ID   MANBB_ASPOR             Reviewed;         844 AA.
AC   Q2TXB7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 3.
DT   22-FEB-2023, entry version 87.
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=AO090010000208;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   GENE MODEL REVISION.
RX   PubMed=24021641; DOI=10.1016/j.febslet.2013.08.029;
RA   Reddy S.K., Rosengren A., Klaubauf S., Kulkarni T., Karlsson E.N.,
RA   de Vries R.P., Stalbrand H.;
RT   "Phylogenetic analysis and substrate specificity of GH2 beta-mannosidases
RT   from Aspergillus species.";
RL   FEBS Lett. 587:3444-3449(2013).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE66106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007175; BAE66106.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001827239.2; XM_001827187.2.
DR   AlphaFoldDB; Q2TXB7; -.
DR   SMR; Q2TXB7; -.
DR   STRING; 510516.Q2TXB7; -.
DR   ChEMBL; CHEMBL4155; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   VEuPathDB; FungiDB:AO090010000208; -.
DR   OrthoDB; 2504097at2759; -.
DR   UniPathway; UPA00280; -.
DR   PRO; PR:Q2TXB7; -.
DR   Proteomes; UP000006564; Chromosome 8.
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; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome.
FT   CHAIN           1..844
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000394656"
FT   ACT_SITE        432
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   844 AA;  95960 MW;  4FBC82ACDB12075A CRC64;
     MAAFSQYPLS TGWSFKDSDD QSPEAWMPVP VVPSVAHQDL QANQKLKNPY IGFNELDARW
     VNDKSWTYRT VFQKPAVAAG SSIILAFDGL DTFATVKLDG SVILQSDNMF LAHRVDVTKA
     LEAEGDHVLE IDFDCAMRRA RELREKDTKH NWASFNGDPA RMAVRKAQYH WGWDWGPLLS
     TAGIWREVRL EVYSAKISDL WTEVELASDH QTARVSAFAE VDAADSVDSY KASFLLSLHG
     KEVAREVATL KDKVANVTFD 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 GVIDHKAQPE PHVLAARLWV DGEVTARDVD WPQPFKYLDL SDRGLEVNKV
     SESGNEQKLL ITAKKPVKCL VFEERDGIRV SDSAMDIVPG DGQTVTVTGL KAGDAPLKYK
     YLGQ
//