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Database: UniProt
Entry: A0A0S7C2J5_9BACT
LinkDB: A0A0S7C2J5_9BACT
Original site: A0A0S7C2J5_9BACT 
ID   A0A0S7C2J5_9BACT        Unreviewed;       865 AA.
AC   A0A0S7C2J5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=TBC1_121064 {ECO:0000313|EMBL:GAP45243.1};
OS   Lentimicrobium saccharophilum.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC   Lentimicrobium.
OX   NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP45243.1};
RN   [1] {ECO:0000313|EMBL:GAP45243.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBC1 {ECO:0000313|EMBL:GAP45243.1};
RA   Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA   Cruz R., Yamaguchi T., Sekiguchi Y.;
RT   "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT   Methanogenic Wastewater Treatment System.";
RL   Genome Announc. 3:e01168-15(2015).
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; DF968183; GAP45243.1; -; Genomic_DNA.
DR   RefSeq; WP_062045473.1; NZ_DF968183.1.
DR   AlphaFoldDB; A0A0S7C2J5; -.
DR   STRING; 1678841.TBC1_121064; -.
DR   PATRIC; fig|1678841.3.peg.3847; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000053091; 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:UP000053091};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          221..325
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          691..780
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          783..858
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   865 AA;  99290 MW;  9FB2DEC12FDE6132 CRC64;
     MKKLIVIFIL LSGLILKGSL SLMAQTSVEL NNDWEFRQAG TPQWYPAVVP GTVHTDLLAN
     GQIEDPYYRL NEKNLQWIDK VNWEYRTRFQ LDAAQLRAGS LMLRFHGLDT YATVMVNGAL
     LFKADNFHRT WEAEAGKHLK EGENEIFIRF ESPVMQGLLK QEALGYGLPA DNDQSENGGM
     GSVRISIFTR KPGYHFGWDW GPRLVTSGIW RPVELIINRT ARINDLFVRQ ESVTAKEARV
     KAGVEVSVQQ EGLYKLEILM DGQPVAAREI SMSPGIRHPD IDFIIKNPRL WWPNGAGGQP
     LYTVSAVLSH KGKELHTFNR QIGLRSLKHV RRPDAKGGGE SFHFEVNGRP VFAKGANYIP
     NDIFLPRVDS ARYEFIVKSA AEANINMLRV WGGGIYENDY FYDLCDRHGI MVWQDFMFAC
     AMYPGDKDFL DNVRLEAVDN IKRLRNHACI ALWCGNNEIE YAWAEGDFTR GWGWKEKYDK
     AQQREIWQSY DTLFHHILPA AVKQYAPDYT YWPSSPTQGG GVLANWSGNR GDVHYWGVWH
     GQEPISAFRN YKARFMSEYG FQSFPEFNSV KKYTLPEDWN IESPVMTSHQ RSGIGNLRIR
     QYMEQDYQIP DNFEHLLYVG QLLQADAIGM ALRTHRSDMP FCMGSLYWQL NDVWPVASWS
     GIDYYGKWKA MHYFVKDALK NQIIQVVVEN GKLLVYGVSD TDQKTPALLR LNLADFNGLS
     LWNRPYKVTL PANGATLLCS IDLKELPLNY QENKVFLTAT LMDGSRVIDQ EFAYFAKPKD
     LLLPDPGLKS RISDKGDHFV IEISTRNFCK NLMLVSDNTD VNFSDNFFDM QPGETRLITC
     SATMRWEDFE KGFRMLHLGQ TMRKQ
//
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