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Database: UniProt
Entry: A0A1I0IZV8_9BACL
LinkDB: A0A1I0IZV8_9BACL
Original site: A0A1I0IZV8_9BACL 
ID   A0A1I0IZV8_9BACL        Unreviewed;       846 AA.
AC   A0A1I0IZV8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=SAMN03159358_3171 {ECO:0000313|EMBL:SEU02908.1};
OS   Paenibacillus sp. NFR01.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1566279 {ECO:0000313|EMBL:SEU02908.1, ECO:0000313|Proteomes:UP000198735};
RN   [1] {ECO:0000313|EMBL:SEU02908.1, ECO:0000313|Proteomes:UP000198735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR01 {ECO:0000313|EMBL:SEU02908.1,
RC   ECO:0000313|Proteomes:UP000198735};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOIK01000002; SEU02908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0IZV8; -.
DR   STRING; 1566279.SAMN03159358_3171; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000198735; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198735};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          199..301
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          671..759
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          762..843
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   846 AA;  95477 MW;  6C6A62C990CD97D7 CRC64;
     MKQKHLVLAD WQFKACLEHE WLPAKVPGTV HTDLLANGKI TEPFYGTNEH DLQWIDKLDW
     EYRTTLELGE EWLQLPVAEL QFDGLDTYAD VFVNGVHALA ADNMFRAWTV DVKGLIKAGP
     NEILVKFRSP VNEDLPKLEQ LGYALPAPND QSELGGLEGQ QISVFARKAP YHYGWDWGPR
     FLTAGIWREA VLKGREAAEI SDLYIRQNEV KAQAARLTAV AEIDAPEAWE GTLRITADGQ
     EWTRAVSLQP GKQTVELDLV IDQPRLWWCR GLGEPELYEF SAALLAQETV VTEANVTTGL
     REIKLIRKPD ARGTSFYFEV NGVPVFAKGA NHIPNDSFIT EVTEERYRHE IESAALSGMN
     MLRVWGGGFY EEEVFYRLCD EYGLLVWQDF MFACSMYPGD AEFLESVRLE AEYNVRRLRN
     HPSIALWCGN NEIDSAWSHY EEDAGWGWKR NFSSELREKL WSDYQEIFHV ILPKAVAELH
     ADIAYWPSSP MRGVTGDINQ HATGITGEGD IHYWGVWHAI EPFENYNVKV GRFMSEYGFQ
     SFPELKSVLS YAEDADMELE SKVMLAHQKN GRGNLLIKEY MDIYLPKPKN FPSFLYMSHI
     LQADAIRMAI ESHRRNKPYC MGTLYWQMND CWPVASWAGM DYYGRWKALQ YTVKESFRDL
     LLSIDGTDGE NIHVHAVSDL RKPVEAELKL GLYSFGGELL KAIAQPVMLA ADSAAVVFSI
     SAAELLGSTA VDQAVLVATL EQGGEELARK LHYFAAPKEI RLATPELTIQ EVPGSGGLKY
     TVSSNVLARG VYLTAEDEGI FSDNFFDLLP GQPKTVSFLL RSGGEQHFVP AAPKGLAVSS
     MADYIE
//
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