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
//