ID D0TRJ7_9BACE Unreviewed; 870 AA.
AC D0TRJ7;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=HMPREF0102_02691 {ECO:0000313|EMBL:EEZ03629.1};
OS Bacteroides sp. 2_1_22.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469588 {ECO:0000313|EMBL:EEZ03629.1, ECO:0000313|Proteomes:UP000005775};
RN [1] {ECO:0000313|EMBL:EEZ03629.1, ECO:0000313|Proteomes:UP000005775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_22 {ECO:0000313|EMBL:EEZ03629.1,
RC ECO:0000313|Proteomes:UP000005775};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA McDonald J., Allen-Vercoe E., Strauss J., Ambrose C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 2_1_22.";
RL Submitted (JUL-2009) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG705175; EEZ03629.1; -; Genomic_DNA.
DR RefSeq; WP_008770933.1; NZ_GG705175.1.
DR AlphaFoldDB; D0TRJ7; -.
DR HOGENOM; CLU_005015_3_2_10; -.
DR Proteomes; UP000005775; 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, ECO:0000313|EMBL:EEZ03629.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..870
FT /note="Beta-mannosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003017135"
FT DOMAIN 222..331
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 688..787
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 790..866
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 870 AA; 99997 MW; C368D047B48ADFB1 CRC64;
MMINLIGKKT QIACGLLCCC SMAYAQSNDN SEVVVLNTGW EFSQAGTELW RPAQVPGTVH
QDLIYHKQIP DPFYGINEQK IQWVENEDWE YRTAFTVTPE QLKRDDAQLV FEGLDTYADV
YLNGALLLKA DNMFVGYTIP VKSQLRLGEN LLHIYFHSPI RQTMPQYNSN GFNYPADNDH
HEKHVSVFSR KAPYSYGWDW GIRMVTSGIW RPVTIRFYDA ASISDYHVKQ LSLTDQLAKL
SNELEINNIL PQALQAEVRI NTSFEGNTEK GISQAITLQP GINHISIPSE VLSPVRWMPN
GWGKPALYDF SAQIIVEDKV VAQQSHRIGL RTVRLVNEKD QDGESFYFEV NGVPMFAKGA
NYIPQDALLT NVTTERYQTL FRDIKEANMN VIRVWGGGTY EDDRFYDLAD ENGILIWQDF
MFACTPYPSD PTFLKRVEAE ACYNIRRLRN HASLAMWCGN NEILEALKYW GFDKKFTPEI
YQEMFQGYDK LFHQLLPTKV KELDADRFYI HSSPYLANWG RPESWGIGDS HNWGVWYGQK
TFESLDTDLP RFMSEFGFQS FPEMKTIATF AAPEDYQIES EVMNAHQKSS IGNALIRTYM
ERDYIIPEKF EDFVYVGLVL QGHGIRHGLE AHRRNRPYCM GTLYWQLNDS WPVVSWSGID
YYGNWKALHY QAKRAFAPVH INPLLEGDNL CVYLLSDHLD TREKLTLEMR LTNFAGKKAG
RTVVLPSLTL PANTSQCVYR TSLTTLFFPA KRPLADDLRH CFMQLTLKDK SGHTVAETVH
FFRKTKDLLL PKTTVSCKIK QKDGVCELTL LSPCLAKDVF IEVPIQGARF SDNFFDLLPG
ERKTVVITSP QIKKGEELPL TIKHIRETYN
//
