GenomeNet

Database: UniProt
Entry: A0A089KUU9_9BACL
LinkDB: A0A089KUU9_9BACL
Original site: A0A089KUU9_9BACL 
ID   A0A089KUU9_9BACL        Unreviewed;       886 AA.
AC   A0A089KUU9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, 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=R70331_03880 {ECO:0000313|EMBL:AIQ50748.1};
OS   Paenibacillus sp. FSL R7-0331.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ50748.1, ECO:0000313|Proteomes:UP000029487};
RN   [1] {ECO:0000313|EMBL:AIQ50748.1, ECO:0000313|Proteomes:UP000029487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ50748.1,
RC   ECO:0000313|Proteomes:UP000029487};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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; CP009284; AIQ50748.1; -; Genomic_DNA.
DR   RefSeq; WP_042172966.1; NZ_CP009284.1.
DR   AlphaFoldDB; A0A089KUU9; -.
DR   STRING; 1536773.R70331_03880; -.
DR   KEGG; paee:R70331_03880; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_005015_3_2_9; -.
DR   Proteomes; UP000029487; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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; IPR006104; Glyco_hydro_2_N.
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; PF02837; Glyco_hydro_2_N; 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:UP000029487};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          62..127
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          199..301
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          670..759
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          763..822
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   886 AA;  99128 MW;  DEDF7291DE7E5E88 CRC64;
     MTHKQLVLDN WEFRASGDES WLPAAVPGTV HTDLLRSGLI DQPFYGTNEH RLQWIDKKDW
     EYRTTLQLDE GWESLAVTEL NFAGLDTYAD VYVNNVHALS ADNMFLAWTV DVKGLLRAGE
     NEILVKFRSV VTEDLPKLEQ LGYDLPAPND QSELGGLEEK RISVFARKAP YHYGWDWGPR
     FLTSGIWREA VLTGRNAAAI ADVYIRQDEV KEASARLTAI VEVDAPDSWA GTLRMTVEGQ
     EWTREVTLEP GKGVVELDLV IDQPRLWWCN GLGAPELTTF RAELLENGAV LADAEVRTGL
     REIKLIRQPD AKGASFKFEL NGVPVFAKGA NHIPNDSFIT EVSEERYRHE IASAAESNMN
     MLRVWGGGFY EEEVFYRLCD EYGLLVWQDF MFACSMYPGD EVFLENVRKE AEYNVRRLRN
     HPCIALWCGN NEIDSAWAQF EENKGWGWKE KLSGEVRETL WTAYEEIFHR ILPEAVTAHH
     PGIDYWPSSP LRELTNDADQ HSVRIAGDGD VHYWGVWHGI EPFENYNVKV GRFMSEYGFQ
     SFPELKSVLT YAEEKDMELE SEVMLAHQKN GRGNQIIKEY MDIYLPEAKD FKSFLYMSQI
     LQAEAMRMAI ESHRRNKPYC MGTLYWQMND CWPVASWAGM DYYGRWKALQ YTARRSFNDV
     MLSVEVTDGD NVQVHAVSDL PGALAGALVL RLHAFSGAVL KEWKQSVQLA ADSSAVVFTV
     PLAELMAGLD AKQVVLAASL LAEDGTLLER KEHYFAAAKE LTLEQPVLTV AEVPGSGGLS
     FTVSTDVLAR GVYLTAEQEG IFSDNYFDLL PGQVKTVQFL RRRADAAAGA GMETGAGAGV
     ETVETGAKAG AGAGVATGVK AGAGVPYFVP AAPQGLEVRS MADYVN
//
DBGET integrated database retrieval system