ID D7J1K6_9BACE Unreviewed; 870 AA.
AC D7J1K6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HMPREF0106_01307 {ECO:0000313|EMBL:EFI14457.1};
OS Bacteroides sp. D22.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=585544 {ECO:0000313|EMBL:EFI14457.1, ECO:0000313|Proteomes:UP000003817};
RN [1] {ECO:0000313|EMBL:EFI14457.1, ECO:0000313|Proteomes:UP000003817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D22 {ECO:0000313|EMBL:EFI14457.1,
RC ECO:0000313|Proteomes:UP000003817};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Sibley C., White A., Ambrose C.E., Allen-Vercoe E.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain D22.";
RL Submitted (MAR-2010) 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; GG774800; EFI14457.1; -; Genomic_DNA.
DR RefSeq; WP_009039375.1; NZ_GG774800.1.
DR AlphaFoldDB; D7J1K6; -.
DR HOGENOM; CLU_005015_3_2_10; -.
DR Proteomes; UP000003817; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}.
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..867
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 870 AA; 100106 MW; 781D442DDA0D8D5C CRC64;
MMIDLIGNKT QIACGLLCCC SMAYAQSNDN SEVVVLNAGW EFSQAGTELW RPAQVPGTVH
QDLIYHKQIP DPFYGINEQK IQWVENEDWE YRTAFTVTPE QLKRDDAQLV FEGLDTYADV
YLNGALLLKA DNMFVGYTIP VKSQLRLGEN LLHIYFHSPI RQTMPQYNSN GFNYPADNDH
HEKHVSVFSR KAPYSYGWDW GIRMVTSGIW RPVTIRFYDA ASISDYHVKQ LSLTDQQAKL
SNELEINNIL PQALQAEVRI NISFEGNTEK GISQTITLQP GINHISIPSE VLSPVRWMPN
GWGKPALYDF SAQIIVEDKV VAQQSHRIGL RTVRLVNEKD QDGESFYFEV NGVPMFAKGA
NYIPQDALLT NVTTERYQTL FRDIKEANMN VIRVWGGGTY EDDRFYDLAD ENGILIWQDF
MFACTPYPSD PIFLKRVEAE 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 LTNFAGEKAG
RTVVLPSLTL PANTSQCVYR TSLTTLFFPA KRPLADDLRH CFMQLTLKDK SGHTVAETVY
FFRKTKDLLL PKTTVSCKIK QKDGVCEFTL LSPALAKDVF IEIPLQGARF SDNFFDLLPG
ERKTVVITSP QIKKGEEIHL TIKHIRETYN
//
