ID   MANBB_ASPTN             Reviewed;         843 AA.
AC   Q0CCA0;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   25-MAY-2022, entry version 74.
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=ATEG_08684;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU30816.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476606; EAU30816.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001217270.1; XM_001217269.1.
DR   AlphaFoldDB; Q0CCA0; -.
DR   SMR; Q0CCA0; -.
DR   STRING; 341663.Q0CCA0; -.
DR   EnsemblFungi; EAU30816; EAU30816; ATEG_08684.
DR   GeneID; 4323103; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   eggNOG; KOG3066; Eukaryota.
DR   OrthoDB; 517710at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000007963; 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..843
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000394657"
FT   ACT_SITE        430
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        721
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   843 AA;  96245 MW;  EE4DB1B4648C2506 CRC64;
     MASFFQQSLA TGWSFKDAED NSAEAWMPVA QVPSVVHQDL IANNKLQDPY VGFRELDARW
     VNEKSWTYRT VFQKPAVPAG SSVILAFDGL DTFAKVKLNG NVILESNNMF LAHRIDVTKA
     LGADGDHVLE IDFDCAMLRA RELRAKDPQH KWVGFNGDPA RMGVRKAQYH WGWDWGPVLM
     TAGIWRDVRL EVYTARVADL WTETDLAVDH HAAQISAFAQ VEGAISSSKV NFILSLHGQE
     VARAVAEPQD QVAKVAFDVQ QPSLWWPNGY GDPTLYEISA TLDQDGATVH QISKKIGIRT
     AEVVQRPDKH GKSFFFRING VDIFCGGSCW IPADNLLPSI SAERYRKWIE LMVHGRQVMI
     RVWGGGCYED DSFYQACDEL GVMVWQDFMF GCGNYPTWPE MLESVEKEAI YNVRRLRHHP
     SIVVYVGNNE DYQVQEQQGL TYNFEDKDPQ NWLKSDFPAR YIYEKILPEV VQRYSPSTFY
     HPGSPWGDGK ITSDPTVGDM HQWNVWHGTQ EKYQIFDTLG GRFNSEFGME AFPHMSTIEY
     FVENEKDKYP QSHVLDFHNK ADGHERRIAT YLVENLRTAT DLETYIYLTQ VVQAETMMFG
     YRGWRRQWGD ERHCGGALLW QLNDCWPTIS WAIVDYFLRP KPAFYAVARV LNPIAVGVRR
     EHHDWSVTHA QPPKKSKFEL WVASNLQKET RGMVELKFLS VDTGREIRER IVREDVIIVP
     NGTTDIIVDG VIDHQEYAEP HVLAARLWVD GKIVARDVDW PQPFKYLDLS GRGLEVKTVS
     TSDDQQTLLI SAQKPVKCLV FEERDGVRVS DSAMDIVPGD EQTVTITGLK ADAPPLKYKY
     LGQ