ID A0A0U2UXC7_9BACL Unreviewed; 841 AA.
AC A0A0U2UXC7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=IJ21_10080 {ECO:0000313|EMBL:ALS26417.1};
OS Paenibacillus sp. 32O-W.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS26417.1, ECO:0000313|Proteomes:UP000059673};
RN [1] {ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS26417.1, ECO:0000313|Proteomes:UP000059673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-W {ECO:0000313|EMBL:ALS26417.1,
RC ECO:0000313|Proteomes:UP000059673};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
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; CP013653; ALS26417.1; -; Genomic_DNA.
DR RefSeq; WP_062490923.1; NZ_CP013653.1.
DR AlphaFoldDB; A0A0U2UXC7; -.
DR STRING; 1695218.IJ21_10080; -.
DR KEGG; pow:IJ21_10080; -.
DR PATRIC; fig|1695218.3.peg.1049; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000059673; 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:UP000059673};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 34..138
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 673..759
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 762..829
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 841 AA; 95426 MW; 0D3212280467AC42 CRC64;
MEIASNWRIQ HFDVGQARPL EVASAGLDDR FWITAKVPGD VHSTLIERNI IENPYFGHND
AKCRWIETKE WWYRTQFDYE VDPDSGERHE LVFEGLDTFA TVYVNGLEVG KTSNMFTTYT
FDVTRIVRSG KNAIAVKFDP LSLHNRDKEL FQWSSYTKER PWIRKAAMNF GWDWGPRLVT
VGIWGKVRIE RRKTAKLDGV FARTLRADAE SADVRVDVDV KAYKRGAAAA VDVALKDRDG
AVVANAVATV AGGKVSVDLR VVAPRLWWTH DLGEPYLYEL DVVLRAEGKE VDRQTHAFGI
RTIELQLKDE QGRNSFTFVL NGVKLFAKGS NWIPADHFIG AIPNERYRDL IDLAVEGRMN
MLRVWAGGIY EKDAFYDECD RRGVLVWQDF AFANALFPDF NRDFMDSVRE EVACNVKRLR
NRASLALWCG NNEIDWLYDM KTAGGDITCP FYGESIYHEL IPDVLAELDD SRAYWPSSPY
GRANGMDDND PDVGDRHNWQ VWHGSVYPRK FGEAPILDYS IQGVTFKNYK KDFALFSSEF
GIHGSANRYT LEKYIPKGQF YWGSAEMAYR NKDTNHQKGI LLMEGFTGIP RDIEEYMNFS
MLTQAEGLKY GIEHYRRNKP RTSGALVWQL NDSWPGTSWS MIDYELLPKA AYFYGKKFFH
PVLLSVDHDP GEPLHVWAVN DTLEPLVGAV KLAVTDFAGN AVFETEFEAN VPANGAVRLG
TLSERDVLNG RAAEDVVVVL TAQGFEAPAN VVYLRDPKDL RLPAAELDVV VNEAESTVRV
TARGHLARFV KLDLPQGNVR FSDNFFDLLP GESKTVRVTD RTGEPVSLAR LSVSALNVKQ
R
//
