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Database: UniProt
Entry: H6NN10_9BACL
LinkDB: H6NN10_9BACL
Original site: H6NN10_9BACL 
ID   H6NN10_9BACL            Unreviewed;       838 AA.
AC   H6NN10;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE   AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614};
GN   ORFNames=PM3016_4278 {ECO:0000313|EMBL:AFC31050.1};
OS   Paenibacillus mucilaginosus 3016.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC31050.1, ECO:0000313|Proteomes:UP000007523};
RN   [1] {ECO:0000313|EMBL:AFC31050.1, ECO:0000313|Proteomes:UP000007523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3016 {ECO:0000313|EMBL:AFC31050.1,
RC   ECO:0000313|Proteomes:UP000007523};
RX   PubMed=22535950; DOI=10.1128/JB.00323-12;
RA   Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA   Shen D., Du B., Li J.;
RT   "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT   Functional as Microbial Fertilizer.";
RL   J. Bacteriol. 194:2777-2778(2012).
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         Evidence={ECO:0000256|ARBA:ARBA00000829};
CC   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC       {ECO:0000256|ARBA:ARBA00004740}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
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DR   EMBL; CP003235; AFC31050.1; -; Genomic_DNA.
DR   RefSeq; WP_014370855.1; NC_016935.1.
DR   AlphaFoldDB; H6NN10; -.
DR   STRING; 1116391.PM3016_4278; -.
DR   KEGG; pmq:PM3016_4278; -.
DR   HOGENOM; CLU_005015_3_2_9; -.
DR   Proteomes; UP000007523; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 3.
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; IPR006104; Glyco_hydro_2_N.
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; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AFC31050.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007523};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          67..148
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          204..301
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          671..755
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          762..832
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   838 AA;  96479 MW;  522B627DCC9EBE9A CRC64;
     MELSGLWRLQ HFETGQVRPL ETASVWLDDR FWMTAEVPGD VHSALIERGL IEHPYFGHQD
     LKCRWIEQKE WWYRRSFDYS LEAGGFEKHE LIFEGLDTFA TVYVNGLEIG TTNNMLMAHA
     FDVTRILRDG RNTIAVKFDP LHLHNRDKAL FEWSSYTKER PWLRKAAMNF GWDWGPRMVT
     TGIWGAVRLE RHRLARLDGV FARTAELAGT SAVVKVDVET TAFRRNAELR CEVRLLDADG
     RPAAQGTAER AGRREDFELE IAEAKLWWTH DLGEPYLYRL EVSLYADGEL VDRRQEPFGI
     RTIELQLKDE QGQHAFAFLL NGVKLFAKGA NWIPADHFIG SIPDQRYRDL IDLSVEANMN
     MLRVWGGGIY EKDVFYAECD RRGVLVWQDF AFANALFPDY NRDFMENVRR EVEYNIRRLR
     NHASLALWCG NNEIDWLYDM KSAGGDITGP FYGEAIYHEL IPQALENLDD SRAYWPSSPY
     GGSDANDPDV GDRHNWQVWH GSVYPRRHGE VPLLDYSVEG VTFKNYKQDF TLFSSEFGMH
     ASANRYTLEK NIPEGQFYWN STEMAYRNKD TNHKKGILLM EGYTGIPRDI EEYMNFSMLT
     QAEGLKYGIE HYRRNKHRTS GSLIWQLGDS WPGTSWSLID YELLPKASLH YAKKFYHPLL
     LSVDHDPGLP LHLWVVNDSL NPLDGEVRLE VYTFGGERLY SCRVEAHCGA NSAVRLLTLS
     EEDILQGADP ASVVVKVSTA DWDAPDNLVY LRDQKELQLL PVQLDVQRDE AAGTVRITAG
     GAHVRMVKLD LPQGNLRFSD NFFDLLAGES RTVQIRSAAG EAIRWDRLRV SALNQHRD
//
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