ID   MANBB_ASPCL             Reviewed;         845 AA.
AC   A1CGA8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 77.
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=ACLA_066240;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027053; EAW10988.1; -; Genomic_DNA.
DR   RefSeq; XP_001272414.1; XM_001272413.1.
DR   AlphaFoldDB; A1CGA8; -.
DR   SMR; A1CGA8; -.
DR   STRING; 344612.A1CGA8; -.
DR   GlyCosmos; A1CGA8; 2 sites, No reported glycans.
DR   EnsemblFungi; EAW10988; EAW10988; ACLA_066240.
DR   GeneID; 4704556; -.
DR   KEGG; act:ACLA_066240; -.
DR   VEuPathDB; FungiDB:ACLA_066240; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_1_0_1; -.
DR   OMA; MFANFDY; -.
DR   OrthoDB; 2504097at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000006701; 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; 2.60.120.260; 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; 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   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 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..845
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000394651"
FT   ACT_SITE        432
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
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;  96760 MW;  41EE1CB40C7719C7 CRC64;
     MAALQRFPLS KGWSFKDSED KSEDAWMPVP VVPSVVQQDL QANNKLKDPY IGFNELETRW
     VNEKSWTYKT TFQKPAVPAG SAIFLAFDGL DTFATVKLDG NVILESDNMF LAHRLDVTKA
     LEAEGDHSLE IDFDCAFLRA KELRKQDSKH NWASFNGDPS RLSVRKSQYH WGWDWGPVLM
     TAGIWREVRL EVYTARVADL WTDVQLASDH QNAQITAFAE VESVNSDAHK ARFTLSLHGQ
     ELGREEVSVS EDGSAKVSFD VKSPSLWWPH GYGDATLYEV SVSLVKDQDE VHQVSKKFGI
     RTAEVVQQPD KHGKSFFFRV NGVDIFCGGS CWIPADNYLP SVTADRYRKW IELMVHGRQV
     MIRVWGGGNY EDDSFYDACD ELGVLVWQDF MFGCGNYPTW PNLLESIRKE SVYNVRRLRH
     HPSIVVWVGN NEDYQVQESA GLTYDFEDKN PENWLKTDFP ARYIYEKILP EVVEEYSPST
     FYHPGSPWGD GKTTSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
     DYFVENEADK FPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETHVYL TQVVQAETMM
     FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLNPIAVGV
     RREHHDWSVT HAQPPKTSKF ELWVASSLQK EVQGTVELRF LSINTGLEVR ERIVHENVSI
     VPNGTTNLIV DGLIDYKVHP EPHVLAVRIW VNGELVARDV DWPQPFKYLD LSNRGLEVKL
     VSESENEQTL LLSAQKPVKC LVFEEREGVR ISDSAIDIVP GDEQRVTIKG MKPGDAPLKY
     KFLGQ
//