ID A0A1W9QS51_9BACT Unreviewed; 836 AA.
AC A0A1W9QS51;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=B6D61_11055 {ECO:0000313|EMBL:OQX75149.1};
OS Bacteroidetes bacterium 4484_249.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1970778 {ECO:0000313|EMBL:OQX75149.1, ECO:0000313|Proteomes:UP000192581};
RN [1] {ECO:0000313|Proteomes:UP000192581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) 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:OQX75149.1}.
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DR EMBL; NATE01000239; OQX75149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9QS51; -.
DR Proteomes; UP000192581; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 208..312
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 671..755
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 758..835
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 836 AA; 98220 MW; 762E287A6F2C5533 CRC64;
MHKLFKIPYL ILITFSLIAC IRQPVQNLEL NQNWQFKQTG TEDWLPANIP GCIHTALFDN
GIINDPFFGD NEQNLQWIGK TDWEYKSVFF ANDEFLESKH IELGFAGLDT YAKVYLNDSL
ILTANNMFRK WDVDCKNYLI TGKNELFVKF ESPVTKDSLK AASLPYKLPD NRAITRKAPY
QYGWDWGPKF VTQGIWKPVY LRTWNDARIK NIQVVQDSII NETAWLTSNF EIESSKEQDC
FLTLIDEDSR EIKNKIRVRL NKGTHLYPIT FSIENPQLWW TNGLGDQHLY KFKYRIQTNG
SIDEYSERIG IRTIELVQEP DSIGESFYFK LNGVPVFMKG ANYIPQDNFP SRVSEKKYRQ
TIQSAVDANM NMLRVWGGGF YENDIFYDLC DENGILVWQD FMFACNLYPG DEAFVENVKQ
EAIQNVKRLR NHPSLGLWCG NNEVDEAWFN WGWQKSLCYS KEDSIEVRSN YLKIFESLLP
EVISEFDQRR AYWPSSPKQG WGHEQALYSG DMHYWGVWWG EEPFEMYEEK IGRFMSEYGF
QGFPDLRTLD SCLLPEDKNL QSQALLNHQK HPRGMELIRT YMDREFDVPD KFEEYIYVSQ
LVQAYGIKTA IEAHRRAKPY CMGTLYWQLN DCWPVISWSS VDYYNRWKAL HYFVKNAYDE
FLISFEEKND SVKVFVVSDK LQSINAELEM KIIDFKGEEY WSDKQIITID SNSSNIYFKK
EINGFSKKDH LFLAKLVSNG KILASNIYYF LPVRDLQLPE PNIQKEIIKT EKGYQIVLKT
DKLAMNVFLS VDRDGFFSVN YFDLLPGEVK RITYIPDKEI DSFESEIKVV SIFDTL
//