
     MIRVWGGGIY EDYSFYDACD ELGVLVWQDF MFGCGNYPTW PNLLESIRKE SVYNVRRLRH
     HPSIVIWVGN NEDYQVQEQA GLTYNYEDKD PENWLKTDFP ARYIYEKLLP EVVQEYSPGT
     FYHPGSPWGD GKTTSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
     DYFVENEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETHIYL TQVVQAETMM
     FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLNPIAVGV
     RREHHDWSVT HAQPPKTSKF ELWVASSRQQ EIQGTVELRF LSVNTGLEVR ERIVHENVSI
     VPNGTTNLIV DGLIDHTVHS EPHVLAARIW VDGQLVARDV DWPQPFKYLD LSDRGLEVKK
     ISESEDEQTL LISTKKPVKC LVFEEREGVR ISDSAMDIVP GDDQRVTIKG LKPGDAPLKY
     KFLGQ