ID   MANBB_THETO             Reviewed;         855 AA.
AC   I2C092;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Beta-mannosidase B;
DE            EC=3.2.1.25;
DE   AltName: Full=Mannanase B;
DE            Short=Mannase B;
GN   Name=man9; Synonyms=bmann9, mnd2I, mndB;
OS   Thermothelomyces thermophilus (Myceliophthora thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX   NCBI_TaxID=78579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=C1 / VKM F-3500D;
RX   PubMed=23240568; DOI=10.1134/s0006297912110090;
RA   Dotsenko G.S., Semenova M.V., Sinitsyna O.A., Hinz S.W., Wery J.,
RA   Zorov I.N., Kondratieva E.G., Sinitsyn A.P.;
RT   "Cloning, purification, and characterization of galactomannan-degrading
RT   enzymes from Myceliophthora thermophila.";
RL   Biochemistry (Mosc.) 77:1303-1311(2012).
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       Is also severely restricted by galactosyl substitutions at the +1
CC       subsite (By similarity). Has no activity against polymeric mannan.
CC       {ECO:0000250, ECO:0000269|PubMed:23240568}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.41 mM for p-nitrophenyl-beta-mannopyranoside
CC         {ECO:0000269|PubMed:23240568};
CC         Note=kcat is 15 sec(-1) with p-nitrophenyl-beta-mannopyranoside as
CC         substrate.;
CC       pH dependence:
CC         Optimum pH is 5.3. Active from pH 4.2 to 6.5.
CC         {ECO:0000269|PubMed:23240568};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:23240568};
CC   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23240568}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000305}.
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DR   EMBL; JQ437476; AFJ59925.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2C092; -.
DR   SMR; I2C092; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   CLAE; MND2I_MYCTH; -.
DR   PRIDE; I2C092; -.
DR   VEuPathDB; FungiDB:MYCTH_90655; -.
DR   UniPathway; UPA00280; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 2.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR041625; Beta-mannosidase_Ig.
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; PF17753; Ig_mannosidase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted.
FT   CHAIN           1..855
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000425599"
FT   ACT_SITE        430
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        693
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        730
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   855 AA;  97352 MW;  C90A3DB3050FEC9D CRC64;
     MAPRVVIPLD QNWEFRQADK PDSKFLPVSQ FPTNVHLDLQ HHGLIPDPFI GKNELLVQWV
     GEAQWTYRTV FAAPPVPEGA RAVIAFDGLD TFATVVLNGT TILESDNMFL PHRVEVTSVL
     KAEGNELVIT FDSAYLRGCK LVEQHPNHKW GCWNGDVSRL AVRKAQYHWG WDWGPTLLTC
     GPWRPVHLEI YESRLSDLYA ETVVDKSLKR ASVKVTAVAE RRADRVRFDI ALDGQQVATE
     TAELDATSGE ATVSFLIDSP ALWYPVRYGK QPLYDIRATL LAGDDEVDTL SKRIGLRRAE
     LIQRPLEGQP GTSFFFEVNN IRIYCGGSDW IPADNFIPRI SRRRYYDWVR LVAEGNQFMI
     RVWGGGIYEE QAFYDACDEL GILVWQDFMF GCGNYPAWPA LLESIRREAT ENVKRLRHHP
     SIVIWAGNNE DYQYQESEGL TYDYANKDAE SWLKTDFPAR YIYEKILADV CADLVPSTPY
     HPGSPWGAGL NTHDATVGDI HQWNVWHGTQ EKWQNFDRLV GRFVSEFGMQ AFPAVKTIDA
     YLPLGRDDPD RYPQSSTVDF HNKAEGHERR IALYLVENLR YAPDPLEHFV YCTQLMQGEC
     LASAYRLWKR EWRGPGREYC GGALVWQTND CWPVTSWSIV DYYLRPKLAY FTVKREMAPV
     SIGITRRTHL HPRDRHTRVN VDVKTQIEVW ASNLTLEDLT VDCVLKAWDV ESGEETFSET
     VAAALLLREN RSTEIAALDV PVRQKNVGEE GRIVVAAYLV DKEGRQMARY VNWPEPLKYV
     HLQKPRALRA QLTADYSAVE VSAEVPVKGV ALECEDDGVR FDDNLVDIVP GEVVTIGVSG
     AGKDTKIETR YLGMI