ID   MANBB_NEOFI             Reviewed;         845 AA.
AC   A1D911;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=NFIA_114030;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027692; EAW20872.1; -; Genomic_DNA.
DR   RefSeq; XP_001262769.1; XM_001262768.1.
DR   AlphaFoldDB; A1D911; -.
DR   SMR; A1D911; -.
DR   STRING; 36630.CADNFIAP00010151; -.
DR   EnsemblFungi; EAW20872; EAW20872; NFIA_114030.
DR   GeneID; 4589289; -.
DR   KEGG; nfi:NFIA_114030; -.
DR   VEuPathDB; FungiDB:NFIA_114030; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_1_0_1; -.
DR   OMA; MFANFDY; -.
DR   OrthoDB; 517710at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000006702; 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; Reference proteome.
FT   CHAIN           1..845
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000394659"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  96945 MW;  278825BC6EFB8733 CRC64;
     MSKLQQFPLS KGWSFRDSED TSEDAWMPVP VVPSVVHQDL QANSKLKDPY IGFNELEARW
     VNEKSWTYKT VFQKPAAPAG SCIVLAFDGL DTFAKVKLDG NVILENDNMF LARRVDVTKA
     LEAEGDHVLE IDFDCAFLRA KELRKQDPKH NWASFNGDPS RLSVRKAQYH WGWDWGPVLM
     TAGIWRDVRL EVYSARVADL WTEVQLASDH QSAQVTAFAE VESVHSGSHR ACFTLSLHGQ
     EIAREEIGVT ENGTAKATFD VKEPSLWWPH GYGDATLYEV SVSLRKEQEE LHKVSKKFGI
     RTAEVVQRPD KHGKSFFFRV NGVDIFCGGS CWIPADNLLP SITAERYRKW IELMVHGRQV
     MIRVWGGGIY EDNSFYDACD ELGVLVWQDF MFGCGNYPTW PNLLESIRKE SVYNVRRLRH
     HPSIVIWVGN NEDYQVQEQA GLTYNYEDKD PESWLKTDFP ARYIYEKLLP EVVQEFSPST
     FYHPGSPWGD GKTTSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
     DYFVENEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETHIYL TQVVQAETMM
     FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLNPIAVGV
     RREHHDWSVT HAQPPKTSKF ELWVASSRQQ EVQGTVELRF LSVNTGLEVR ERIVHENVSI
     VPNGTTNLIV DGLIDHRVHS EPHVLAARIW VDGQLVARDV DWPQPFKYLD LSDRGLEIKK
     ISESEDEQTL LISTQKPVKC LVFEEREGVR ISDSAMDIVP GDDQRVTIKG LKPGDAPLKY
     KFLGQ