ID W0ENX7_9BACT Unreviewed; 862 AA.
AC W0ENX7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=BARVI_06420 {ECO:0000313|EMBL:AHF12472.1};
OS Barnesiella viscericola DSM 18177.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF12472.1, ECO:0000313|Proteomes:UP000018901};
RN [1] {ECO:0000313|EMBL:AHF12472.1, ECO:0000313|Proteomes:UP000018901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007034; AHF12472.1; -; Genomic_DNA.
DR RefSeq; WP_025278416.1; NZ_CP007034.1.
DR AlphaFoldDB; W0ENX7; -.
DR STRING; 880074.BARVI_06420; -.
DR KEGG; bvs:BARVI_06420; -.
DR PATRIC; fig|880074.11.peg.1344; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_3_2_10; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000018901; Chromosome.
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; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 86..153
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 220..330
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 688..776
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 780..858
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 862 AA; 99859 MW; 9E6D44E12D5946B0 CRC64;
MNYRIVILLI IFLFFMKPSY SQHPVDDTRE IMLDRGWCFA PEGETQSYPA TVPGTVHADL
LRNGLLDDPF YGKNEEKVKW VEEKDWCYTT TFTVDRTTRE RYSHARLIFE GLDTFARIFL
NGKPVMQTDN MFVAWEKEVK PLLVVGENTL TVHFTSPLKA VEPIYRQTGI DYPADNDHST
PHLSVYARKA PYHYGWDWGI RLVGCGIWRP ARLLLYNGLR IDDAFTRTLH VDNDRAELST
DLLVVNENSR PVESVEVRFT LSHAGSEVTH WCREYTLQPG ENRITLPAEV AHPKLWQPNG
WGEAHLYDVE ITLAKGGKQL SSRRYQTGIR TIEFINEPDE LGRNFYFRVN GRPLFAKGTN
YIPQDIILPR VTPADYERLF RDMKESHMNM VRVWGGGVYE EELFYRLADR YGILVWQDFM
FACSAYPGDT AFLGNVAREA RYNIRRLRNH PSLALWCGNN EIYEGLKYWG WNHRYPAETF
EQMRRDYHTL FRDTLAECVR RYDPQRSYIH TSPDSANWGR PATQTQGDIH YWGIWYGREM
FDTMDTLSLR FVSEFGFESF PEMKTLLTFA GPDDLHIDSE VMTHRQKSSI GNELIQEYMQ
NYYRMPRTFD DFVYLGLLLQ GHGIAHGIET NRRQRPVCMG SLYWQLNDSW PAISWSAIDY
YKNKKALYYH ARDAFAPLML STTVQSDSLS VYTLSDRIDR IDQARITIGL QDFYGKELNT
VSFACDIEPN ATRHIATLSL ANLLGGWKKN EVLLTLRIEH QGETLFDGHK FLTVPKELNL
PRPHLTQTVE TTPLGVTLTL TTDCLAKDVF IEIPTQGADL SDNFFDLLPG ERKVVTIDGA
DITPEAVTRI RIRTLTDTYE GK
//
