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Database: UniProt
Entry: H6NFB7_9BACL
LinkDB: H6NFB7_9BACL
Original site: H6NFB7_9BACL 
ID   H6NFB7_9BACL            Unreviewed;       864 AA.
AC   H6NFB7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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_2644 {ECO:0000313|EMBL:AFC29526.1};
OS   Paenibacillus mucilaginosus 3016.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC29526.1, ECO:0000313|Proteomes:UP000007523};
RN   [1] {ECO:0000313|EMBL:AFC29526.1, ECO:0000313|Proteomes:UP000007523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3016 {ECO:0000313|EMBL:AFC29526.1,
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; AFC29526.1; -; Genomic_DNA.
DR   RefSeq; WP_014369823.1; NC_016935.1.
DR   AlphaFoldDB; H6NFB7; -.
DR   STRING; 1116391.PM3016_2644; -.
DR   KEGG; pmq:PM3016_2644; -.
DR   HOGENOM; CLU_005015_3_2_9; -.
DR   Proteomes; UP000007523; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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; 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:AFC29526.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007523};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          201..303
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          671..760
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          763..845
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   864 AA;  98428 MW;  AFF3775CAE5D683C CRC64;
     MTITKPAYMT LSGWEFKACK DEHWLPAAVP GCVHTDLLRN GKIEDPFYGT NEKRLQWIDK
     EDWEYRTSFA ASPEQLSRAN VELVFDGLDT YADVTLNGQP ILSADNMFRS WRADVKELLQ
     EENTLRVRFR SPIQEDLPKL RALGYALPAA NDQSEAGGLG DEKVSVFARK APYHYGWDWG
     PRFVTSGIWK DVRLESWSGI RIRDFHIRQD QVTAEAARLT ALVEVETDEA WSGELRVSAE
     GRQWSRDVRL EAGSHTVQLA AELESPRLWW SRGLGAQELT DFRAELVSGG DVHAQETVTT
     GLRSAKLVRQ KDAHGTSFYI ELNGVPVFCK GANHIPNDSF VTEVTYERYR HEVASAAEAN
     MNMLRVWGGG IYEHDDFYRL CDEYGILVWQ DFMFACSMYP GDEAFLASVR SEAEENVKRL
     RRHPSVVLWC GNNEMDTAWS HYDENAGWGW KKKYSPELRE KIWRDYEAIF HEILPETIRA
     LSPETDYWPS SPMREVTGDA NQHATSSSPD GDIHYWGVWH NVEPFSNYKV HIGRFMSEYG
     FQSFPEEKTV ETYAAEEDMA LVSEVMLSHQ KNGRGNMLIK EYMDQYLSEP KDFRSFLYMS
     QVLQGEAMKT AIEAHRRRMG FTMGSLYWQM NDCWPVASWA GMDYLGRWKA LQYYAKRSFR
     DVMLSLDEND GKVEIHGVSD LQVPLTGTLE LRLLDFQGNV LRQWPASVTL AANAAGHLKS
     LAREEVLEGA DPASVVLTAR FEGSEGTTDL KEHYFLPVKD LRLEEPGVRI TRRTEGEQVL
     FTLEADRLAK QVWLSSEAEG HFTDNFFDLL PGSPVTVAFR KRSDGGEPFA AGDPGSMQVR
     SMYDFIKSSA GAQEADRQAE EQAL
//
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