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
//