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Database: UniProt
Entry: R5UHE4_9BACE
LinkDB: R5UHE4_9BACE
Original site: R5UHE4_9BACE 
ID   R5UHE4_9BACE            Unreviewed;       870 AA.
AC   R5UHE4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=BN535_01329 {ECO:0000313|EMBL:CCZ75119.1};
OS   Bacteroides caccae CAG:21.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1263037 {ECO:0000313|EMBL:CCZ75119.1, ECO:0000313|Proteomes:UP000017990};
RN   [1] {ECO:0000313|EMBL:CCZ75119.1, ECO:0000313|Proteomes:UP000017990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:21 {ECO:0000313|Proteomes:UP000017990};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCZ75119.1}.
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DR   EMBL; CBAN010000207; CCZ75119.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5UHE4; -.
DR   Proteomes; UP000017990; 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}; 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_5004406031"
FT   DOMAIN          222..331
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          689..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;  100315 MW;  104B03166A40DB57 CRC64;
     MILNLTGKKA QIACGLLCCC SMAYAQSNDN SEVVLLHTGW EFSQAGTELW RTAEVPGTVH
     QDLIHHKLLP SPFYGMNEQK IQWVENEDWE YRTSFTVTME QLERDDAQLI FEGLDTYADV
     YLNGSLLLKS DNMFVGYSLP VKPQLRLGEN LLHIYFHSPI RQTLPQYASN GFNYPADNDH
     HEKHLSVFSR KAPYSYGWDW GIRMVTSGIW RPVKIRFYDA ASINDYHIKQ LSLTEHSAEL
     SNELEINNIL PQSIQAEIRI NYSFEKGEET VISRSVTLQP GLNSIHIPSE VLSPVRWMPN
     GWGKPALYDF SAQVVFDGKV VAEQSHRIGL RTVRLVNEKD ADGESFYFEV NGIPMFAKGA
     NYIPQDALLP SVTTERYQTL FRDIKEANMN VVRIWGGGTY EDDRFYDLAD ENGILVWQDF
     MFACTPYPSD PTFLKRVEEE ACYNIRRLRN HPSLAMWCGN NEILEALKYW GYQKKYTPEI
     YQEMMSGYDK LFRELLPAKV KELDADRFYI HSSPYLANWG RPESWGIGDS HNWGVWYGQK
     PFESLDTDLP RFMSEFGFQS FPEMKTIATF AAPGDYQIES EVMNAHQKSS IGNALIRTYM
     ERDYIVPEKF EDFVYVGLVL QGQGMRHGLE AHRRNRPYCM GTLYWQLNDS WPVVSWSSID
     YYGNWKALHY QAKRAFAPIH INPIQRNDSL CVYLLSDRLD TLEKMTLEMK VIDFEGKKIS
     KPMLLKSLSV PANTSQCVYR TKLDALLSST KRPLSEELLH CFMLLTLKDK SGHVVDETVY
     FFAKTKDLLL PETTISYKMK QTDGECELTL LSPVLAKDVF IEVPLQGARF SDNFFDLLPG
     ERKTILITSP QIKKGEELPL TVKHIRETYN
//
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