ID   MANBB_ASPFN             Reviewed;         844 AA.
AC   B8NW36;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=AFLA_117830;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963485; EED45554.1; -; Genomic_DNA.
DR   RefSeq; XP_002384490.1; XM_002384449.1.
DR   AlphaFoldDB; B8NW36; -.
DR   SMR; B8NW36; -.
DR   STRING; 5059.CADAFLAP00012355; -.
DR   EnsemblFungi; EED45554; EED45554; AFLA_117830.
DR   VEuPathDB; FungiDB:AFLA_117830; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_1_0_1; -.
DR   OMA; MFANFDY; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000001875; 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..844
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000394653"
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;  96003 MW;  CB0DFBDDBC8C0ADF CRC64;
     MAAFSQYPLS TGWSFKDSDD QSPEAWMPVP VVPSVAHQDL QANQKLKNPY IGFNELDARW
     VNDKSWTYRT VFQKPAVAAG SSIILAFDGL DTFATVKLDG SVILQSDNMF LAHRVDVTKA
     LEAEGDHVLE IDFDCAMRRA RELREKDTKH NWASFNGDPA RMAVRKAQYH WGWDWGPLLS
     TAGIWREVRL EVYSAKISDL WTEVELASDH QTARVSAFTE VDAADSVDSY KASFLLSLHG
     KEVAREVATL KDKVAKVTFD VTQPSLWWPN GYGDPALYEI SVSLEKEDCE IHSVSKKIGI
     RTAELIQQPD RHGKSFFFRI NGVDVFCGGS CWIPADNLLP SITAERYRKW IELMVAGRQV
     MIRVWGGGCY EDDSFYQACD ELGVLVWQDF MFGCGNYPTW PELLESIEKE ANYNVRRLRH
     HPSIVVYVGN NEDYQVQESA GLVYDYEDKN PENWLKTDFP ARYIYEKLLP SVVEKLSPKT
     VYHPGSPWGD GKITSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
     EYFVENEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETYVYL TQVVQAETMM
     FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLKPIAVGV
     RREHHDWSVT HAQPPKTSKY ELWIASSLQK ETVGTIELRF LSVNTGLDVR APILRDNVKI
     VPNGTTNILE GVINHKAQPE PHVLAARLWV DGEVTARDVD WPQPFKYLDL SDRGLEVNKV
     SESGNEQKLL ITAKKPVKCL VFEERDGIRV SDSAMDIVPG DGQTVTVTGL KAGDAPLKYK
     YLGQ